CAZyme Information: MGYG000003072_02304

Basic Information

• Species: Paenibacillus amylolyticus
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus amylolyticus
• CAZyme ID: MGYG000003072_02304
• CAZy Family: GT2
• CAZyme Description: D-alanine--poly(phosphoribitol) ligase subunit 1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
5009	MGYG000003072_8|CGC1	563776.16	4.7119

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003072	7042795	MAG	China	Asia

• Gene Location: Start: 15931; End: 30960 Strand: +

Full Sequence      

MLRHMLCRIAFTDEERGTIQMAFEKETLFWNEKFGSDDYTLTRLPYNKAPNSLVPNVKTV
GGSLSEEAAQRVLQMSKGAPLAAFMILLAGVQALLHKYTGASDILVGMPVVPKKGETRRS
VNHTVILKNSLSVGATFKTLLSELRTSLPEAIQHQHIPFLKMTEKLDLQYAEGIPFVHTL
VSLKELHLDEIGQNVVTDCSFEFSLAGGTIQLALSYNEHLYDSEFMNRVVGHLNRLLSVG
LHELELDIVRADMLSEDEKYQLIQSFNDTEKDYPRDRTIHQLVEEQAKRVPEATAVVFEG
QRLSYAELNERANQLARTLRSVGVLPNQLVGLMVRRSLETVIGILAVLKAGGAYVPIDPE
YPEERIRYILENSNAQLLLTQRELLQQVPFEGTVLALDDKQAYSDDGSNLEAASGPHDLA
YVIYTSGTTGKPKGVMLEHRGLVSLKLMFADRLGITEHDRIVQFASLSFDASCWEVFKAL
YFGAALYIPTAETILDTRLFESYMNEHAITAAILPPTYSAHLNPDRLPSLTKLVTGGSAV
SAEFVQQWKEKVHYFNAYGPTEASIVTTLWDADEQQPERRVIPIGRPLSNHRIFILDAHL
QLVPPGVDGELCVAGVGLARGYLNQPELTAEKFVEHPFAPGERLYRTGDLARWLPDGNME
YLGRIDHQVKIRGFRIEVGEIEEQLLKIDSVQETIVIAREGKSGQELCAYLVASLPLTLG
ELRSALAQKLPNYMIPAHFVQLPQMPLTPNDKIDRKALPAPEGNALTGGEYVAPRNEAER
TLADVWQAVLNADRVGVTDHFFELGGDSIKSIQVSSRLHQAGYKLEIRDLFKYPTISQLS
LHVIPIGRTIDQGEITGETALTPIQHWFFESSFADPHHFNQSVMLYRKERFDEEMVRQVL
QKLAEHHDALRMVFRKTEQGFSARNRAIQEDEMFTLDVFDFKDAENPTQTVEAKATDIQA
GIDLENGPLMKAGLFQCADGDHLLLGVHHAVVDGVSWRILMEDFALGYEQTGKSEEIRFP
AKTDAYRTWSEQLAAYAQSPEMEKERAYWQAVDQMEVPAVPKDMEADVTTQQDSESLFVR
LAPEETELLLKRVHRAFNTEMNDILVTALGIALRKWTGHERVRINLEGHGRESIGTDIDI
TRTVGWFTTKFPVVLEPETDRDLTYQIKQVKENLRRIPNKGLGYGICRYLSKSEEGLVWG
AEPEINFNYLGQFDDDVNQGEIGISSYSSGSPASDRQARSFVLDINGMVLDGALSLDLSY
SRKQYRKETMEAFAQRLEQSLRELITHCAGKENTEMTPSDVQFKGLTITELEQIAQRSSH
LGEIENIYSLTPMQKGMWFHSALDRQTAAYFEQTRFTMRGALDVQLFERSWMELAKRHLV
LRANFVNGPAGEPLQIIYRDKPVGFEYEELLHLQVHEKQAYLDEKAEEDKLRGFDMEHDA
LVRFTILRTEEQSYHVLWSFQHILMDGWCLAQLTQELFEIYSALTSGKQPAGGKGSDYGD
YIEWLEKQDDQAASGYWTAFLAGYEGQTVLPGQKEPAPSGRFTADHVTAELGKDLSKRMD
RVAKQHLVTVNTLLQAVWGVMLQKYNGTNDAVFGSVVAGRPAEIPGIESMIGLFINTVPV
RVNSEVDTVFADLMAKLQERALDSGRYDYYPLYEIQARSVQKQNLINHIIAFENYPVDEQ
MEQAGDQQHGGLTIADVQMEEQTNYNFNVTVMPGTEIEIRFDFNAEVFDKDSIERLKGHL
VHLLEQVTDNPEITVGELELVTEAEKADLLGRFNDTTTEFPRGQTLIQLFEEQAEYIPDA
TAISMNEQEMTYRELNERVNRLARTLRSHGISQGRLVAIMAERSIEMVIGILAAHKAGAA
YVPIDPEYPEERIRFLIEDSGAQVMLTQSRLRERLAGLDSVILLDDESFYHEDGTNLNQG
IEATDLACVIYTSGTTGKPKGNLVSHRNIVRVVQNTNYIDITNRDHVLQLSSYSFDGAIF
DIFGALTNGARLVLVPRETLLEIGLLADLIQRQRISVMFITTAFFNVLVDVNVNCFRDVR
AILFGGERVSVGHVRKALAHLGAGRLNHVYGPTESTIFTTYLPVDFVDESALTVPIGRPI
SNTTVYIVDSRNKLLPIGVVGELCVGGEGLVRGYNNRPELTAEKFVHNPFTSGERMYRTG
DLAKWLPDGTIEYVGRTDDQVKIRGFRIELGEIETQLQKVEGIRKTTVFARENVSGEKQL
CAYYEADCELPAAELKSVLSQELPAYMIPTYLIQLERLPLTTNGKVDRRSLPAPEESLQP
GEGHTPPRTPLEANLAEIWKSVLGLEHIGVHDNFFDLGGHSLRATTLVSKVHQELNVELP
LRDVFRYSTIEQMALALSRIEEHSFSSIPLVGARAYYPLSSAQKRLFILNQLEGAEQSYN
MPGVLLLEGSIDHSLLEKAFRGLIQRHETLRTGFEVVQGEAVQRIYESVDFSVVCRHANE
EEAPAVVQAFIRPFDLAKPPLLRAELVELAADRYLLMFDMHHIISDGVSMDVFVEELVRL
YGGESLEPLHIQYKDYAVWQQSDEQKVQLKREEAYWLDRYRGELPVLEMPTDYPRPAVQS
YEGHTLTSFVDEATNEGLKQLAAQRGTTLYMVLLAAYTVLLHKYTGQDDLIVGTSIAGRT
HGDTQPLIGMFVNTLAIRNYPASEKTFLSYLEEVKETTLGAYEHQNYPFEELVDKVQVSR
DLSRNPLFDTMFSLQNLEESEFELEGLKLSPYPSEYGMAKFDLSVDVTEENGGLECNFEF
ATALYKESTIRRLSIHFGHLLAAIVSHPNAKIAELDLLTEEEKEQILGAFNPAQPEAAPA
AAFHRLFEEQAERTPEAEAVVYENVRLTYAELNVRANGLAATLRASGIGREEIVGILAER
SVDLLVAVLAVWKAGGAYVPLDPDYPADRVRFMLEDSGAKVLLTQTLLRERAEAWLSQEE
LALAKVLYLDDEMSYSENRENAPLGSSMVSGKVSGELTGAVNSDDPSHLKVAGLDSFHEA
RPEDLAYVIYTSGTTGKPKGVMIEHRSLVNTAAGYRREYRLDQFPVRLLQLASFSFDVFV
GDIARTLYNGGTMVIVPKDDRIDPSRLHHWIEREQVTIFESTPALIVPFMEYVHEQGLEL
SGMELLITSSDSCSVADYRTLQERFGSSFRIINAYGVTEAAIDSSFYEEELAKLPQTGHV
PIGKAWLNAKFYIVDAHLNPVPVGVLGELVIGGVGVARGYLNRPELTEEKFVDSPFTAGE
RLYRTGDLARWMEDGNVDFIGRIDNQAKIRGYRIETGEIESQLLRVEGVREAVVLVRSDA
NGQKALCAYYTPDTGVELVVNDLRRALAQELPGYMIPSYFVELERLPLTPNGKIDRKVLP
APEGEAGSGTEYVAPRNELETKLAAIWQEVLGLAKEIGVHDNFFDIGGHSLRATTLVSKI
HKELNVDLPLRDVFRHSTIESMATAISRLDQQIFVSIPVTDGREVYPQSFAQKRLFILNQ
LEVAELSYNMPEAMLLEGALDRARFEETFRKLVARHEMLRTGFEMVDGEASQRVYQDVNF
AVEFYQADEQEVEAVVHGFVRPFDLAKPPLLRVGLVELAPERHILMYDMHHIISDGVSME
IFVEEFVRLYGGEQLEPLRIQYKDYTVWQHSQEQQERLQHQGAYWLDMFQGELPVLEMPT
DYPRPAVQSYEGQTLEFSFDASKTGGLKQLASETGTTLFMVLLAAYNVLLHKYSGQEDVI
VGTPIAGRNHGDVQPLIGIFLNTLAIRSYPSSEKTFLSYLNEVKETTLRAFEHQNYPFEQ
LVDKVQVTRDLSRNPLFDTMFTMQNTENEQFELEGLRLIPYPSVLDTAKFDISLDVGEEN
GGLDYSFEYATALYKRETIERLAKHYEQLLLTIVNRPDAKIAELNLLTAEEKEQVLSAFN
PAQLEAAPAATFHRLFEKQAERTPEAEAVVYENKRLTYVELNERANRLALTLRANGIGRE
SIVGILAERSVDLLVAVLAVWKAGGAYVPLDPDYPADRVRFMLEDSGAKVLLTQTPLRER
AEAWLREEELALMSVLYLDDEASYSEDRANARMCFDQGSNMASSQVSGKLTGAVNGADRN
HLDVVDDVDVDVVGMDSFHEARPEDLAYVIYTSGTTGKPKGVMIEHRNLVNTAAGYRREY
RLDQFPVRLLQLASFSFDVFVGDIARTLYNGGTMVIVPKDDRIDPSRLHYWIVRERVTIF
ESTPALIVPFMEYVHEQGLEFSGMELLITSSDSCSVADYRTLQERFGSSFRIINAYGVTE
AAIDSSFYDEALTKLPHTGHVPIGKAWLNAKFHIVDAHLNPVPVGVLGELVIGGVGVARG
YLNQPELTEEKFVDSPFAVGERLYRTGDLARWMEDGNVDFIGRIDNQAKIRGYRIETGEI
ESQLLRVEGVREAVVLVGSDANGQKVLCAYYTPDTGAKLAVNDLRSALAQELPGYMIPSY
FVELERLPLTPNGKIDRRALPAPEGEAGSGTEYVAPRNELEMKLAVIWQEVLGLAKQIGV
HDNFFDIGGHSLRATSLAGKVFKELNVNLPLRDVFRHSTIAAMAKAIARMERREHEAIPQ
AEQREYYPLSSAQKRLFIQHTLDGADQLYNMPELVQVEGEFDLDRLEAALRKLITRHESL
RTGFEMMKGEVVQRIYPQVDFAIEYHQADTEDSDQIEQIVRNFVRPFDLGQPPLLRAGVI
ELEPHLRILLFDMHHIVSDGVSMAIVMEEFSSFYAGEQLPPLRIHYKDYAVWQQSKAHRE
RIGRQEAYWLQTFEGELPTADLPMDYERSAVRSYEGAHVEFDVEASLSAQLRELAAECES
TLFMVLLAAYTVLLSKYSGQEDLIVGTPVAGRTNADLERVIGMFVNTLALRNRPSGDKTF
LSYLEEVKETALGAFENQDYPFEDLVERLNVKREPGRFPLFDAVFDLQNIEERDAELEGV
SLKNYELDPLEEAKFDLTLFMYENEGALSGGFFYATKLFKETMIRTLTEDYLRVLSQIAE
NPQLELSRIECHKPAAGAKSAVDTIEFAF

Enzyme Prediction     

No EC number prediction in MGYG000003072_02304.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd19531	LCL_NRPS-like	0.0	3465	3877	1	427	LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity. LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
cd17655	A_NRPS_Bac	0.0	1788	2275	1	490	bacitracin synthetase and related proteins. This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
cd19531	LCL_NRPS-like	0.0	2376	2788	1	427	LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity. LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
cd12117	A_NRPS_Srf_like	0.0	1788	2271	1	483	The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C). The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
cd17655	A_NRPS_Bac	0.0	281	762	1	490	bacitracin synthetase and related proteins. This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QND46664.1	0.0	1862	4600	1	2709
BAY90071.1	0.0	1505	4544	306	3280
BAY30132.1	2.74e-314	1498	4547	300	3294
BAZ00088.1	1.78e-311	1498	4547	300	3292
BAZ75991.1	1.78e-311	1498	4547	300	3292

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MFZ_A	0.0	1779	3447	200	1798	Crystalstructure of dimodular LgrA in a condensation state [Brevibacillus parabrevis],6MFZ_B Crystal structure of dimodular LgrA in a condensation state [Brevibacillus parabrevis]
6MFY_A	0.0	1779	3368	200	1721	Crystalstructure of a 5-domain construct of LgrA in the substrate donation state [Brevibacillus parabrevis],6MG0_A Crystal structure of a 5-domain construct of LgrA in the thiolation state [Brevibacillus parabrevis],6MG0_B Crystal structure of a 5-domain construct of LgrA in the thiolation state [Brevibacillus parabrevis]
2VSQ_A	4.04e-265	1323	2350	8	1032	Structureof surfactin A synthetase C (SrfA-C), a nonribosomal peptide synthetase termination module [Bacillus subtilis]
6MFW_A	3.92e-206	1779	2802	200	1205	Crystalstructure of a 4-domain construct of LgrA in the substrate donation state [Brevibacillus parabrevis]
6MFX_A	1.80e-205	1779	2802	200	1205	Crystalstructure of a 4-domain construct of a mutant of LgrA in the substrate donation state [Brevibacillus parabrevis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P39847	0.0	1323	3918	6	2554	Plipastatin synthase subunit C OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsC PE=1 SV=2
Q5AUZ6	0.0	76	4868	1114	5995	Nonribosomal peptide synthase atnA OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=atnA PE=2 SV=1
Q04747	0.0	1324	4767	6	3328	Surfactin synthase subunit 2 OS=Bacillus subtilis (strain 168) OX=224308 GN=srfAB PE=1 SV=3
P94459	0.0	1324	4870	7	3449	Plipastatin synthase subunit D OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsD PE=1 SV=2
Q70LM4	0.0	24	3457	1244	4683	Linear gramicidin synthase subunit D OS=Brevibacillus parabrevis OX=54914 GN=lgrD PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000044	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003072_02304.