CAZyme Information: MGYG000001436_01819

Basic Information

• Species: Paenibacillus_F sp000411255
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_F; Paenibacillus_F sp000411255
• CAZyme ID: MGYG000001436_01819
• CAZy Family: GT2
• CAZyme Description: D-alanine--poly(phosphoribitol) ligase subunit 1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2220		246514.41	5.1536

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001436	6290841	Isolate	not provided	not provided

• Gene Location: Start: 2046428; End: 2053090 Strand: -

Full Sequence      

MLESFNDTTRAYSSDDMLTIHGLLERQAARTPDRPAVVSGKRQWSYRELNERANRLARTL
QAKGVGRESLVGILAERSPEMIAAALAVMKAGGAYVPIDPDYPEARIRYMLEDAGVSLLL
AQSRLRNRVAFGGEWLLLDDPQSFSGDGSNLADSVKAGDLAYVIYTSGTTGQPKGVLVEH
AGVCNYKLFYDEALKVCEQDRVLQFASFSFDAACSEMTMSLFGGAALYVPDASVIADYRL
LEQYVRDNGITVATLPPTYAAYLNPAHMPSLTRLITAGSASSPELARRWSGFVRYFNNYG
PTEDSICSTAWPYSTLDDTAKTVPIGRPIANHQVYILGADQSIMPVGIPGELCVSGIGLA
RGYLNRPELTAEKFVPVPFAPERRMYRTGDLARWLPDGNLEYMGRIDDQVKIRGYRIELG
DVLTQLNRLPSVREALIVAHADKAGAVELCAYFTAEKTWSVGELRQALLQELPAYMVPTY
AVQLAAFPLTPNGKIDRSALPAPDVDLAERSGEGTEAPRTALEARLTELWREVLGAEAVG
IRDHFFEIGGHSLRAAALTARIHQALQVEVPMRMVFEHPTVESLAQAMEGLQPNPYAGIP
AAGEQESYPVSSAQKRLYVLSQLETDGFGYNMPGVLRLDGEPDVARLEQAFRALIRRHEA
LRTAFTLRDGVPVQRIAPKEAPPEFTLPRIRVRGEAEARQAARAFIRPFDLEQAPLLRAA
LVDEGANRHRLLVDMHHIVSDGVSTAILLEELSRLYNGEGESEVLPELRIQYKDYAVWQQ
SEAGNERVRAQEAYWLERLKGELPVLDLPADRTRPAVFSYTGGVVRFTLGAERTSGLKRL
ALRTGATLYMVLLAAYSTLLSKYSGQEEVIVGTPVAGRPHAELERVMGMFVNTLALRTYP
SADKPFEAYVREVKELALEAYAHQDYPFEELVEKLNVRRDMSRNPLFDTMFAWQGEGGAV
PELAGLKASAEEADYRSAKFDLTLDAEEQGDELLFRLEYCDALYERETAERMAGHFVQLI
DAALADPQAKLSALSMLTPEERSGLLDHFANAGLEAGRGMAGVFHEAFTAQAARIPAQTA
VVYRDERLSYRELDERSNRLARKLQACGVGRETLVGILAGRSPLLLVAVLAVWKAGGAYV
PLDPDYPPERIRFMLEDSGASVLLTEAALEPRLEVILADNEAGTAVLALDDEAIYDDQGS
AVAVINRPGDLAYLIYTSGTTGRPKGVMIEHQSLMNTAEGYRREYRLDQFPVRLLQLASF
SFDVFVGDLARTLYNGGMMVICPKDDRLDPTRLHHWIQAYDVNVFESTPALIVPFMQYVT
DRGLDIGAMKLLITSSDSCNVADYRALQERFGAQIRIINAYGVTEAAIDSSYYDQPLKRL
PDAGHVPIGRPLLNARFYILDSQLRPVPVGVLGELCIGGAGVARGYWNRPDLTGEKFVPN
PFVPGERLYRTGDSARWLPDGDVDFIGRLDDQVKIRGHRIELGEVEARLMKQSFILEAVV
AGKESIHGQKQLCAYIVANRIISPGELRKELAEELPDYMIPSAWVQLDRLPLTPNGKVDR
KALPAPNREENPDAAYAAPHTKLQQTLTELWQKLLGAETIGIDDNFFERGGHSLTAIQLI
AQAQTAGIPIGIHHIFQGQTIRKLSALLEQPAEVNIQPAETVQESERRLKKAFGLRSRFV
TEESEDGLRVTLNMEPCHGVKVSELLAFIRAELASNLHPHYLTTGESAADSVAEGRDAAI
EQLVPLAISEKSPAEIKRRVKRELSRIQVLHEALQSDIIVGAVECRYALAPAQEYHLERP
QCSGTVIRLDVLGLDADLLSEAVRSLLARHSLLRSVLVRDGQDWVWEQRAVPEQLTLPAV
DLSDYSKADQQELLVRLLPKLFTEPYRLSGRLLYRMALVRLNWREHRLLLPCSHLIYDET
SGSILESELLEAYRRLASRSEEDLTAWPQLRTSGAEAGTAGMPADGYPAYVAQVRKGPQH
IGDHELVRLFHLEDFDAGLELVNESIQALLGQGYTKAELRFDMSGFKELASVNWGVWSLQ
LAGRFFRRYLQVAAVPVWMTHYGRHYENNAFFKTVGECIDQIPLLLTGTEADSESVRDKL
QTAAARNINFLNLVYNEQTASNYPKSRRLLQKGLDSTAIVYNYLGESEDAAYLFEEAEAA
GGESHAQQPPVLHFTSQHQGSVWQISVTLPYREEKETIMEMLEKELQTLAASLRSVKAHV

Enzyme Prediction     

No EC number prediction in MGYG000001436_01819.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd19531	LCL_NRPS-like	0.0	608	1027	2	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.
cd17650	A_NRPS_PpsD_like	0.0	1076	1563	1	447	similar to adenylation domain of plipastatin synthase (PpsD). This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. 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 bond 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.
PRK12316	PRK12316	0.0	599	2171	40	1471	peptide synthase; Provisional
cd17655	A_NRPS_Bac	0.0	1066	1566	1	489	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.
PRK12467	PRK12467	0.0	601	1679	2639	3706	peptide synthase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QND46664.1	0.0	1	1650	994	2664
ACX49739.1	5.46e-213	2	1312	447	1818
BAY90071.1	3.89e-193	467	1650	2069	3285
BAY30132.1	1.41e-189	479	1650	2102	3296
BAZ00088.1	1.45e-188	492	1650	2116	3294

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MFZ_A	0.0	19	1645	206	1794	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	3.25e-317	19	1567	206	1716	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]
6P1J_A	1.53e-210	606	1563	4	964	Thestructure of condensation and adenylation domains of teixobactin-producing nonribosomal peptide synthetase Txo2 serine module [Eleftheria terrae],6P1J_B The structure of condensation and adenylation domains of teixobactin-producing nonribosomal peptide synthetase Txo2 serine module [Eleftheria terrae]
5U89_A	1.24e-201	1	1046	10	1071	Crystalstructure of a cross-module fragment from the dimodular NRPS DhbF [Geobacillus sp. Y4.1MC1]
6MFW_A	6.27e-189	19	1030	206	1196	Crystalstructure of a 4-domain construct 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	14	1654	460	2079	Plipastatin synthase subunit C OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsC PE=1 SV=2
Q04747	0.0	19	1650	1497	3106	Surfactin synthase subunit 2 OS=Bacillus subtilis (strain 168) OX=224308 GN=srfAB PE=1 SV=3
P94459	0.0	19	1698	1495	3167	Plipastatin synthase subunit D OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsD PE=1 SV=2
Q70LM4	0.0	1	1654	448	2099	Linear gramicidin synthase subunit D OS=Brevibacillus parabrevis OX=54914 GN=lgrD PE=1 SV=1
P39846	0.0	1	1646	455	2074	Plipastatin synthase subunit B OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsB 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
1.000042	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001436_01819.