CAZyme Information: MGYG000001321_02457

Basic Information

• Species: Desulfovibrio piger
• Lineage: Bacteria; Desulfobacterota; Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae; Desulfovibrio; Desulfovibrio piger
• CAZyme ID: MGYG000001321_02457
• CAZy Family: GT2
• CAZyme Description: D-alanine--poly(phosphoribitol) ligase subunit 1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2965	MGYG000001321_47|CGC2	320778.84	5.4244

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001321	2826258	Isolate	not provided	not provided

• Gene Location: Start: 254540; End: 263437 Strand: -

Full Sequence      

MATQCPGTTCKTEDDAFVSIIDGIRKKALSHPDSPALSFLPDGKAENAELCSYSRLDMRA
RAIAAAIQATGQGDGRPVLLMLPPGLEFIAAFFGCLYARAIAVPMTPPGLARMARTFNRL
ARIVEDSGSRVFITSARLRKAVEELAERVHFADSIRIICLDETDDALSRSWQELPLTAHT
PGWLQYTSGSTSSPKGVIITHGNIMANLDSIAGHMRLRENIPTVSWLPPFHDMGLVGGIL
TPLHLGCLCVTMPPMAFLRQPLCWLRAVTHYRAQLTGGPNFAYDLCCDRIPEDRLRELDL
SSLSVCYCGSEPIRLKTIRRFLERFSSAGLDPASFYPCYGLAENTLFTTGCWKNDGDFAV
FLDKQEYAAGRIRFLQEQHADAMPLLSCGTAGRNNDVRIVDPQTCREVEEKELGEIWIRG
TCVSPGYWEQPEATKTVLHAVLAGSGEGPFLRTGDMGFMSGGHLFVSGRCKEMIILNGRN
FFPQDLEECVLQNVPGLEQNGAAAFGIDSDAGERLVMVFETRLPATAHEATLAAIRRSLS
EEFDISPCAVVLCKRHGVPKTTSGKIQQSLCRHLYLHGELPVLAEWREEPRAGAPAWNRP
PQEQDAPASREAWQNWLRDGLSARLGLSPDSVGLHTPFSSLGMGSATAVALTGELQQACG
RPLPATLFYDHADIASLASFMAGDLSDEAPLPAHCAGQQAVAIIGMACRLPGADSPEALE
ALLFGGKDAITRRDPAHRDGTAAPEDGDRAVWGGFLDDISAFDAALFGISPREAVEIDPQ
QRLLLEVSWQALERAGIAPDSLRRSRTGVFTGISSSDYENRRLQCGQSLNAYVGTGNAHS
IAANRLSYFYGFEGPSMAVDSACSSSLLALHLACRSLRDGECETALACGVNILAGSEGQD
IFTDAHLMAPDGRCKTFSADADGYVRAEGCVVLVLKTLERALNDQDPILGIVRGSAVNQD
GRSNGLTAPSRRAQARLLREALHNAGLTAADIDGIEAHGTGTPLGDPIEFGAISDVYSGS
READRPLLVSSIKTNVGHLEAAAGLAGVCRVLISLQAAAIPPHLHLKRLNPEIRPDGIPA
AIPVATTPWPRTPGRPRRAGVSSFGFGGTNVHVILEEAPLTDAPSGTLPGPLPVLPLAAA
SEGQLRELAADYREYLARAPEREMADACLTCGTGRASLPCRAALAGPDIVRGLEQLASGM
PVPFMGHVPDSAPHRPVVFFLDSMTGCPDASLPDVPPLASARTALLEQLPSGTETDGQAR
AFLDLMATAEAWRRMLGEPAAILCTPATVSVAACLAGHLDPEEGLALYRALENDGAPIPQ
FKVRAPEAGTVSLPLFNLGSSRLISAEEARDPAFWRAYAPTTGAPEEAHAIAQARRLAPS
ADILAMRPGDLPDGNTADTPLLLPAFAPDAAATPQHMAAVLACCWTRGTNVRWAAVHAGS
AARRIPLPTYPFARERFWFGGTDMTDAPAALPARRSPAPLEIPDVSCVMQETARADRLDD
AELLALLSREARAVLRLPENVSLSPETPLVRAGFDSLLFMELAQRLSRRLGMTLPPALLM
ETATLAALRERLCLQGQTAPAPQEMTDIVARPEDRHLPFPLTDVQHAYWIGRDGSMTLGG
VSCSNYVEADFTGLDVPRLEKALDALVRRHDMLRCVITPDGRQRVLPAVPACRIPLEDLS
ALAEEEKEHVLRQKREQLSHKVLPTDKAPLLEITASRLDAATVRLHVKLDLLVADAYSFG
ILMQDLAAWYADPGMEKSPLALSFRDCVLAAEAEKDTPAWQADREYWLQRLPFLPAGPEL
PLARTPQSLGTPRFHRRTAMLDAARWARLKEMGRAQGLTPSGLLLAAFSLVLSRWTAQPH
FCLMLTTFDRRYRHEEMGAVVGDFTRLLLLEVQREKGATFLEHATALGRQLIRDMGHSRF
SAVDVLRELAKDHGEDMTSSRSAVVFTSALPLSGDDPFAAADGLGAKLAYAVSQTPQVWL
DHQVCEYRGQLVYTWDAVEDLFPSGMLDAMFTVYGDFLTALCEDAALWQQPVPLHRLPAS
QADVRHAANATEAAIPPRTLFAPFLDHASRDGAPAAVIGEGVSLSRAEAESISRLLGNGL
RSRGLRPGEIVAVMMEKGWEQVVAVMGILRAGGAYLPVSPSLPDKRIAYMFKDAGVRFCF
VQPGLEARAEACGSEAVPVLRAFPEQAAPAAAPLPDTDVSPEGLAYVIYTSGSTGLPKGV
MVSHAAAHNTLADLGQRLDLGPRDRVIALASLSFDLSVFDLFGVTAAGGAVVIPAPGQER
DPAAWCRLMREQGVTVWNSTPSLMQLLLDYLDDHPEDRPERLRLALLSGDWIPLAMPDRM
HALWPDMTVAALGGATEAAIWSNIQIVDRIPAEWHSIPYGRPLANQGYLVLDQDLSPCPD
LVAGDLYITGAGLARGYLNDPSKTAAAFFRHPRSGQALYRTGDLGRYWPDGTLEFLGRKD
SQVKINGFRIELGEVERALNALPGVGNAAVIALRSDKGDRLAGFVSPAPQAVMPAPSDES
PEAREARYRSMRDVGITLVDDVERLAYKQAGHNLRKDLDSLPRIGLATEDEATSLSLFSR
RISSRRFTEAPMEREAFERLLGCLRGLDIPQWPVVRHRYGSAGWTYAVQVYVLVRPGRIR
ELDGGCYYYHPLENALVRMADAPEDAATVFPGHNADIFSHSAFALFLVADMEAIRPLYGD
RSEEFVLIEAGLMSQLLEETAMELRAGLCQIGALDFDRLRGSFSLGAGQRYLHCLTGGAV
TREPGWDFTRALAESLPHQAAAGGLSPEDLQGLLRQWLPDYMVPQTLTVIDAIPLTANGK
VDRRQLAALGAGPAAGPACVHPEGETEEQLTAIIRDMLGKETVSVLDNFFDLGATSLQLV
LFQRRISELLHRQVAITDIFAHPNIRDLAAFLAPQGGEDSAEDAMSMAGRRARLRRQMRR
PGPAHAVTPRNLGPQDSLPGTESNS

Enzyme Prediction     

No EC number prediction in MGYG000001321_02457.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00833	PKS	0.0	701	1115	3	421	polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.
cd19535	Cyc_NRPS	0.0	1598	2024	1	422	Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family. Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. 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). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, 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 Cyc-domains. 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.
cd12114	A_NRPS_TlmIV_like	0.0	2076	2516	5	438	The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes. 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 TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
cd05931	FAAL	0.0	28	576	3	546	Fatty acyl-AMP ligase (FAAL). FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
COG3321	PksD	2.12e-173	700	1480	5	893	Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BAY90071.1	1.95e-168	32	2569	592	3207
BAZ00088.1	2.80e-166	52	2569	606	3216
BAZ75991.1	2.80e-166	52	2569	606	3216
BAY30132.1	3.69e-166	32	2569	593	3218
AFY93865.1	6.35e-87	52	1575	366	1980

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7EMY_A	5.98e-187	1522	2915	32	1424	ChainA, Dihydroaeruginoic acid synthetase [Pseudomonas aeruginosa PAO1],7EMY_B Chain B, Dihydroaeruginoic acid synthetase [Pseudomonas aeruginosa PAO1],7EN1_A Chain A, Dihydroaeruginoic acid synthetase [Pseudomonas aeruginosa PAO1],7EN1_B Chain B, Dihydroaeruginoic acid synthetase [Pseudomonas aeruginosa PAO1],7EN2_A Chain A, Dihydroaeruginoic acid synthetase [Pseudomonas aeruginosa PAO1],7EN2_B Chain B, Dihydroaeruginoic acid synthetase [Pseudomonas aeruginosa PAO1]
7LY7_A	4.44e-176	1590	2505	2	885	ChainA, BmdB, Bacillamide NRPS [Thermoactinomyces vulgaris]
7LY4_E	4.57e-176	1590	2505	2	885	ChainE, BmdB, bacillamide NRPS [Thermoactinomyces vulgaris]
6LTA_A	1.50e-171	1576	2546	32	1003	ChainA, Nonribosomal peptide synthetase [Streptomyces sp. Sp080513GE-23],6LTB_A Chain A, Nonribosomal peptide synthetase [Streptomyces sp. Sp080513GE-23],6LTC_A Chain A, Nonribosomal peptide synthetase [Streptomyces sp. Sp080513GE-23],6LTD_A Chain A, Nonribosomal peptide synthetase [Streptomyces sp. Sp080513GE-23],6LTD_B Chain B, Nonribosomal peptide synthetase [Streptomyces sp. Sp080513GE-23]
4MZ0_A	1.23e-129	698	1196	38	555	ChainA, CurL [Moorena producens 3L],4MZ0_B Chain B, CurL [Moorena producens 3L]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P48633	2.88e-187	1516	2912	27	1474	High-molecular-weight protein 2 OS=Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081) OX=393305 GN=irp2 PE=3 SV=1
A0A0H2ZGB9	2.21e-186	1522	2915	32	1424	Pyochelin synthase PchE OS=Pseudomonas aeruginosa (strain UCBPP-PA14) OX=208963 GN=pchE PE=1 SV=1
G3XCV2	2.21e-186	1522	2915	32	1424	Pyochelin synthase PchE OS=Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) OX=208964 GN=pchE PE=1 SV=1
Q9HWG4	1.60e-182	1590	2888	60	1454	Pyochelin synthase PchF OS=Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) OX=208964 GN=pchF PE=2 SV=1
A0A0H2ZGJ4	1.32e-181	1590	2888	60	1454	Pyochelin synthase PchF OS=Pseudomonas aeruginosa (strain UCBPP-PA14) OX=208963 GN=pchF 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
1.000047	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001321_02457.