CAZyme Information: MGYG000000227_04514

Basic Information

• Species: Bacillus sonorensis
• Lineage: Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; Bacillus sonorensis
• CAZyme ID: MGYG000000227_04514
• CAZy Family: GT2
• CAZyme Description: Phthiocerol synthesis polyketide synthase type I PpsD

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1861	MGYG000000227_13|CGC1	205109.67	5.3772

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000227	4782975	Isolate	China	Asia

• Gene Location: Start: 11368; End: 16953 Strand: +

Full Sequence      

MKETEIALEPIAIIGIGCRFPGGVNSPESYWKMLSEGIDAISEIPSDRWGVESYYDQDRF
KKGKTVSKWGGFLEKFDQFDVEFFGMSPREAVSLDPQQRLLLMASWEALEDGGQVLERLA
GSDTGVFIGGFTLDYKLLQFSESNRSLVEAHTATGSMMTLLSNRLSYAFDFRGPSISVDT
ACSSSLVAVHLACQSLWNHEASLALAGGVNVMLKPDYTIAESKAGMLSPDGRSKTFDSSA
NGYVRGEGVGVAVLKPLSKALKDGDRIYATIRATAVNQDGHSNGLTVPRGESQEELLRQA
YSKAGISPGRVQYMEAHGTGTPVGDPIEANALGSVLSMDRPEGDTCYIGSVKTNFGHTEA
AAGIAGLIKAALCLKHKAIPPHLHLNDPNPKILFEQLCLQVPRALTPWPDTNGPAVAGVN
SFGFGGTNAHVVLEEAPHVMPPVRTFTEKPYVFPASARSLEALKDVAAAYKDRLEQDDSA
CSTLHDLCYTAGVKRTHHSCRLAAVADSKEELINQLHAFLSEEPYPGLSVVQEVRHHDLV
KGATASLPLVFVYSGMGPQWWGMGRKLLETEPVFRQAVEQCDRLLQQYGGWSVLKEMLKN
EEQSLLEETEFAQPAIFALQVGLTALWKSWGIKPDAIVGHSAGEVAAAYASGALSIEQAV
RVIYHRSRLQQKTTGMGKLAAVGLSLEDVKPLLNGFEDSVSVAAVNSPGSLTLVGDPDSL
EKIIKPLEEQGVFCRYLRGKVPYHSHYMNPLKEELLKSLHDLSPHRTITPLYSTVTGKQI
AGRDLTADYWWENVRKPVQFASSIEEIIQSDYHTFLEISPHPVLAHSISETLKNANKKGT
VLASLRRFEDDSLKLFETLGGLYTAGYQIDWSIFYPDGGAFEKLPTYPWQLERYWQESEA
SAQDRLGHKVHPLLGKRLSSPLPTWESEVNMTHLSYLKDHLIQGNVVFPGAAYAEMGLAA
AKEIYQDSVSILTVDHVEFHKALFIPESETIMLRLMFHPKDGEFTIYSKFNNEQQDWKLN
ASGRLIVQTAQAPEPVDLDELKGRCLTEIGHAACYQQFRTLGLEYGQTFRGIEKLWQGSE
EALAKVSIPAELHGEISDYHYHPAVLDVCFQVLAAALPFAGEGGAETVYMPTGVESAYIP
EGAGGAFYPEVKPDMWIYARINSQNDSLLIGDIFLLDEQGNIILNIKNCHAKSLKEQTAD
QNTMKEQAFYDLQWETQQLEDAKRTESKTRHGKWLIFADRKSVGQSIAGILADRDEQFVM
VYPGEQFVKSAGEYRIQPSDPEDYRKLVLEAGGNGSHLKGIIHLWNLDAADMQDAAPETL
RQAELLGSISVLHVVQALAGFSWKTAPRLWVMTRNAQNIVNDDGAIHVLQAPVWGLGKVI
NQLEHRDIKGGLIDLDPLPDAGEAERIWKEIASRSDEDQIAFRNGLRYVARLIERKDLHL
PADPVFRFDGSYLITGGFGALGLLVARWLAERGARHLILMGRKPLPERHAWNDIRPDHPM
ADRVKAVKELEKLGAAVHVAAVDVNDEQSLSDYLKAYKQESWPEIRGVIHSAGAALPQIL
LQVQQKDFSRVMEPKTIGAWNLHKQFEDHPLDFFVLFSSIASLVASTGQGSYSAANAFMD
GLAHYRRAKGLPALSINWGPWGQAGMATQLDLLQYFVHRGFYPMTNDQGLEAFGHLLGQK
VAQAAVVGADWPLVVKANFGGNQPSMLSVVTAEEKTADKDPDAAAGQSGDPLTALLALKD
PDARRSFIISHLQDIAAGVLSLNRSKLSPEQSLGNYGLDSMMAIELKNRIDDHFHINIAI
VDLLKGPSIVRLSEQISSRLTDIPAEELNEETAEVLQELENLSKDELQALLHEISAGEEK
E

Enzyme Prediction     

No EC number prediction in MGYG000000227_04514.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00833	PKS	0.0	9	433	1	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.
COG3321	PksD	0.0	9	1096	4	1053	Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism].
smart00825	PKS_KS	4.22e-172	11	435	1	298	Beta-ketoacyl synthase. The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.
cd08955	KR_2_FAS_SDR_x	6.26e-130	1298	1691	8	376	beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x). Ketoreductase, a module of the multidomain polyketide synthase, has 2 subdomains, each corresponding to a short-chain dehydrogenases/reductase (SDR) family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerizes but is composed of 2 subdomains, each resembling an SDR monomer. In some instances, as in porcine FAS, an enoyl reductase (a Rossman fold NAD binding domain of the MDR family) module is inserted between the sub-domains. The active site resembles that of typical SDRs, except that the usual positions of the catalytic asparagine and tyrosine are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular polyketide synthases are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) fatty acid synthase. In some instances, such as porcine FAS , an enoyl reductase module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER). Polyketide syntheses also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes the KR domain of the Lyngbya majuscule Jam J, -K, and #L which are encoded on the jam gene cluster and are involved in the synthesis of the Jamaicamides (neurotoxins); Lyngbya majuscule Jam P belongs to a different KR_FAS_SDR_x subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
smart00827	PKS_AT	3.46e-127	552	847	1	297	Acyl transferase domain in polyketide synthase (PKS) enzymes.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BAZ00088.1	3.35e-144	11	918	1214	2111
BAZ75991.1	3.35e-144	11	918	1214	2111
BAY30132.1	5.98e-144	11	903	1216	2103
BAY90071.1	2.52e-143	11	903	1213	2100
AFY93865.1	1.25e-121	3	903	953	1869

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4MZ0_A	5.04e-229	3	895	34	935	ChainA, CurL [Moorena producens 3L],4MZ0_B Chain B, CurL [Moorena producens 3L]
7M7E_A	6.77e-211	2	1827	26	1490	ChainA, 6-deoxyerythronolide-B synthase EryA2, modules 3 and 4,EryAI,6-deoxyerythronolide-B synthase EryA3, modules 5 and 6 chimera [Saccharopolyspora erythraea],7M7E_B Chain B, 6-deoxyerythronolide-B synthase EryA2, modules 3 and 4,EryAI,6-deoxyerythronolide-B synthase EryA3, modules 5 and 6 chimera [Saccharopolyspora erythraea]
7M7I_A	4.53e-206	2	1861	26	1521	ChainA, EryAI [Saccharopolyspora erythraea],7M7I_B Chain B, EryAI [Saccharopolyspora erythraea]
7M7J_A	1.21e-205	2	1861	26	1521	ChainA, EryAI [Saccharopolyspora erythraea],7M7J_B Chain B, EryAI [Saccharopolyspora erythraea]
7M7F_A	7.00e-204	2	1827	26	1497	ChainA, EryAI,6-deoxyerythronolide-B synthase EryA3, modules 5 and 6 chimera [Saccharopolyspora erythraea],7M7F_B Chain B, EryAI,6-deoxyerythronolide-B synthase EryA3, modules 5 and 6 chimera [Saccharopolyspora erythraea],7M7G_A Chain A, EryAI,6-deoxyerythronolide-B synthase EryA3, modules 5 and 6 chimera [Saccharopolyspora erythraea],7M7G_B Chain B, EryAI,6-deoxyerythronolide-B synthase EryA3, modules 5 and 6 chimera [Saccharopolyspora erythraea],7M7H_A Chain A, EryAI,6-deoxyerythronolide-B synthase EryA3, modules 5 and 6 chimera [Saccharopolyspora erythraea],7M7H_B Chain B, EryAI,6-deoxyerythronolide-B synthase EryA3, modules 5 and 6 chimera [Saccharopolyspora erythraea]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P9WQE2	1.89e-282	4	1820	32	1785	Phenolphthiocerol/phthiocerol polyketide synthase subunit C OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=ppsD PE=3 SV=1
Q7TXL7	1.89e-282	4	1820	32	1785	Phenolphthiocerol/phthiocerol polyketide synthase subunit C OS=Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) OX=233413 GN=ppsD PE=1 SV=1
P9WQE3	1.89e-282	4	1820	32	1785	Phenolphthiocerol/phthiocerol polyketide synthase subunit D OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=ppsD PE=1 SV=1
P9WQE7	9.93e-242	9	1820	102	1836	Phenolphthiocerol/phthiocerol polyketide synthase subunit A OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=ppsA PE=1 SV=1
P9WQE6	1.38e-241	9	1820	102	1836	Phenolphthiocerol/phthiocerol polyketide synthase subunit A OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=ppsA PE=3 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
0.565366	0.010167	0.423759	0.000097	0.000070	0.000547

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000227_04514.