CAZyme Information: MGYG000002886_02575

Basic Information

• Species: Stenotrophomonas maltophilia
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia
• CAZyme ID: MGYG000002886_02575
• CAZy Family: GT2
• CAZyme Description: Enterobactin synthase component F

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1025	MGYG000002886_132|CGC1	110658.89	6.1797

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002886	4276654	MAG	United States	North America

• Gene Location: Start: 32; End: 3109 Strand: +

Full Sequence      

MGRLGNASARVPAMVMNVLPLRVAAGEGSVEAFTRGLGRKLSQGRKHGRYRGEQLRRDLG
LVGAQQRLHGPLVNVQPFYKPLALAGVQATLEVLCTGPVDDLTLGFRGDGQSLLDLEIEA
NPALYSREDVEAHAARLLHFVSAALQADDIAAVPLATPEEAQQVLQEFNATAHALPETTL
VELLQQGMDRDPHAPALVFGDAALDYATLEARSFALAAQLRAMDVGPGSVVAVALPRSLE
LVIALVAVLRAGAAYLPLDLAHPDERLARILASAQPVCVLAAAEDSARMAGVPMLAPEQW
TALSFAAPWADPAPSDAAYVIYTSGSTGEPKGVVIEHRAIVNRLLWMREHYGIRADDRVL
QKTPATFDVSVWEFFLPLLCGATLMVAGPDAHRDPTELARLIRGHGITTAHFVPSMLDAF
LAAPASAGLQLRRVFTSGEALDASLRDRFHGRVQAELHNLYGPTEAAVDVSYWPASAQDR
SRPVPIGFPVWNTRLYVLDARMQPVPIGVAGDLYLGGVQLARGYLGRDDLTTERFLADPF
LPGERIYRTGDVARWRRDGAVEYLGRSDHQVKLRGLRIELGEIEAALRELPGMERVEVLL
RQDAPGDARLVAYVPTALADAVMLRSHLATRVPDYMVPSAFVGVDHWPVTANGKLDRNAL
PKPPQLEVAGLAPRTPLEQELALLFAQALGREAPVAVDADFFSLGGDSLSAVHLLLAIEQ
RWRCDLGLGALFAQPTVAALAVRIAEPPALADHALGPVIALAATDAAGPTPLFVLHPAGG
IAWNYRTLARALQPARPVYGLQSPALDARQPLPSSIEAMANDYVQRVVALQPKGPVHLLG
WSVGGILAQAMAVRLHEIGREVGELVLLDAYPSECWRAEPEPDAIAALRALLAIAGHDPD
AHPELDSRERILAFLRRGGSALGSLPDVVLDGVVRAVTGTNRLIREHVHQPFDGTLVHVR
AGRDHQARPQLQSALWRTHARKVQALELPFLHAELTGRDAVAQLAPWLSARLRQWDEQEE
IATCS

Enzyme Prediction     

No EC number prediction in MGYG000002886_02575.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd17646	A_NRPS_AB3403-like	0.0	181	660	1	488	Peptide Synthetase. 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.
cd05930	A_NRPS	0.0	192	660	1	444	The adenylation domain of nonribosomal peptide synthetases (NRPS). 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.
PRK12467	PRK12467	0.0	125	872	3039	3795	peptide synthase; Provisional
PRK10252	entF	0.0	1	1014	279	1296	enterobactin non-ribosomal peptide synthetase EntF.
cd17651	A_NRPS_VisG_like	6.11e-170	189	661	6	491	similar to adenylation domain of virginiamycin S synthetase. This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QND46664.1	7.47e-136	16	869	1903	2784
BAY30132.1	4.10e-128	114	869	2641	3415
BAY90071.1	7.49e-128	114	869	2630	3404
BAZ75991.1	6.18e-127	114	869	2639	3413
BAZ00088.1	6.18e-127	114	869	2639	3413

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5JA1_A	1.49e-206	1	1014	278	1295	EntF,a Terminal Nonribosomal Peptide Synthetase Module Bound to the MbtH-Like Protein YbdZ [Escherichia coli K-12],5JA2_A EntF, a Terminal Nonribosomal Peptide Synthetase Module Bound to the non-Native MbtH-Like Protein PA2412 [Escherichia coli K-12],5T3D_A Crystal structure of holo-EntF a nonribosomal peptide synthetase in the thioester-forming conformation [Escherichia coli K-12]
6P1J_A	1.98e-154	101	660	386	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	1.04e-143	156	792	2	664	Crystalstructure of a cross-module fragment from the dimodular NRPS DhbF [Geobacillus sp. Y4.1MC1]
6EA3_B	1.13e-135	165	663	39	552	Thermobifidafusca FscH adenylation domain complexed with MbtH-like protein FscK and Ser-AMP [Thermobifida fusca YX]
6N8E_A	6.64e-125	1	937	301	1237	Crystalstructure of holo-ObiF1, a five domain nonribosomal peptide synthetase from Burkholderia diffusa [Burkholderia diffusa]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q8XBV9	1.31e-207	1	1014	276	1293	Enterobactin synthase component F OS=Escherichia coli O157:H7 OX=83334 GN=entF PE=3 SV=1
P11454	7.76e-206	1	1014	276	1293	Enterobactin synthase component F OS=Escherichia coli (strain K12) OX=83333 GN=entF PE=1 SV=3
P29698	3.66e-194	1	1014	276	1281	Enterobactin synthase component F OS=Shigella flexneri OX=623 GN=entF PE=3 SV=2
P45745	4.46e-169	64	1014	1387	2375	Dimodular nonribosomal peptide synthase OS=Bacillus subtilis (strain 168) OX=224308 GN=dhbF PE=1 SV=4
Q0E7C4	4.77e-162	163	874	1968	2704	Vanchrobactin synthase VabF OS=Vibrio anguillarum OX=55601 GN=vabF 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
1.000066	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002886_02575.