CAZyme Information: MGYG000002518_00496

Basic Information

• Species: Serratia surfactantfaciens
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Serratia; Serratia surfactantfaciens
• CAZyme ID: MGYG000002518_00496
• CAZy Family: GT2
• CAZyme Description: D-alanine--poly(phosphoribitol) ligase subunit 1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2376	MGYG000002518_11|CGC2	266605.34	5.7503

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002518	5076569	Isolate	India	Asia

• Gene Location: Start: 254912; End: 262042 Strand: +

Full Sequence      

MKILNILVNHTVEPLRSHIVRYLLDAGHFVYLIGLSDAERTRWTGSQHNLFCYSDVGDQR
IDYELCLEESASVRGPIVRLAVFADRQNVLFQIHAEEDGNIRALAQRELPWREARRALSQ
TVLGELFIDGVVMLSREAKDLDIALPEGPNRVTDWLVAQQRVQQEQRALENDEPRYGCFN
LRDEVSAVNDAAVVQRTIDGVAQPQQALLLAFQLQFLLNARRPGLYALQLQDRQRSSKVL
RLLNGSETYAELSPWLVRVLQGDSANPFYESHHDGRFLSVVGVDVIMDEGDVDAAAAPIR
IVWNSTRCTLSLQFYGENPFFDVVAANIDEFMAALATFMRNEGDIDALTGVSENSYQRYY
AKINATQCEYPRQTIVGMFEQQARALNDHPAVITKNETLSYRMLQQQASRLADYLQRQYG
VAAGDKIALMMPREAELAVCLMAVLKLGCAYIPIDKNAPVVRTYSILADAQPALIIGAHA
QSAGSLPQGLNYLDWREYAASPFAGADGCNEFPSQAEASALAYIIYTSGTTGKPKGVAVE
HRSFVNIASDISRRMSVTHQDRFLAITTLAFDISTLEIFMPLMFGATVVLTDQKTLLANN
DLPHFIASHSVSLMQGTPSFWHQVAQQYAETTLPVRALCGGEAVPHAVARWLSENTERAW
NVYGPTETTVWSTADELLPGGDSVTIGRPLANTQCFILDERRRLLPPGVIGEMYISGLGV
ARGYYGNARQTQASFLPNICSSTPSAWFGRIMYKTGDRVRCLPDGRFEYLSRWDNQIKLR
GHRIELGEIESVLRTYPGMQQVVVNLQPAKEEQQAFLVAYYQAKSPVARQQLQDYLVTLL
PDYMLPSAYMYLPEIPLNMNGKVDRKALPQVQAQDKAHYVAPGNEFQRCLCQLFQDVLGS
ESGRVGITDDFFALGGNSLSAIRLVNRINGTLQCDLKVKDIFERKNVARLAPLVAAGRGS
FLYQDYQIAQCDETHLYHPFPLNNVQQSYYLGRMKSFDLSEVSTHIYNEFVFDHIDHDKL
ERAYNQLIARHPALRTVFEEGEQRFLSAAAHYKIGYHPLRNEDELLALRAEYSHKVYKPD
CYPLFDIFLSEFQGKYLLHVSFDAIIIDMTSFEILFGEWIALYHDENLALPPLDISYRDY
QLQYERLRGGALFERAQQYWLQKIDDYTLEVGLPLAAHPARIDKPSFRRLSATIPMSSWQ
KIVDKCQRFNISPTALILELYSRTLCYWSGQESLCLNLTLFNRLPLHSQVEKIIGDFTVL
SLFNYQRQNGVAMSEQLSAIHRTLLNDVDNNLFDGIDVQRLLKQRRNLPANTVIAPVVLT
SVLGMNNKASMFELPLNEGYRGVQYAISQTSQVWLDHKAYENDEGFVAEWDYVEQLFDEK
TIKAMHEGYCSLIRWVAEHDWETMSFPQPELPAEHAEAVMRWNATQSKVSEQTLHGLFLS
SLETPQTAERIAVIETEGERHFTYARLEQDSNTLGRALLRHTKGEKGRITAILLEKGYAQ
AVSTLGIMRSGGAYLPLHIEWPWERIRDILQQARCDILLLSAQQRHDLAHELSALPSDIT
ILVFDEIVASAQERASTAVAWPIVRAEDLAYIIFTSGSTGKPKGVAIDHQGAVNTILAVN
QRWSVGREDRILALSELSFDLSVYDLFGLLAVGGGVVIPSQRETKAPQAWVAALRRHDVT
LWNSVPQLAGLLVDEVEPATQALTRLRLFLLSGDWLPLNLPHRLKTQSPDGKMVSLGGAT
EGSIWSIWHEIDRVDARWKSIPYGVAMPNQQMWVLDEWGNACPFGVTGEIHIGGLGVAQG
YWQAETLTRERFIYHPTYGRLYKTGDLGRWSAEGYIEFLGRRDAQVKLNGYRVELEDIEN
NLSQLPGIRQTIVRLSEGDLMAYVVPEAQQPVPLYFANRDAFVLSLPALRQDLQPSRAIP
YPLDETVYRARKSTRQFTAEALSAETISSLYEALPGWLTQQMAQEGSTLSPASLAGLLAV
CAAIRSPQRALPKYRYPSASSLYAVQVYLGLPAAMGEYAAGYYYYHPLEQHLYQAEASGE
HTGPYLDLVVRWETITALYAERAFALAQIEVGHMLALLTEHLQSLGVAYYVKPADAVSPD
EGALACRIHLGVCAVTSPPQVSVDFSVMENEGGTYFARASGQHYCLGETSVLAESSDVYG
VLQSSQVLLQVHGAKNACHYQASGWMMQRFGALAAQRRIGGCILGVTPAEDTLCSMAIGY
ARAEDEPAFDVPALTVSMTQTIRRHLARRLPDYMLPQHVTLIPEIPLSNNGKVDTSRLPK
VVKHSECLAPRSDDEIRMRRLWAELLDKREERIGCDQSFFTQGGNSLLAMRLVRKINLAT
GTEMRLEDLYNNNTIQEMAAWVAGQPCGNGREEGAL

Enzyme Prediction     

No EC number prediction in MGYG000002518_00496.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK12316	PRK12316	0.0	309	1891	1935	3496	peptide synthase; Provisional
PRK12467	PRK12467	0.0	357	1923	496	2060	peptide synthase; Provisional
cd12114	A_NRPS_TlmIV_like	1.11e-165	1449	1919	2	459	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.
cd05930	A_NRPS	6.96e-159	388	868	2	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.
cd12116	A_NRPS_Ta1_like	6.97e-159	388	868	2	470	The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase. 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 myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QND46664.1	4.81e-148	375	1950	1011	2607
ACX49739.1	4.77e-97	361	1688	448	1817
AFZ04852.1	5.70e-95	329	951	538	1180
BAZ00088.1	1.84e-78	345	951	550	1175
BAY30132.1	1.84e-78	345	951	550	1177

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7LY7_A	7.16e-166	973	1892	4	891	ChainA, BmdB, Bacillamide NRPS [Thermoactinomyces vulgaris]
7LY4_E	7.36e-166	973	1892	4	891	ChainE, BmdB, bacillamide NRPS [Thermoactinomyces vulgaris]
6MFY_A	6.54e-146	373	1892	205	1673	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]
6MFZ_A	2.00e-145	373	1892	205	1673	Crystalstructure of dimodular LgrA in a condensation state [Brevibacillus parabrevis],6MFZ_B Crystal structure of dimodular LgrA in a condensation state [Brevibacillus parabrevis]
6LTA_A	2.89e-129	979	1887	56	958	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O68006	1.79e-254	364	1887	27	1517	Bacitracin synthase 1 OS=Bacillus licheniformis OX=1402 GN=bacA PE=3 SV=1
O30409	1.98e-170	344	1945	1473	3051	Tyrocidine synthase 3 OS=Brevibacillus parabrevis OX=54914 GN=tycC PE=1 SV=1
P0C064	6.14e-169	344	1892	442	1952	Gramicidin S synthase 2 OS=Brevibacillus brevis OX=1393 GN=grsB PE=1 SV=2
P0C063	6.15e-169	344	1892	442	1952	Gramicidin S synthase 2 OS=Aneurinibacillus migulanus OX=47500 GN=grsB PE=3 SV=2
O30408	3.16e-165	310	1905	401	1982	Tyrocidine synthase 2 OS=Brevibacillus parabrevis OX=54914 GN=tycB 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
1.000048	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002518_00496.