CAZyme Information: MGYG000002350_03759

Basic Information

• Species: Serratia marcescens_I
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Serratia; Serratia marcescens_I
• CAZyme ID: MGYG000002350_03759
• CAZy Family: GT2
• CAZyme Description: D-alanine--poly(phosphoribitol) ligase subunit 1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2376	MGYG000002350_132|CGC1	266757.61	5.6517

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002350	5255807	Isolate	United States	North America

• Gene Location: Start: 16966; End: 24096 Strand: -

Full Sequence      

MKILNILVNHTVEPLRSHMVRYLLDAGHFVYLIGLSDAERTRWTGSQHNLFCYSDVGDQR
IDYELCLEESASVRGPIVRLAVFADRQNVLFQIHAEEDGNIRALAQRELHWREARRALSQ
AVLGELFIDGVVMLSREAKDLDIALPEGPNRVTDWLVAQQRVQQEQRALENDELRYGCFN
LRDEVSAVNDAAVVQRTIDGVAQPQQALLLAFQLQFLLNARRPGLYALQLQDRQRSSKVL
RLLNGRETYADLSPWLVRVLQGDPANPFYESHHDGRFLSVVGVDVIMDEGDVDTAAAPIR
IVWNSTRCTLSLQFYGENPFFDVVAANIDEFMAALATFMRNEGDIDALTGVSENSYQRYY
AKINATQCEYPRQTIVGMFEQQARALNDHPAVITKNEVLSYRMLQQQASRLADYLQRQYG
VAAGDKIALMMPREAELVVCLMAVLKLGCAYIPIDKNAPVVRTYSILADAQPALIIGAHA
QSAGSLPQGLNYLDWREYAASPFAGADGCNEFPSQAEASALAYIIYTSGTTGKPKGVAVE
HRSFVNIASDISRRMSVTHQDRFLAITTLAFDISTLEIFMPLMFGATVVLTDQKTLLANN
DLPQFIASHSVSLMQGTPSFWHQVAQQYAETTLPVRALCGGEAVPHAVARWLSENTERAW
NVYGPTETTVWSTADELLPGVDSVTIGRPLANTQCFILDERRRLLPPGVIGEMYISGLGV
ARGYYGNARQTQASFLPNICSSTPSAWFGRIMYKTGDRVRCLPDGRFEYLSRWDNQIKLR
GHRIELGEIESVLRTYPGMQQVVVNLQPAKEEQQAFLVAYYQAKSPVARQQLQDYLVTLL
PDYMLPSAYMYLPEIPLNMNGKVDRKALPPVQAQDKAHYVAPGNEFQRCLCQLFQDVLGS
ESGRVGITDDFFALGGNSLSAIRLVNRINGTLQCDLKVKDIFERKNVARLTPLVAAGRGS
FLYQDYQIAQCDETHLYHPFPLNNVQQSYYLGRMKSFDLSEVSTHIYNEFVFDHIDHDKL
ERAYNQLIARHPALRTVFEEGEQRFLSAVAHYKIGYHPLRNEDELLALRAEYSHKVYKPD
CYPLFDIFLSEYQGKYLLHVSFDAIIIDMTSFEILFGEWIALYHDENLALPPLDISYRDY
QLQYERLRGGALFERAQQYWLQKIDDYTLEAGLPLAAHPARIDKPSFRRLSATIPMSSWQ
KIVDKCQRFNISPTALILELYSRTLCYWSGQESLCLNLTLFNRLPLHSQVEQIIGDFTVL
SLFNYQRQNGVAMSEQLSAIHRTLLNDVDNNLFDGIDVQRLLKQRRNLSANTVIAPVVLT
SVLGMNNKASMFELPLNEGYRGVQYAISQTSQVWLDHKAYENDEGFVAEWDYVEQLFDEK
TIKAMHEGYCSLIRWVAEHDWETMSFPQPELPAEHAEAVMRWNATQSTVSEQTLHGLFLS
SLETPQTAERIAVIETEGERHFTYARLEQDSNTLGRALLRHTKGEKGRITAILLEKGYAQ
AVSTLGIMRSGGAYLPLHIEWPWERIRDILQQARCDILLLSAQQCHDLAHELSALPSDIT
ILVFDEIVAPAQERASTEVAWPIVRADDLAYIIFTSGSTGKPKGVAIDHQGAVNTILAVN
QRWSVGREDRILALSELSFDLSVYDLFGLLAVGGGVVIPSQRETKAPQAWVAALRRHDVT
LWNSVPQLAGLLVDEVEPATRALTRLRLFLLSGDWLPLNLPDRLKTQSPDGKMVSLGGAT
EGSIWSIWHEIERVDARWKSIPYGVAMPNQQMWVLDEWGSACPFGVTGEIHIGGLGVAQG
YWQAETLTRERFIYHPTYGRLYKTGDLGRWSAEGYIEFLGRRDAQVKLNGYRVELEDIEN
NLSQLPGIRQTIVRLSEGDLMAYVVPETQQPVPLYFANRDAFVLSLPALRQDLQSSRAIP
YPLDETVYRARKSTRQFTAEALSAETINSLYEALPGWLTQQMAQEGSALPPASLAGLLAV
CAAFRSPQRALPKYRYPSASSLYAVQVYLGLPAAMGEYAAGYYYYHPLEQHLYQAEASGE
HTGPYLDLVVRWETITALYAERAFALAQIEVGHMLALLTEHLQSLGVAYYVKPADAVSPD
EGALACRIHLGACAVTSPPQVSVDFSVMENEGGAYVARASGRHYCLGETSVLAESSDVYG
VLQSSQVLLQVHGAKNACHYQASGWMMQRFVALAAQRRIGGCILGVTPAEDTLCSMAIGY
ARAEDEPAFDVPALTVSMTQAIRRHLARRLPDYMLPQHITLIPEIPLSNNGKVDTSRLPK
VVKHSECLAPRSDDEIRMRRLWAELLDKREERIGCDQSFFTQGGNSLLAMRLVRKISLAT
GTEMRLEDLYNNNTIQEMAAWVAGQPCGNGREEGAL

Enzyme Prediction     

No EC number prediction in MGYG000002350_03759.

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	1916	496	2050	peptide synthase; Provisional
cd12114	A_NRPS_TlmIV_like	9.13e-167	1449	1911	2	454	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	2.07e-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	1.92e-158	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	1.83e-146	375	1929	1011	2586
ACX49739.1	9.54e-96	361	1700	448	1830
AFZ04852.1	1.74e-93	329	950	538	1179
BAZ00088.1	1.22e-77	345	950	550	1174
BAY30132.1	1.22e-77	345	950	550	1176

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7LY7_A	2.24e-167	973	1889	4	890	ChainA, BmdB, Bacillamide NRPS [Thermoactinomyces vulgaris]
7LY4_E	2.30e-167	973	1889	4	890	ChainE, BmdB, bacillamide NRPS [Thermoactinomyces vulgaris]
6MFY_A	8.81e-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	2.69e-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	1.43e-130	979	1888	56	959	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	5.47e-255	364	1887	27	1517	Bacitracin synthase 1 OS=Bacillus licheniformis OX=1402 GN=bacA PE=3 SV=1
O30409	2.75e-172	344	1945	1473	3051	Tyrocidine synthase 3 OS=Brevibacillus parabrevis OX=54914 GN=tycC PE=1 SV=1
P0C063	2.62e-169	344	1892	442	1952	Gramicidin S synthase 2 OS=Aneurinibacillus migulanus OX=47500 GN=grsB PE=3 SV=2
P0C064	2.62e-169	344	1892	442	1952	Gramicidin S synthase 2 OS=Brevibacillus brevis OX=1393 GN=grsB PE=1 SV=2
O30408	1.05e-166	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
1.000058	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002350_03759.