CAZyme Information: MGYG000000249_00616

Basic Information

• Species: Mediterraneibacter faecis
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Mediterraneibacter; Mediterraneibacter faecis
• CAZyme ID: MGYG000000249_00616
• CAZy Family: GT2
• CAZyme Description: D-alanine--poly(phosphoribitol) ligase subunit 1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2620	MGYG000000249_2|CGC2	297696.86	4.7226

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000249	3112009	Isolate	China	Asia

• Gene Location: Start: 172820; End: 180682 Strand: -

Full Sequence      

MMNNEATHVKTQEDYSKFSSIVNEFLQEQMNEDFMEKNLLEAGVTSLQMMRISNALRKHG
YKISFAKMISDPYVKHWWDNADINVKRKSVPPLETSNNSPKQFPLTDVQYAYWVGRKEGQ
VLGGNACHAYFEFDPDTVNLERLQEAWEELQARHPMLRAKFNNNGTQEIMEKPYSAKLQI
YDFRKSDDFEHDLLAVREKLSHRKLDIANGQVAELGISLLPEDKLRMHFDIDLLVADMQS
LQIIFRDLAAIYNSEYRPAIPENWDFGIYLENEKNNKINDYRKAEKYWKSEIESLPLGPA
LTLRTQPETIAAPKFSRRKYLLEHKKWEKLKSLAAQYCTTPAMVLLTLYAAVLDRWSTNQ
SFLINMPLFDRNTEIENIDNVIADFTNVLLFHADCKENCTFYEQLQKVQNQFRESVDNSE
YSGVQVVRELSKLHPGEKCIAPVVFSCNYGTPFVDDKFEKTFGSLNYMVSQTPQVWIDFQ
IFEINNGLNLSWDAVDELFPDGMLDKMFAAFVAMLNELVSVKDWNKYVELLPDLAQERGI
DNITEYYGNGQLLHSAFFVNAVKKKNQIAIIDENDGRNYTYEEVANKAKRVSSYLKEQGV
APGDLLAVSLSRGINQIISILGILAAGAGYIPINVNQPLSRRERIYSKSDIKFAITDTRL
KKELEWPETVTVLDVMEADAYEPLNTIENYPDSNTAYVIFTSGSTGEPKGVEIAHFAAVN
TIETINKQYRVSADDKIIAVSSYDFDLSVYDIFGILSAGGTLILIKDSNSRDAEVWLDIA
ERHSVTLWNSVPTLLNMLLIVAEGKGKEIPSLRLAMLSGDWIGMDIPERLNHVAKNSHLL
SMGGATEASIWSNFFDVELPVPEEWSSIPYGKPLKNQYYRVVDSKGRDCPTWVPGELWIG
GTGVAKGYIGDSEITDKSFVNWNENRWYKTGDLGRYWADGNIEFLGRKDFQVKIRGHRIE
LGEIEAAMNKYPGVKKSVAAAVGDVQGNKYLAGYIIPENGYPESLFDVNKVSDTDLMYKW
DRLWADLKEGVAEVTAENNVQEYLTLANCLDEVSREYMYSLMRTLGIWVEPGTKYKLSAL
LMSAGIDLSYQELIQQWVNELVKIGRILAEEDYFVNCSSPKEMDRVAFIEKYPEWKHEID
DALKYLEQFKKYCHAIMTGNMDTPQLLAKEDYISPDAYMATLPGAIECKRTIKNILSFQK
KEGTAGQTVRIMELGARNLGLTSELLDCMDGIEYEYVCTDASSYYLNQAKEKFKNNSRVH
YENLDINSAPNTQGLAMHYFDVVLAVSTLHRCRDIKASLKHAGEYLRAGGLLILLETTEN
TILQHVSTGILEKGFSTVTDERKGTGKPLLTKDQWSDAVLKCGFAKVNTAPNDQLDLPIY
NQGVIVALAQPETYAFNSTKLKAYLENMIPSYMIPTAFMEIDKFPLSANGKVDRKALPVP
VGETRENAKDQFQEPETAVEKELAAIWKTVLHTENISRNDNYFELGGDSLLATQLNAEIN
KKFNINLSLEKIFSNPIFAEQAISIASMLEDCEVKNMNAEKLEMVSPKPKEWGEPFPLTD
VQQSYWLGRNGGFALGDVSTHCYFEMDCGGLDTDLAEEKWRRLILRHGMMRAVFLNDGQN
QKILSNVPEYEIKVYDLASQEETVDEKLESIRKEMAYQIFDTSKWPLFDVRFSKLPGGNV
RLHISFDNIIFDGWSMFLILREWKMLYDNPEKEVEPLDLSFRDYVLAYEDIKKTEFYKRD
EEYWQKRLPDIFPAPELPVIKENGNTAVQKFIRYESKLTGSQWSAIKNMASQNGLTASGV
LMTAYAEVLGRWSKSQKFTINLTRFNRLPIHNQIMDVVGDFTSLTLLSIDNTAGKSFLER
CKNLQQQLWSDLAHPYYSGVELEREISKKQEIRNAAIMPIVFTSGLGIKQGGSNEQEEYF
GEMVYGLSQTPQVWIDHQVTEQNERLVLTWDAVQDIFPAGVLDEMFAAYISLLEVLSTEQ
EAWNRESNSLVQIPNMENRELANSVNGKIPDETLISLVEKSMKENPERIAIINNERKLSY
GELERYSTGIGHILQRENVERNSLVAIVMEKGWEQIVAAISILKAGAAYLPIDPSFPEER
VHLLLKNASVKVVLTQEKVNREVNWPEDTTIICVDGVDVESIDTTDFESIATGNDLAYVI
YTSGSTGMPKGVMIEHRAAVNTIIDVNERFAVGKDDKCIALSNLNFDLSVYDIFGLLIAG
GTVVIPDAKQVKEPQHWLEIMQENKITVWNSVPAFMQMFMEFLSTKPDTKLPLRVVIMSG
DWIPMELPEMIKMHSESVRMISMGGATEASIWSNYYEVESVKDGWTSIPYGKPLTNQKFY
VLDQEMNDCPNWVAGRLFIAGEGLARGYWKDRKRTEERFINHPVTHERLYYTGDLGRYWP
DGNIEFLGREDTQVKVRGHRIELGEAENVLLTHELIKSAVVVVEEDKSGLAAAVVLNEDS
DCCDNKNVEKILHEYLGKKLPEYMVPGKILVMEQLPLSVNGKVDRKALRKILGGYQGQIS
EEKKKEAPQGELEVKIAAIWERVLGTKEISRDDDFFMCGGDSLKAVKIISELNATEGLPN
DLAIQTLFALPTVALLAEQIEKLVSLLDVEENTEYEEGVL

Enzyme Prediction     

No EC number prediction in MGYG000000249_00616.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd19535	Cyc_NRPS	0.0	1555	1979	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	566	1003	2	435	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.
cd12114	A_NRPS_TlmIV_like	0.0	2026	2508	1	477	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.
cd19535	Cyc_NRPS	0.0	103	519	2	420	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.
PRK12316	PRK12316	0.0	138	2602	2637	5141	peptide synthase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QND46664.1	4.24e-148	38	2602	465	2664
BAZ00088.1	3.38e-113	1415	2597	2105	3289
BAZ75991.1	3.38e-113	1415	2597	2105	3289
BAY30132.1	3.88e-112	1431	2597	2120	3291
BAY90071.1	1.96e-111	1423	2597	2101	3280

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7LY7_A	1.68e-221	1554	2603	9	1019	ChainA, BmdB, Bacillamide NRPS [Thermoactinomyces vulgaris]
7LY4_E	1.73e-221	1554	2603	9	1019	ChainE, BmdB, bacillamide NRPS [Thermoactinomyces vulgaris]
7EMY_A	2.24e-218	36	1555	36	1451	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]
6LTA_A	2.73e-201	1539	2600	40	1098	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]
6MFZ_A	2.23e-147	554	2597	208	1794	Crystalstructure of dimodular LgrA in a condensation state [Brevibacillus parabrevis],6MFZ_B Crystal structure of dimodular LgrA in a condensation state [Brevibacillus parabrevis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P48633	0.0	36	1991	42	1917	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
O68006	5.02e-253	541	2573	27	1626	Bacitracin synthase 1 OS=Bacillus licheniformis OX=1402 GN=bacA PE=3 SV=1
A0A0H2ZGB9	2.08e-217	36	1533	36	1429	Pyochelin synthase PchE OS=Pseudomonas aeruginosa (strain UCBPP-PA14) OX=208963 GN=pchE PE=1 SV=1
G3XCV2	2.87e-217	36	1519	36	1415	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
O30409	2.35e-182	142	2600	1094	3111	Tyrocidine synthase 3 OS=Brevibacillus parabrevis OX=54914 GN=tycC 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
1.000052	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000249_00616.