CAZyme Information: MGYG000001453_00484

Basic Information

• Species: Aneurinibacillus aneurinilyticus
• Lineage: Bacteria; Firmicutes; Bacilli; Aneurinibacillales; Aneurinibacillaceae; Aneurinibacillus; Aneurinibacillus aneurinilyticus
• CAZyme ID: MGYG000001453_00484
• CAZy Family: GT2
• CAZyme Description: Linear gramicidin synthase subunit B

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1722	MGYG000001453_31|CGC1	195915.09	5.4972

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001453	5302959	Isolate	not provided	not provided

• Gene Location: Start: 20562; End: 25730 Strand: -

Full Sequence      

MNHSRGYILKKINSISILTAQEREQILFEWNDTEVSYPGDKGLHQLFEEQVLRTPEHVAA
VFGDEQITYDELNRHSNQLAHYLREIGVQKDTAVGILMERSLDLVVALLGILKAGGSFLP
LDTENPSARIGHILEDAQATICITQDHLVDKLSELQWVKPVFFEEQLDFIQSFSQDNLDV
SHDPDQLVSIYYTSGSTGNPKGVASTHRGWVNRMDWMQKKHQLTSRETVLQKTTLTFDDA
AVEFFWPLMVGARIALMEPGSHRDPRAILDAAIRYDAAVIQFVPSMLRMVLETITPEDKA
QLSSLRVVVSSGEALQACLVGEFLEKMPGDLFNSWGATEVSIDSTVHKCSKEDALYGGVV
SVGRPINNNQVYILDSYLQPVPIGVPGDLYLGGVGLAREYINQPKKTNEAFVNNPFVHGT
RMYKTGDTGYYTPDGSIMFLGRKDNQIKIRGMRVELGEIESVLMRCSGIKEAVVDVSGHD
DIKRLVAYIVSDDKELNQSKLRSFLSNQLPDYMIPSFYIFLEKLPLNANGKIDRKALPQP
DLEQVVSDSDFVAPKTDTEKKLAEIFSRVLGLKRIGIHDNFFALGGHSLLVVKLVSRIQE
LFEVRLPLRTIFESPTVEKLSFILDQEQSPRGNITSLMKCDRSQTIPLSYAQRRLWFLNQ
LDSENAAYNMPIIMKLNGQLDLEALKQSLRRIIERHEILRTTFKSADGGPVQVIDDTYDI
QLNMVDFTSYSKEQRIERAQDWYRIEARRPFVLSQSPLIRPYLLRLDSQEYALVINVHHI
LSDGWSLDILKHELTCCYEAFVQHREPSLPTLTYQYADYAYSQHQWMKNEEFQRQLAYWK
ERLAGDIPLLTLPTDHVPMPTSQEHIRKLPIKLTDDLRQWSEKQGATLFMTMLAVFKILL
HRQTGQEDIMVGTPVINRDNQHLEPLIGLFLNTIVLRTQFSRKMSFKEIVHLIRDNFIDD
FSHKDVPFEMLVEEVQPNRNLNRSPLFDVFVNYVNFDNNMKPKWNMHNIAMEPLDWLEPV
SKFLLTLYIVETEEGLVLNFVHQSDAFSAERVEMWLDQYQLLLEQMLEQPDQPIHSFSLT
RQYTDGLLPDPTVDLDQPEVQKVYQLISNQAQQHPNKVSITQGNKSYTYSQLMEKADQVA
NFLRKRGVQSKQVIAVRGKRSHAFIPIMLGIWKVEGILLLIDSAFPDARQQSLIQESSAS
WLIDIPLDCHIENYEQNVTMKPLANEAPINLNLSTDQADLDPAYIFFTSGTTGKPKGVLG
SHQGLSHFLLWQQKEFGIHSQDRAAQLTNLSFDVYLRDTLLILISGGTLCIPEDPYDLHG
ETIISWLKKEKITLIHSVPSILQSWVMDQQSQTSLASLRWIFSAGEPLTGSLIEKWRAKF
QQTGTFVNLYGPTETSLAKCFYIVPDSIQQGILPVGQPIPQTQVLILNEERSLCGVGEVG
EMVIRTPFRSMGYCNSPDETKRLFSPNHFKNERNDLLYYTGDMGRYRPDGSIEILGRTDD
EIKIRGVKIHPSEISAVIAKHPAVSQCVVVAVKEQSGDHKLFSYIVAKSDTGINDEELRE
YISQELPVSMQPSGFMFLPRLPLTLNGKIDRKALPNPVFRISEVAYVPPSDEIEEKICEV
WASLLNVEKIGIKDNFFSLGGHSLLAVQVVARIRKTFSIDFSVPHLFENPTVAKLAELVR
NSKSSSPLVQPITKIEKEWDSESIDKLSNEEIEGMIESLMKN

Enzyme Prediction     

No EC number prediction in MGYG000001453_00484.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd17646	A_NRPS_AB3403-like	0.0	44	537	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.
cd19531	LCL_NRPS-like	0.0	645	1070	1	427	LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity. LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. 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). In addition to the LCL-type, there are various subtypes of C-domains such as 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 heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. 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. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
PRK12467	PRK12467	0.0	10	911	1543	2443	peptide synthase; Provisional
PRK12467	PRK12467	0.0	11	1693	483	2178	peptide synthase; Provisional
cd05930	A_NRPS	0.0	55	537	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QND46664.1	9.77e-290	12	1683	980	2666
BAY90071.1	3.95e-185	522	1687	2100	3291
BAY30132.1	3.19e-184	522	1687	2111	3302
BAZ00088.1	9.09e-182	522	1687	2109	3300
BAZ75991.1	9.09e-182	522	1687	2109	3300

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MFZ_A	1.13e-254	38	1683	202	1801	Crystalstructure of dimodular LgrA in a condensation state [Brevibacillus parabrevis],6MFZ_B Crystal structure of dimodular LgrA in a condensation state [Brevibacillus parabrevis]
6MFY_A	1.65e-234	38	1597	202	1715	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]
5U89_A	7.98e-199	21	1074	5	1056	Crystalstructure of a cross-module fragment from the dimodular NRPS DhbF [Geobacillus sp. Y4.1MC1]
6MFW_A	6.87e-157	38	1079	202	1200	Crystalstructure of a 4-domain construct of LgrA in the substrate donation state [Brevibacillus parabrevis]
6MFX_A	3.46e-156	38	1079	202	1200	Crystalstructure of a 4-domain construct of a mutant of LgrA in the substrate donation state [Brevibacillus parabrevis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q70LM4	0.0	10	1679	432	2093	Linear gramicidin synthase subunit D OS=Brevibacillus parabrevis OX=54914 GN=lgrD PE=1 SV=1
Q70LM6	0.0	10	1682	3007	4674	Linear gramicidin synthase subunit B OS=Brevibacillus parabrevis OX=54914 GN=lgrB PE=1 SV=1
Q70LM5	0.0	10	1682	5611	7273	Linear gramicidin synthase subunit C OS=Brevibacillus parabrevis OX=54914 GN=lgrC PE=3 SV=1
P0C064	6.92e-317	11	1704	2512	4184	Gramicidin S synthase 2 OS=Brevibacillus brevis OX=1393 GN=grsB PE=1 SV=2
O30409	5.29e-315	15	1682	1474	3114	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
1.000068	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001453_00484.