CAZyme Information: MGYG000001514_03666

Basic Information

• Species: Paenibacillus_A ihumii
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A ihumii
• CAZyme ID: MGYG000001514_03666
• CAZy Family: GT2
• CAZyme Description: Tyrocidine synthase 2

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
3620	MGYG000001514_12|CGC40	409034.62	4.9245

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001514	5923787	Isolate	not provided	not provided

• Gene Location: Start: 2346655; End: 2357517 Strand: -

Full Sequence      

MFNRDQVEDIYNLSPMQLGMLYHSIRDDNAQAYFEQMNFTLQGDIKVGILEKSFQMLIQR
YGILRTVFIYENVDRPLQVVLKHREAAVTHIDLSNMQAGEQEERLRQIESEDRERGFDLT
RDVLMRMILVKLDSTRYRLIWSHHHILLDGWCFSIIVNDFFQLYTAQLANAPAQLGPVYP
YSHYIKWLETQDMDEALEFWKGYLADCEQRTVLTGQEERLAGENGYDKGELVVSIDKEIT
AALTSIAKEHQVTLNHIVQSIWGILLARYSGTEDVVYGSVVSGRSSDIPGIEKMVGLFIN
TIPVRIKAEEHSTFDQLVRDVKWRDIEAQRHDYISLAQIQASSPLKQDMFDILYVFQNYP
VIGGNSGMEEQPGLGFAVQETDTHEQTNYNLTFMAAPGEEIVLKMTFNSNVYSHALIKQL
LKHFVHLSRQVAADPTQRIGELEIITEAEKRRIAEDFNATQAPYPKEKTVVELFEEQVKR
LGEQPAVIYGGQQLSYRELDERSSQLAHALRSRGVGRDMPVAVMAERSAEMIVCLLGILK
AGGAYVPIDPAYPQERIRYMLEDSCAKWLLLPTGASIESTPGYSPVLTLSLQDAGLQEYP
IESPPISGSPHDLAYVIYTSGSTGRPKGVMIEHQSIVRLVKNTNFIDFTETHRILQTGSI
VFDASTLEIWGALLNGGELYLEDQERLLSPQGLKEAVGKHQITTMFLTTPLFHQLLEQDV
DIFGGLKLLMVGGDALSPVHANKLRAHYSQLKLVNGYGPTENTTFSTTYTAEKIEGSSVP
IGQPIANSTAYVMNASMQLQPIGVAGELCVGGDGLARGYLNNPELTSERFVPHPLIPGER
LYRTGDLAKWTAEGNLLFLGRLDHQVKIRGYRIEPGEVAEQLRRHEAIKEAYVRVCKEEQ
SDISYLCAYYAADREFTGDEARSYLAQYLPDYMMPSRYIQVDQLPLTINGKVDTGRLPEP
GPDSSSKPAYIAPRTDIETALARIWEDVLGVSPVGIHDHFFQLGGHSLSAMTVIAGIHKQ
LNRQIPLKLLFEQPTIEGLARALEQQEQQEFAAIAPAGKRAYYPVSAAQRRMYVVSQLEN
AKTSYNMPNVLVVEGQLDIRRLEDVFQTLVQRHEAFRTGFEMIDGQLVQKIQEQVELKVE
ELAVDTAHPSGAVDLEQEKAHIAAFIRPFDLSQAPLLRVGMIRRSEQEHVLLIDMHHIIS
DGVSMTVLTEEFSRLYAGKPLPELRIQYKDYAVWQQEQQGTEQQREQETYWLETFSGELP
VLSLPTDYPRPAMQQFEGAQFTFDIGPELSAKLFRLMKAENTTLYMVLLAAYNVLLSKYS
GQEDIIVGTVAAGRTHADLESVIGMFVNTLPIRNYPKGSCSFREFLQQVKENGLKAFEHQ
AYPFEELVERLELPRDLSRNPLFDTLFGVQNLREASERTEGLEFRPYGHEERMAKFDLTM
TAWELEEGIQFELEYSTHLFHADTIRRMAEHYKQVLEQIAERPEQKLSALEIITEAEKRR
ITEDFNATQVAYPKDKTVIELFEEQAERLGEQPAVIYGGQQLSYRELDERSSQLAHALRS
RGVGRDMPVAVMAERSAEMIVCLLGILKAGGAYVPIDPAYPQERTRYMLEDSGAKWLLLP
TGASSASTALAESTPEYSSVLTLSLQDAGLQEYPVDRPAISASPHDLAYVIYTSGSTGRP
KGVMIEHQSIVRLVKNTNFIDFTEPHRILQTGSIVFDASTLEIWGALLNGGELYLEEQER
LLSPQGLKEVIGRHQITTMFLTTPLFHQLLKQDADLFDGLKLLMVGGDILSPADANKVRV
QNPQLKMLNVYGPTENTTFSTSYPMDRMREGMVPIGQPIANSTAYVMNASMQLQPIGVAG
ELCVGGDGLARGYLNNPELTSERFVPHPLIPGERLYRTGDLAKWTAEGNLLFLGRLDHQV
KIRGYRIEPGEVAEQLRRHEAIKEAYVRVCKEEQSDIPYLCAYYAADREFTGDEARSYLA
QYLPDYMMPSRYIQVDQLPLTINGKVDTGRLPEPGPDSSSKPAYIAPRTDIETALARIWE
DVLGVSPVGIHDHFFQLGGHSLSAMTVIAGIHKQLNRQIPLKLLFEQPTIEGLARALEQQ
EQQEFAAIAPAGKRAYYPVSAAQRRMYVVSQLENAKTSYNMPNVLVVEGQLDIRRLEDVF
QTLVQRHEAFRTGFEMIDGQLVQKIQEQVELKVEELAVDTAHPSGAVDSEQEKAHIAAFI
RPFDFSQAPLFRVGLMRWSEQRHVLMLDMHHIISDGASMTVLTEEFSRLYAGKPLPELRI
QYKDYAVWQQEQQGTEQQREQETYWLETFSGELPVLSLPTDYPRPAMQQFEGAQFTFDIG
PELSAKLFRLMKAENTTLYMVLLAAYNVLLSKYSGQEDIIVGTVAAGRTHADLESVIGMF
VNTLPIRNYPKGSCSFREFLQQVKENGLKAFEHQAYPFEELVERLELPRDLSRNPLFDTL
FGVQNLREASERTEGLEFRPYGHEERMAKFDLTMTAWELEEGIQFELEYSTHLFHADTIR
RMAEHYKQVLEQIAERPEQKLSALEIITEAEKRRIAENFNATQTLYPQEKTVVELFEEQA
ERLGEQPAVIYGGQQLSYRELDARCNQLARVLAGKGVGPESIVALRVERSFEMVAAILAI
LKAGGAYLPIDPEFPAERVEYMLEDSGARVLLSRGPQAAELGFRGEWIDLLEPELYQGDA
SPLERRPEPGHLAYVIYTSGSTGQPKGVMIEHRNLSHILHALQRAYPLQREDRYALKTNY
TFDVSVSELFGWIPGGGALVVLPPGAEKEPEAILSAIEAERITHINFVPSMLQLFVMAGQ
RLERLNQLKYLFVAGEALPVQLADKLREQADGVRLENIYGPTEGTIYATRYSVTGGERTM
PIGKPLDNVRAYIVNEAGQLQPPGVPGELCIAGAGLARGYLNRAELTAEKFAANPFEPGE
RMYRTGDLARWLADGTIEYLGRMDFQVKIKGYRIELGEIAARLREHDQVRDAVVLAREDE
AGQPYLCAYVVAEPGWERKELRRYASGYLPHYMVPSFYVGLEELPLGSSGKIDSRRLPEP
DREQAAETDYTAPANEKERLLSEIWQTVLGMKRVGTEDNFFELGGDSIKAIQIAAQLKQH
GYKLEMKDLYMNPTISALTPAVQPVKYRVDQSEVVGDVRLSPVQKWFFESSFSEPHHFNQ
AMMLFRAEGFQSELVRMAFDKVVEHHDALRIIFLHQAGHLTQVNRSAKAENQQLYTLTSY
DISEDQISLAANELQSSLNIHEGPLIRLGLFHTEAGDHLLLAIHHLLIDGVSWRIVLEDL
EQCYQQALEGSTLHLPDKTSSYRDWTERLYAYANSSSMHRELDYWRSLANLKLQPLPKQR
LAADRTWENTRTLSIQFSEEETDLFLRKAPSAYNTEPNDLLLAALGITLHAFTGYERAAI
LLEGHGREELFEELDITRTVGWFTTMYPVVLDMSKVHDLAYHIKNVKETLRSIPNKGIGY
GLLNYLTERTKEQDQSLAIAPDISFNYLGQFDGDIDKGQFVQSPLSSGSAISPRNKRECS
LDISGLVLDHKLTMNFSYHQEEYSEQQMIELLESCKKALLDIIRHCAEKEGSEATPSDLG
HEDLSVEDLLTITDKIQFSL

Enzyme Prediction     

No EC number prediction in MGYG000001514_03666.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd17655	A_NRPS_Bac	0.0	1520	2014	1	489	bacitracin synthetase and related proteins. This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. 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.
cd17655	A_NRPS_Bac	0.0	2574	3061	1	490	bacitracin synthetase and related proteins. This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. 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.
cd17655	A_NRPS_Bac	0.0	472	960	1	489	bacitracin synthetase and related proteins. This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. 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.
PRK12316	PRK12316	0.0	6	1046	4098	5142	peptide synthase; Provisional
cd05930	A_NRPS	0.0	483	957	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QND46664.1	0.0	546	3161	1	2679
BAY90071.1	2.46e-302	188	3155	306	3296
BAZ00088.1	1.62e-298	181	3155	300	3305
BAZ75991.1	1.62e-298	181	3155	300	3305
BAY30132.1	7.73e-298	181	3155	300	3307

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MFZ_A	0.0	1513	3142	202	1797	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	0.0	1513	3066	202	1721	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]
2VSQ_A	7.19e-251	2	1156	4	1158	Structureof surfactin A synthetase C (SrfA-C), a nonribosomal peptide synthetase termination module [Bacillus subtilis]
6P1J_A	1.02e-216	2117	3057	6	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]
6MFW_A	5.23e-198	465	1497	202	1205	Crystalstructure of a 4-domain construct 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
P39845	0.0	1063	3617	6	2559	Plipastatin synthase subunit A OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsA PE=1 SV=2
P94459	0.0	1	3618	1	3602	Plipastatin synthase subunit D OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsD PE=1 SV=2
P39847	0.0	1063	3617	11	2553	Plipastatin synthase subunit C OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsC PE=1 SV=2
P39846	0.0	1063	3612	11	2553	Plipastatin synthase subunit B OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsB PE=1 SV=1
Q04747	0.0	3	3620	2	3582	Surfactin synthase subunit 2 OS=Bacillus subtilis (strain 168) OX=224308 GN=srfAB PE=1 SV=3

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
1.000038	0.000002	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001514_03666.