CAZyme Information: MGYG000002817_02127

Basic Information

• Species: Paenibacillus_B sp900539405
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_B; Paenibacillus_B sp900539405
• CAZyme ID: MGYG000002817_02127
• CAZy Family: GT2
• CAZyme Description: D-alanine--poly(phosphoribitol) ligase subunit 1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1924	MGYG000002817_9|CGC1	217494.05	5.6282

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002817	6425839	MAG	United States	North America

• Gene Location: Start: 18836; End: 24610 Strand: -

Full Sequence      

MTNKNELETRRSLLSDKQRELLEQWKLGRGRKQPRIVPRPEEDGLVLSPAQKRLWFMDQM
LADKSAYNMYFAVRFSGELDIEAARRALQHIIDRHESLRINFINSGGRPQLRRMDRFTLE
LPIEDVSGLHETEAEAQANAVIQRVISSPFDLERGLLMRAQVIRLKEREHMLAICLHHII
SDGWSMGVLAKEWVACYRSYSEGKTPALAPLPIQYSDFAHWQTEQLKSGAWEKHLRYWKD
RLEHCPSIALAPDKKMTDWAGNRGGEVPFELPDDLAHALKSFCAEADATMFMTLLALFGG
LLYRYTHERTLVVGTPVANRNDTEIEGLIGYFVNLLPLRMDIGADMTFRELLRQVAATAA
EAYDHQDFPFDRIVEELQPDRQGWAIPLVRNLFVYQNTPAVDIQLPKARAESIRLFNGTS
KSDVLLSMAELQGKITGRLEYNANLFVPQSMQNFVNHFIQFIRSALSAPDRAIGRLDLME
EGERESMLQRSAAIEETAAASEGIHRQFERNAALYPNNVALKWNEAVWTYRELNAYANRL
ARHLLQSGAEPGQFIGLCMYRSPYLIAGILAILKAGCAYVPLDPAYPEERIRWMLSDSGC
ALLLVDEETRDVVAFRSCTRINAAALPEDPSSDSASDLSVVVNESDLAYMIYTSGSTGKP
KGVLVEHGSVNRLFAATRRLFGFHAEDVWTLYHSCAFDFSVWEIWGALLHGGSLVIVPAG
VTRSFEDFYRLLARERVTVLNQTPSAFKQLVHVEQHAGFEEAGELSLRYIIFGGEALELQ
SLRPWFRLHGDRRPQLINMYGITEITVHATFRPITLEDLDAGAGSVIGAPLPDLEAYILD
EHGQPVPLGVPGELYIGGRGVARGYWNREELTRERFIANPFASVSACGPRARLYRSGDLA
RWTAAGEIEYLGRRDEQVKVRGYRIELGEIESAVSDHELVSQSVVVAERNEHGDAQLTCY
VIPHKNELHAHGTLRQFKGELVERWETVFDSYYAKGNEHEDKTFHIVGWNDTYTGLPIPA
AEMEEWTSETVERILKYRPKRVLEIGCGTGLLLFRIAPSCESYIGTDLSENAIEYVSSHL
HLLGENRHKVSLFKCNAHELPDVDQVDMVILNSVVQYFPDVSYLNEVLQHVAGKLKPGGC
IFLGDICGLMFREAFHCSVVLNGVDERISLPEFNRLVLRKMKQHSELMLDTGYFAQLQRE
LTSIRTVEVLYKKGNYRNEMNKFRYDAVLHVGDKPVWETEALFEWSPDIKRQLREGKLCA
AHSSACFLVTGIPNGRLAEEWEFMRWRRQAAPADTIADYRRHFMRESPLSQWTDPADILQ
WGGQSHHVELLLSDDETCLDAIFMPYGEEKLTPCRYTGATKASLELASIPMQQEVEGRLA
ASIREELKQRLPDFMIPSQFVVLEQFPLTANGKIERAKLRELKPGRHLAEKETALDGAQH
FTDTELALREMWLGLLDAEHIGLEDSFFDMGGHSLLISRMMFQIRKQFQVQIPLVQLMQE
PTIKSIASQIERVLAQEEAGDGLDLASRIVLDPAIQAADIPQAVSMAEDEAVLLTGGTGF
FGAFLLHELLHSDSSRHVYCLVRAADRETGMRRIAEGMRKYGLWKDEYETRVTAVTGDLG
AARLGLDEKAYEFLTKEITSIFHNGAVVNFAQPYLALEAVNVKGCEEILRFAAAGAVKPI
HYISTLYVFSEKDAKIKKIILEDDVPVCSDALKLGYTQSKWVAEGVMREGRRRGIPVSMY
RLGRISGDSRTGACQDSDFFWKIIRFCLQLGAFPDIDFRFNLIPADFAADIIVRLASSRF
SNQTFHVMNDHDCSFKDITRMLAKRGYSFAHLPWMDWKARVSQSLEAGNDAGNDAGNAGG
LDISIVPFIEEMSISEGETPVFNADKVFSFLKERKLDCPQMDADRLAMYIDYFAASGYFE
PISV

Enzyme Prediction     

No EC number prediction in MGYG000002817_02127.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK05691	PRK05691	0.0	28	976	1712	2653	peptide synthase; Validated
cd17643	A_NRPS_Cytc1-like	0.0	516	981	1	421	similar to adenylation domain of cytotrienin synthetase CytC1. This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. 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.
PRK12467	PRK12467	0.0	34	963	41	960	peptide synthase; Provisional
PRK12316	PRK12316	0.0	7	963	18	953	peptide synthase; Provisional
PRK12467	PRK12467	0.0	33	963	1105	2024	peptide synthase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AXG41638.1	7.64e-217	47	1510	82	1539
AWK40831.1	7.64e-217	47	1510	82	1539
AXG46165.1	7.64e-217	47	1510	82	1539
BAY90071.1	1.64e-179	225	982	305	1050
BAZ00088.1	7.06e-173	225	982	306	1051

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6P1J_A	6.10e-160	47	962	8	916	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]
6OYF_A	3.85e-149	47	922	5	873	Thestructure of condensation and adenylation domains of teixobactin-producing nonribosomal peptide synthetase Txo1 serine module [Eleftheria terrae],6OZV_A The structure of condensation and adenylation domains of teixobactin-producing nonribosomal peptide synthetase Txo1 serine module in complex with AMP [Eleftheria terrae],6P4U_A The structure of condensation and adenylation domains of teixobactin-producing nonribosomal peptide synthetase Txo1 serine module in complex with Mg and AMP [Eleftheria terrae]
6P3I_A	3.60e-143	47	922	5	873	Thestructure of condensation and adenylation domains of teixobactin-producing nonribosomal peptide synthetase Txo1 serine module in complex with Mg [Eleftheria terrae]
6N8E_A	1.07e-133	43	967	28	945	Crystalstructure of holo-ObiF1, a five domain nonribosomal peptide synthetase from Burkholderia diffusa [Burkholderia diffusa]
5WMM_A	3.76e-126	492	1423	37	926	Crystalstructure of an adenylation domain interrupted by a methylation domain (AMA4) from nonribosomal peptide synthetase TioS [Micromonospora sp. ML1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q0VZ70	1.08e-240	38	1507	16	1478	Chondramide synthase cmdD OS=Chondromyces crocatus OX=52 GN=cmdD PE=1 SV=1
Q70LM4	2.33e-226	34	1917	3628	5075	Linear gramicidin synthase subunit D OS=Brevibacillus parabrevis OX=54914 GN=lgrD PE=1 SV=1
P45745	1.18e-197	39	982	1047	1995	Dimodular nonribosomal peptide synthase OS=Bacillus subtilis (strain 168) OX=224308 GN=dhbF PE=1 SV=4
Q70LM6	1.71e-181	27	981	3615	4557	Linear gramicidin synthase subunit B OS=Brevibacillus parabrevis OX=54914 GN=lgrB PE=1 SV=1
Q70LM5	7.92e-177	36	962	1065	1978	Linear gramicidin synthase subunit C OS=Brevibacillus parabrevis OX=54914 GN=lgrC PE=3 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
1.000075	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002817_02127.