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CAZyme Information: MGYG000002490_03177

You are here: Home > Sequence: MGYG000002490_03177

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Paenibacillus_B thiaminolyticus
Lineage Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_B; Paenibacillus_B thiaminolyticus
CAZyme ID MGYG000002490_03177
CAZy Family GT2
CAZyme Description D-alanine--poly(phosphoribitol) ligase subunit 1
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
3074 MGYG000002490_29|CGC3 340069.34 5.5202
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002490 6537383 Isolate Japan Asia
Gene Location Start: 117873;  End: 127097  Strand: +

Full Sequence      Download help

MQEPQKLDKS  NVEDILALTP  MQSGMLLQYL  KDPDTTQYVE  LIELGISGDI  DTSLFEQSWS60
CVVQANEALR  TLFRWEEVNQ  PVQIVLKQHR  PVIRYENYSE  LDEEARARQI  AARIAADRQE120
KFKLDQVPFR  LTLCKQTGRN  HTLLISFHHI  LLDGWSTGIL  LKEWLGAYRM  LAQGMKPELR180
RKPPFKQFVA  LLQQQDKKKQ  ASYWSRYLHE  LEAKPIPVSR  GGASPEKASI  AVHTEKRSGT240
YVADLHRFAR  TAQVTQAALF  YTAWGILLQH  YTNSDDVLFG  VTVSGRNTSI  SGMEDMAGLF300
INTLPLRLKA  GPEHGLPDLL  ADVNRSIQAH  EEHAGTSLTD  IKGYGGMRTE  GVPFDSLLVV360
ENYPLDKAVT  SAEGPLAIAS  HHIEEETEFD  LTVRITAAEE  LEMTFAYNEQ  AHRSDTVAKL420
ACHYLYIIEQ  IIQTSTQVTA  YHETRLQDIG  ILTAEEREQI  RHFNLTTASY  PREKTIHELF480
EEQVRLAPEG  TAVTDEQRSC  TYRELNEQAN  RIARALRADG  VERGQVVGLM  ANRSIDMIAG540
IFGILKAGGV  YLPLDSAHPA  ERIAYMLQDG  KVGTVLASAG  LEPLVPEQTK  VWVLNEALLG600
CGEATDMPSV  NGPEHPAYVM  YTSGSTGTPK  GVAVGHRNVV  RLVRNTNYVQ  VEAGDCMLQA660
GAIGFDALTF  EVFGALLNGG  SLHIADKHTL  LDSSRLDAFL  RSRNISVALL  TPALFNQLAQ720
QRPQMFAGLR  HLIVGGDVLS  PKHIEAVRQA  CPGLAMWNAY  GPTENTVIST  CFRIDREYAE780
HIPIGPPISN  STAYIVDRHD  NLLPIGVPGE  LLVGGDGVAL  GYLNQPELTS  EKFVPDPYCP840
GGVMYRTGDM  ACWQEDGSLE  YMGRIDQQVK  IRGHRIEIGE  IETMLLRHPS  VQEAAVTALQ900
RGGHTELCAY  VVASGQAPVS  ELRDYLAATL  PDYMIPSHVV  PLEHIPLTPN  GKLDRKALPA960
PAERVRSARD  AALPRTELER  LIAEAWQAVL  ELESVSIHDK  YFEVGGNSIN  LIQLQSKLQR1020
QLKREVPIVT  LFQYPTVHEL  AAHLAGEADG  TRGRASEQAA  ASREDEPHSQ  AAAGSARPGN1080
EGSRDIAVIG  MAGRFPGARS  IAEFWSNLQQ  GQESISFFTD  DELAEYGFDR  DLLQRPEFVK1140
AKGVLDEMDH  FDPAFFGYTP  DQAAIMDPQV  RLLHECAWHA  LEDAGCDPER  YGGSIGLFAG1200
VTNNFHWLSQ  LSERLHGNLS  DMFEVDSLND  TYTVSTRISH  KLNLRGPAIS  LQTACSTSLV1260
AVHVACQSIL  SGDCDLALAG  GASIVLPHKS  GYLYQEGMVK  SPDGHCRSFD  AQAKGTIGGD1320
GVGFVALKPL  EAAKKDGDRI  YAVIKGSAIN  NDGSRKVGYT  APSVEGQMDV  IKRALAAAQV1380
PSDSITYVEA  HGSGTPLGDP  IEIEALTKAF  QTDRTGFCRI  GSVKTNIGHL  DAAAGVAGLM1440
KTALALHHKR  IPQSLHFETP  NPNIDFANSP  FVVNTALAEW  RNDAGPLRAG  VSSFGIGGTN1500
AHVILEEAPT  REAGGDGRSS  QLLALSARTP  AALDAMTANL  GAYLDERREL  CLADVAYTLQ1560
SGRRHFKYRR  ILSCDTIGEA  IEALTPVEGR  NSFDERKVVT  FAADDGGSPV  VFMFSGQGSQ1620
YVNMGADLYR  DEPVFRAEMD  RCFRLYRDIA  GRDMKEILYP  SGDAEAAALQ  LNQTKHIQPV1680
MFMFEYALAR  LVMAWGVKPE  AMIGYSFGEF  TAACLADVMS  LEDAMRLIIL  RGELMQQVPA1740
GAMLSVPLPE  QEVRLRLDGS  LSLAVVNGPS  CIVSGTEEEI  AAFEHRMKAE  KIMCMRLPVA1800
TAGHSSLLHA  VKEPFAAAMR  QVRLRPPALP  YVSTTTGTWI  TAEEAADPDY  WIRHLTDTVR1860
FADGMALLVQ  EPRRLFVEIG  PGHDLTLLAR  RHLGSGREQQ  ALNLVRPAQR  GGSDSALLVN1920
RIGRLWLHGQ  SIDWQAFHGE  VRAIISLPSY  PFARERYWPQ  ASGGALAAPG  TARSKGRPAS1980
GQMGKQTDMS  DWFYVPTWKK  SPTAASRKGD  AAASWKEDTA  GNWLVFADGA  GLAADLVKHL2040
SERGAQVVTV  RAGERFEQEG  TMQYTVHPRN  ERHYAKLFSE  LQADGRLPNR  MLHAWGVSAP2100
SRSDQQWIRT  AQDLGFYSVL  YTAKALKQQQ  AREEMRMWVV  TDSMHAIAGE  PVLYPEKATV2160
LGPCRVIPQE  LPHIQCRSID  IVLPEAGSWQ  RDRLVGRLLD  EFGAAGTELA  VAYRDNARWV2220
LDYEPFTISE  PEAQTQGPRQ  GGVYLITGGL  GYIGHTLGGY  LARSVQAKLA  LTSRSLFPPR2280
AEWDTWLSVH  GKEDAVSVQI  GKLRQLEAQG  AEVLVLSADA  ADQGQMETVI  RQAEAAFGPL2340
NGVIHAAGMT  GDAAFRMLEE  TDELLCEQHF  RAKMYGLLVL  EQVLAGKELD  FCLLASSLSP2400
MLGGLGFSAY  AAANHFMDAF  VHDRNRRQRI  PWTSVNWDGW  QLEADQTIRG  QAGASISELL2460
IAPAEGVELL  RRLLSVRDMS  QIVISTGDLG  ARIDKWVRRE  GQQEEPEAFR  HGEGSYYSRP2520
ALSGEYVAPA  TETERKLCGM  WEQFFRIDRI  GVQDDFFELG  GDSLKAITVV  SAIHKELSVE2580
IGLPVFFNMP  TIQQLSAYID  GAERSAYHDI  ESAEAKDYYE  LSSAQKRLYL  IQQMEQGHTG2640
YNEIVAGVLE  GRLDRTRLEA  ALRRLVERHE  SLRTSFELVN  GKPMQKINEA  VAIELEYEDY2700
SAAVTPLDSL  DGEEKMDDRI  RAAVATFVRS  FDLTRAPLMR  AGLIKLGEER  HVLMVDLHHI2760
VSDGLSQDIF  VNDFLALYAG  RELPELPLQY  KDFSEWQNRM  MDTDEMKRQG  AFWLERLKDA2820
PRLSLRTDYP  RPDTRSFAGS  LVPFELDAER  TQGLKSLCLK  EDVTLFMALL  AIFNLLLAKV2880
CGQDDIVVGT  PVVGRKQQAL  QLIVGKFVNM  LPLRNRLQEE  MSFRNLLQAV  RSTTLDAFAH2940
QDFQFEEMVQ  QAGRERELGR  NPIFDVVFAL  QNMQNPEMSI  PGLILKPFPF  IHDASHFDLS3000
LIAEEDGDRL  AFKFEYSTRL  FQRDTIDRFA  AYLQDIVFDV  LAHPDKKIQE  IKIAHHLAEP3060
EAVFLAGAQG  EFGL3074

Enzyme Prediction      help

No EC number prediction in MGYG000002490_03177.

CDD Domains      download full data without filtering help

Created with Snap1533074616147689221075122913831537169018441998215123052459261227662920478958A_NRPS_Srf_like488958A_NRPS71115PRK12316321053PRK12467321051PRK12467
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd12117 A_NRPS_Srf_like 0.0 478 958 1 483
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C). 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 adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
cd05930 A_NRPS 0.0 488 958 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.
PRK12316 PRK12316 0.0 7 1115 1548 2668
peptide synthase; Provisional
PRK12467 PRK12467 0.0 32 1053 66 1106
peptide synthase; Provisional
PRK12467 PRK12467 0.0 32 1051 1133 2169
peptide synthase; Provisional

CAZyme Hits      help

Created with Snap15330746161476892210751229138315371690184419982151230524592612276629201633061BAY90071.1|GT22453061BAY30132.1|GT22453053BAZ00088.1|GT22453053BAZ75991.1|GT24491958AFY93865.1|GT2
Hit ID E-Value Query Start Query End Hit Start Hit End
BAY90071.1 0.0 163 3061 269 2678
BAY30132.1 0.0 245 3061 361 2689
BAZ00088.1 0.0 245 3053 361 2682
BAZ75991.1 0.0 245 3053 361 2682
AFY93865.1 0.0 449 1958 305 1861

PDB Hits      download full data without filtering help

Created with Snap1533074616147689221075122913831537169018441998215123052459261227662920610502VSQ_A108619584MZ0_A108324407S6C_A108625997M7J_A108625997M7I_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
2VSQ_A 1.26e-179 6 1050 3 1046
Structureof surfactin A synthetase C (SrfA-C), a nonribosomal peptide synthetase termination module [Bacillus subtilis]
4MZ0_A 9.81e-167 1086 1958 41 935
ChainA, CurL [Moorena producens 3L],4MZ0_B Chain B, CurL [Moorena producens 3L]
7S6C_A 1.64e-158 1083 2440 31 1372
ChainA, 6-deoxyerythronolide-B synthase EryA2, modules 3 and 4, Lsd14 Polyketide synthase fusion [synthetic construct],7S6C_B Chain B, 6-deoxyerythronolide-B synthase EryA2, modules 3 and 4, Lsd14 Polyketide synthase fusion [synthetic construct],7S6C_C Chain C, 6-deoxyerythronolide-B synthase EryA2, modules 3 and 4, Lsd14 Polyketide synthase fusion [synthetic construct],7S6C_D Chain D, 6-deoxyerythronolide-B synthase EryA2, modules 3 and 4, Lsd14 Polyketide synthase fusion [synthetic construct],7S6D_A Chain A, 6-deoxyerythronolide-B synthase EryA2, modules 3 and 4, Lsd14 Polyketide synthase fusion [synthetic construct],7S6D_B Chain B, 6-deoxyerythronolide-B synthase EryA2, modules 3 and 4, Lsd14 Polyketide synthase fusion [synthetic construct],7S6D_C Chain C, 6-deoxyerythronolide-B synthase EryA2, modules 3 and 4, Lsd14 Polyketide synthase fusion [synthetic construct]
7M7J_A 7.95e-155 1086 2599 35 1485
ChainA, EryAI [Saccharopolyspora erythraea],7M7J_B Chain B, EryAI [Saccharopolyspora erythraea]
7M7I_A 7.95e-155 1086 2599 35 1485
ChainA, EryAI [Saccharopolyspora erythraea],7M7I_B Chain B, EryAI [Saccharopolyspora erythraea]

Swiss-Prot Hits      download full data without filtering help

Created with Snap1533074616147689221075122913831537169018441998215123052459261227662920443067sp|O30409|TYCC_BREPA133051sp|P0C064|GRSB_BREBE133051sp|P0C063|GRSB_ANEMI73051sp|Q04747|SRFAB_BACSU93053sp|O30408|TYCB_BREPA
Hit ID E-Value Query Start Query End Hit Start Hit End Description
O30409 2.39e-278 44 3067 3159 5644
Tyrocidine synthase 3 OS=Brevibacillus parabrevis OX=54914 GN=tycC PE=1 SV=1
P0C064 3.43e-271 13 3051 1059 3562
Gramicidin S synthase 2 OS=Brevibacillus brevis OX=1393 GN=grsB PE=1 SV=2
P0C063 1.68e-268 13 3051 1059 3563
Gramicidin S synthase 2 OS=Aneurinibacillus migulanus OX=47500 GN=grsB PE=3 SV=2
Q04747 1.00e-266 7 3051 1 2515
Surfactin synthase subunit 2 OS=Bacillus subtilis (strain 168) OX=224308 GN=srfAB PE=1 SV=3
O30408 1.22e-260 9 3053 6 2520
Tyrocidine synthase 2 OS=Brevibacillus parabrevis OX=54914 GN=tycB PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000047 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002490_03177.