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CAZyme Information: MGYG000001873_00009

You are here: Home > Sequence: MGYG000001873_00009

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
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Marvinbryantia;
CAZyme ID MGYG000001873_00009
CAZy Family GH51
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
502 MGYG000001873_1|CGC1 57469.56 4.9344
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001873 2665919 MAG Denmark Europe
Gene Location Start: 11634;  End: 13142  Strand: +

Full Sequence      Download help

MSDSMLKLYG  TRQRVTGRRD  PMIYGHFIEH  FHRQIYGGVY  DPGNPLSDED  GFRLDVIDAM60
RKIKVPILRW  PGGCFVSSYH  WKDAVGENRS  PMFDKAWRVE  DPNTFGTDEY  IRLCRKIGCE120
PYICTNAGTG  TAEEMSDWVE  YCNLENEGQY  AKWRIQNGFQ  QPHKVRYWSI  GNENYGFWEI180
GAKTAGEWGH  LVCETAKMIK  HVDPDTELTA  AALTDLNWNV  RLLESSGQFL  DWISIHEYWD240
AIQQTNDYAD  YGAVCAYTNN  IDHSIREVHG  LLTAMKLDKK  IRIAFDEWNL  RGWYHPNVHT300
IEQGRTKEDY  LYPRDKNDDN  SRYTMADAVF  TACFLNACNR  HCDIVGMANF  APIVNTRGCI360
FTYPEGIVLR  TTYHVFDLYV  NYLGDTVLDG  WSTDMPRITV  RDKQGNTQET  DVCDFAVTCF420
SDREGLAVAL  VNKDPTNEQP  VQLMLEAAGE  AVLYYIAGES  TDAYNDIRHT  EVEIQRESLG480
SYTPGMTIRL  GPHMVGVLQI  GL502

Enzyme Prediction      help

No EC number prediction in MGYG000001873_00009.

CAZyme Signature Domains help

Created with Snap25507510012515017520022525127630132635137640142645147613499GH51
Family Start End Evalue family coverage
GH51 13 499 3.6e-107 0.7126984126984127

CDD Domains      download full data without filtering help

Created with Snap25507510012515017520022525127630132635137640142645147617502AbfA286472Alpha-L-AF_C286465Alpha-L-AF_C
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3534 AbfA 2.81e-123 17 502 15 500
Alpha-L-arabinofuranosidase [Carbohydrate transport and metabolism].
pfam06964 Alpha-L-AF_C 5.60e-30 286 472 1 168
Alpha-L-arabinofuranosidase C-terminal domain. This family represents the C-terminus (approximately 200 residues) of bacterial and eukaryotic alpha-L-arabinofuranosidase (EC:3.2.1.55). This catalyzes the hydrolysis of nonreducing terminal alpha-L-arabinofuranosidic linkages in L-arabinose-containing polysaccharides.
smart00813 Alpha-L-AF_C 6.59e-26 286 465 1 158
Alpha-L-arabinofuranosidase C-terminus. This entry represents the C terminus (approximately 200 residues) of bacterial and eukaryotic alpha-L-arabinofuranosidase. This catalyses the hydrolysis of non-reducing terminal alpha-L-arabinofuranosidic linkages in L-arabinose-containing polysaccharides.

CAZyme Hits      help

Created with Snap2550751001251501752002252512763013263513764014264514766500QBE94709.1|GH516500QIB56385.1|GH516500QMW80840.1|GH516501QJU16949.1|GH515499AEF80325.1|GH51
Hit ID E-Value Query Start Query End Hit Start Hit End
QBE94709.1 2.56e-276 6 500 1 496
QIB56385.1 7.33e-276 6 500 1 496
QMW80840.1 7.33e-276 6 500 1 496
QJU16949.1 1.07e-270 6 501 1 506
AEF80325.1 4.23e-230 5 499 1 494

PDB Hits      download full data without filtering help

Created with Snap255075100125150175200225251276301326351376401426451476234723S2C_A234724ATW_A234723UG3_A203841PZ3_A203841PZ2_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
3S2C_A 6.96e-95 23 472 20 453
Structureof the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_B Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_C Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_D Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_E Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_F Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_G Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_H Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_I Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_J Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_K Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_L Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1]
4ATW_A 9.27e-95 23 472 20 453
Thecrystal structure of Arabinofuranosidase [Thermotoga maritima MSB8],4ATW_B The crystal structure of Arabinofuranosidase [Thermotoga maritima MSB8],4ATW_C The crystal structure of Arabinofuranosidase [Thermotoga maritima MSB8],4ATW_D The crystal structure of Arabinofuranosidase [Thermotoga maritima MSB8],4ATW_E The crystal structure of Arabinofuranosidase [Thermotoga maritima MSB8],4ATW_F The crystal structure of Arabinofuranosidase [Thermotoga maritima MSB8]
3UG3_A 1.73e-94 23 472 40 473
Crystalstructure of alpha-L-arabinofuranosidase from Thermotoga maritima ligand free form [Thermotoga maritima],3UG3_B Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima ligand free form [Thermotoga maritima],3UG3_C Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima ligand free form [Thermotoga maritima],3UG3_D Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima ligand free form [Thermotoga maritima],3UG3_E Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima ligand free form [Thermotoga maritima],3UG3_F Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima ligand free form [Thermotoga maritima],3UG4_A Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima arabinose complex [Thermotoga maritima],3UG4_B Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima arabinose complex [Thermotoga maritima],3UG4_C Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima arabinose complex [Thermotoga maritima],3UG4_D Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima arabinose complex [Thermotoga maritima],3UG4_E Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima arabinose complex [Thermotoga maritima],3UG4_F Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima arabinose complex [Thermotoga maritima],3UG5_A Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima xylose complex [Thermotoga maritima],3UG5_B Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima xylose complex [Thermotoga maritima],3UG5_C Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima xylose complex [Thermotoga maritima],3UG5_D Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima xylose complex [Thermotoga maritima],3UG5_E Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima xylose complex [Thermotoga maritima],3UG5_F Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima xylose complex [Thermotoga maritima]
1PZ3_A 6.99e-77 20 384 20 383
Crystalstructure of a family 51 (GH51) alpha-L-arabinofuranosidase from Geobacillus stearothermophilus T6 [Geobacillus stearothermophilus],1PZ3_B Crystal structure of a family 51 (GH51) alpha-L-arabinofuranosidase from Geobacillus stearothermophilus T6 [Geobacillus stearothermophilus],6SXU_AAA Chain AAA, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Geobacillus stearothermophilus],6SXU_BBB Chain BBB, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Geobacillus stearothermophilus],6SXV_A GH51 a-l-arabinofuranosidase soaked with aziridine inhibitor [Geobacillus stearothermophilus],6SXV_B GH51 a-l-arabinofuranosidase soaked with aziridine inhibitor [Geobacillus stearothermophilus]
1PZ2_A 5.35e-76 20 384 20 383
ChainA, Alpha-L-arabinofuranosidase [Geobacillus stearothermophilus],1PZ2_B Chain B, Alpha-L-arabinofuranosidase [Geobacillus stearothermophilus],1QW8_A Chain A, Alpha-L-arabinofuranosidase [Geobacillus stearothermophilus],1QW8_B Chain B, Alpha-L-arabinofuranosidase [Geobacillus stearothermophilus],1QW9_A Chain A, Alpha-L-arabinofuranosidase [Geobacillus stearothermophilus],1QW9_B Chain B, Alpha-L-arabinofuranosidase [Geobacillus stearothermophilus]

Swiss-Prot Hits      download full data without filtering help

Created with Snap25507510012515017520022525127630132635137640142645147620384sp|Q9XBQ3|IABF_GEOSE20366sp|A3DIH0|IABF_ACET214465sp|A1CQC3|ABFC_ASPCL17500sp|P94531|IABF1_BACSU17459sp|Q9KBR4|IABF_ALKHC
Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q9XBQ3 3.83e-76 20 384 20 383
Intracellular exo-alpha-(1->5)-L-arabinofuranosidase OS=Geobacillus stearothermophilus OX=1422 GN=abfA PE=1 SV=4
A3DIH0 1.01e-71 20 366 18 366
Intracellular exo-alpha-(1->5)-L-arabinofuranosidase OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=Cthe_2548 PE=1 SV=1
A1CQC3 1.49e-71 14 465 21 470
Probable alpha-L-arabinofuranosidase C OS=Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) OX=344612 GN=abfC PE=3 SV=2
P94531 2.59e-71 17 500 15 496
Intracellular exo-alpha-(1->5)-L-arabinofuranosidase 1 OS=Bacillus subtilis (strain 168) OX=224308 GN=abfA PE=1 SV=2
Q9KBR4 7.14e-71 17 459 16 454
Intracellular exo-alpha-(1->5)-L-arabinofuranosidase OS=Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) OX=272558 GN=abfA PE=3 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
1.000051 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001873_00009.