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CAZyme Information: MGYG000001276_00656

You are here: Home > Sequence: MGYG000001276_00656

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 Eubacterium limosum
Lineage Bacteria; Firmicutes_A; Clostridia; Eubacteriales; Eubacteriaceae; Eubacterium; Eubacterium limosum
CAZyme ID MGYG000001276_00656
CAZy Family CE9
CAZyme Description N-acetylglucosamine-6-phosphate deacetylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
370 MGYG000001276_4|CGC1 39365.34 7.0525
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001276 3903827 MAG Italy Europe
Gene Location Start: 126652;  End: 127764  Strand: +

Full Sequence      Download help

MIIRNAWVYT  PDHRFLKKDL  ILDGPCIGSR  TADPAEMDAF  GLYAIPGLTD  IHLHGCMGRD60
FCDAAADTLK  SIAAYQAHSG  VTSFVPASMT  FSEKRLSGIL  ENAARRTQEA  GAMLLGVNLE120
GPFLAEKKKG  AQNARYLMPP  DIPMFRRLNA  ISGGRIKLVT  LAPELPGASE  FITALKDETI180
ISLGHTEAGF  ETASKAFDLG  ASHVTHLFNA  MQSFNHREPG  LVGAAFDHPG  VTAELICDGV240
HVAPAMVRAA  FRLFSAERIV  LISDSMRATG  LDDGDYTLGG  QAVHVRGNRA  TLADGTLAGS300
VTNLMDCLRN  AVAFGIPLAE  AVRAAAVNPA  RVIGESDRLG  SLEPGKLANV  VLLDKSLNVV360
KVFVKGKSMV  370

Enzyme Prediction      help

No EC number prediction in MGYG000001276_00656.

CAZyme Signature Domains help

Created with Snap18375574921111291481661852032222402592772963143333514366CE9
Family Start End Evalue family coverage
CE9 4 366 1.7e-126 0.9946380697050938

CDD Domains      download full data without filtering help

Created with Snap18375574921111291481661852032222402592772963143333511366NagA1367NagA36367nagA5367nagA43367Amidohydro_1
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd00854 NagA 1.72e-146 1 366 1 374
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling.
COG1820 NagA 2.36e-132 1 367 2 376
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism].
TIGR00221 nagA 7.66e-106 36 367 46 380
N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars]
PRK11170 nagA 9.07e-74 5 367 6 377
N-acetylglucosamine-6-phosphate deacetylase; Provisional
pfam01979 Amidohydro_1 8.01e-23 43 367 1 333
Amidohydrolase family. This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyzes adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilisation as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included.

CAZyme Hits      help

Created with Snap18375574921111291481661852032222402592772963143333511370ARD64548.1|CE91370ADO39468.1|CE91366ALU16578.1|CE91366QCT72192.1|CE91367QIA31363.1|CE9
Hit ID E-Value Query Start Query End Hit Start Hit End
ARD64548.1 2.12e-253 1 370 1 370
ADO39468.1 1.23e-227 1 370 1 371
ALU16578.1 1.71e-220 1 366 1 366
QCT72192.1 3.45e-220 1 366 1 366
QIA31363.1 1.69e-143 1 367 1 369

PDB Hits      download full data without filtering help

Created with Snap1837557492111129148166185203222240259277296314333351453662VHL_A33673EGJ_A323676FV3_A323676FV4_A463671O12_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
2VHL_A 3.78e-77 45 366 56 384
TheThree-dimensional structure of the N-Acetylglucosamine-6- phosphate deacetylase from Bacillus subtilis [Bacillus subtilis],2VHL_B The Three-dimensional structure of the N-Acetylglucosamine-6- phosphate deacetylase from Bacillus subtilis [Bacillus subtilis]
3EGJ_A 1.09e-57 3 367 7 377
N-acetylglucosamine-6-phosphatedeacetylase from Vibrio cholerae. [Vibrio cholerae],3EGJ_B N-acetylglucosamine-6-phosphate deacetylase from Vibrio cholerae. [Vibrio cholerae],3IV8_A N-acetylglucosamine-6-phosphate deacetylase from Vibrio cholerae complexed with fructose 6-phosphate [Vibrio cholerae],3IV8_B N-acetylglucosamine-6-phosphate deacetylase from Vibrio cholerae complexed with fructose 6-phosphate [Vibrio cholerae],3IV8_C N-acetylglucosamine-6-phosphate deacetylase from Vibrio cholerae complexed with fructose 6-phosphate [Vibrio cholerae],3IV8_D N-acetylglucosamine-6-phosphate deacetylase from Vibrio cholerae complexed with fructose 6-phosphate [Vibrio cholerae]
6FV3_A 3.56e-52 32 367 50 390
Crystalstructure of N-acetyl-D-glucosamine-6-phosphate deacetylase from Mycobacterium smegmatis. [Mycolicibacterium smegmatis MC2 155],6FV3_B Crystal structure of N-acetyl-D-glucosamine-6-phosphate deacetylase from Mycobacterium smegmatis. [Mycolicibacterium smegmatis MC2 155],6FV3_C Crystal structure of N-acetyl-D-glucosamine-6-phosphate deacetylase from Mycobacterium smegmatis. [Mycolicibacterium smegmatis MC2 155],6FV3_D Crystal structure of N-acetyl-D-glucosamine-6-phosphate deacetylase from Mycobacterium smegmatis. [Mycolicibacterium smegmatis MC2 155]
6FV4_A 5.29e-51 32 367 50 390
Thestructure of N-acetyl-D-glucosamine-6-phosphate deacetylase D267A mutant from Mycobacterium smegmatis in complex with N-acetyl-D-glucosamine-6-phosphate [Mycolicibacterium smegmatis MC2 155],6FV4_B The structure of N-acetyl-D-glucosamine-6-phosphate deacetylase D267A mutant from Mycobacterium smegmatis in complex with N-acetyl-D-glucosamine-6-phosphate [Mycolicibacterium smegmatis MC2 155]
1O12_A 5.80e-51 46 367 55 370
Crystalstructure of N-acetylglucosamine-6-phosphate deacetylase (TM0814) from Thermotoga maritima at 2.5 A resolution [Thermotoga maritima],1O12_B Crystal structure of N-acetylglucosamine-6-phosphate deacetylase (TM0814) from Thermotoga maritima at 2.5 A resolution [Thermotoga maritima]

Swiss-Prot Hits      download full data without filtering help

Created with Snap183755749211112914816618520322224025927729631433335145366sp|O34450|NAGA_BACSU46367sp|Q8XAC3|AGAA_ECO571357sp|Q84F86|NAGA_LYSSH28367sp|P96166|NAGA_VIBFU3367sp|O32445|NAGA_VIBCH
Hit ID E-Value Query Start Query End Hit Start Hit End Description
O34450 2.07e-76 45 366 56 384
N-acetylglucosamine-6-phosphate deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=nagA PE=1 SV=1
Q8XAC3 7.44e-65 46 367 49 373
N-acetylgalactosamine-6-phosphate deacetylase OS=Escherichia coli O157:H7 OX=83334 GN=agaA PE=1 SV=2
Q84F86 1.80e-61 1 357 6 370
N-acetylglucosamine-6-phosphate deacetylase OS=Lysinibacillus sphaericus OX=1421 GN=nagA PE=2 SV=1
P96166 2.67e-60 28 367 43 383
N-acetylglucosamine-6-phosphate deacetylase OS=Vibrio furnissii OX=29494 GN=manD PE=3 SV=1
O32445 5.55e-57 3 367 4 374
N-acetylglucosamine-6-phosphate deacetylase OS=Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) OX=243277 GN=nagA PE=1 SV=2

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
1.000072 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001276_00656.