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CAZyme Information: MGYG000001159_00265

You are here: Home > Sequence: MGYG000001159_00265

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 Bifidobacterium pullorum
Lineage Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Bifidobacteriaceae; Bifidobacterium; Bifidobacterium pullorum
CAZyme ID MGYG000001159_00265
CAZy Family CE9
CAZyme Description N-acetylgalactosamine-6-phosphate deacetylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
418 MGYG000001159_12|CGC1 44335.25 5.1441
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001159 2232439 MAG Austria Europe
Gene Location Start: 147939;  End: 149195  Strand: -

Full Sequence      Download help

MDQNRMDIVR  RVTAAVTGEP  ERIAIRGARK  VDARGVLEHC  WVTSANGVIT  ATGTSDEEFE60
HACRAIAVDP  ADESSIIEAD  GRLLTPGYVD  IHAHGSWERS  FDDGPEGIDI  ARAGHTVHGT120
TRQVCSLITN  PIDVMCENLR  NVRAAMDRRP  DVLGSHLEGP  FLALARKGAH  DPECLKDPVP180
ELVDELLDAA  DGSLRQITIA  PELPHGIGAI  RQFAAAGVVP  AVGHCDADYA  MAKRGFDAGA240
GIVTHMFNAM  NGLHHREPGP  IPAAVEDPRV  TIEIINDGFH  VQDPMVRLGF  GFAPHRTAFV300
TDAMAATDCP  DGPYKLGALD  VNVVDGHARL  VSNGAIAGST  LLLEVAVRRA  VTVLGISAVD360
AVEAATLTPA  RTFGYDRPNP  VTGAPLGLVA  PGYAADLLLT  DPATWTVGEV  WCAGRKLR418

Enzyme Prediction      help

No EC number prediction in MGYG000001159_00265.

CAZyme Signature Domains help

Created with Snap2041628310412514616718820922925027129231333435537639726414CE9
Family Start End Evalue family coverage
CE9 26 414 2.7e-113 0.9946380697050938

CDD Domains      download full data without filtering help

Created with Snap2041628310412514616718820922925027129231333435537639723414NagA22416NagA20402nagA77397nagA83402Amidohydro_1
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd00854 NagA 4.44e-136 23 414 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 7.77e-105 22 416 1 377
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism].
TIGR00221 nagA 2.83e-71 20 402 2 368
N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars]
PRK11170 nagA 5.86e-55 77 397 44 360
N-acetylglucosamine-6-phosphate deacetylase; Provisional
pfam01979 Amidohydro_1 1.29e-11 83 402 1 310
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 Snap204162831041251461671882092292502712923133343553763971418QAY32584.1|CE91418BAQ31863.1|CE91418ALE11020.1|CE91418ADO52796.1|CE91418AXM91999.1|CE9
Hit ID E-Value Query Start Query End Hit Start Hit End
QAY32584.1 2.64e-285 1 418 1 418
BAQ31863.1 6.00e-259 1 418 1 418
ALE11020.1 1.72e-258 1 418 1 418
ADO52796.1 1.72e-258 1 418 1 418
AXM91999.1 1.72e-258 1 418 1 418

PDB Hits      download full data without filtering help

Created with Snap20416283104125146167188209229250271292313334355376397844016FV3_A844016FV4_A374013EGJ_A804021YMY_A804022P53_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
6FV3_A 1.12e-63 84 401 64 377
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 1.71e-62 84 401 64 377
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]
3EGJ_A 5.79e-39 37 401 7 364
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]
1YMY_A 1.14e-38 80 402 47 365
CrystalStructure of the N-Acetylglucosamine-6-phosphate deacetylase from Escherichia coli K12 [Escherichia coli K-12],1YMY_B Crystal Structure of the N-Acetylglucosamine-6-phosphate deacetylase from Escherichia coli K12 [Escherichia coli K-12],1YRR_A Crystal Structure Of The N-Acetylglucosamine-6-Phosphate Deacetylase From Escherichia Coli K12 at 2.0 A Resolution [Escherichia coli],1YRR_B Crystal Structure Of The N-Acetylglucosamine-6-Phosphate Deacetylase From Escherichia Coli K12 at 2.0 A Resolution [Escherichia coli],2P50_A Crystal structure of N-acetyl-D-Glucosamine-6-Phosphate deacetylase liganded with Zn [Escherichia coli K-12],2P50_B Crystal structure of N-acetyl-D-Glucosamine-6-Phosphate deacetylase liganded with Zn [Escherichia coli K-12],2P50_C Crystal structure of N-acetyl-D-Glucosamine-6-Phosphate deacetylase liganded with Zn [Escherichia coli K-12],2P50_D Crystal structure of N-acetyl-D-Glucosamine-6-Phosphate deacetylase liganded with Zn [Escherichia coli K-12]
2P53_A 5.87e-38 80 402 47 365
ChainA, N-acetylglucosamine-6-phosphate deacetylase [Escherichia coli K-12],2P53_B Chain B, N-acetylglucosamine-6-phosphate deacetylase [Escherichia coli K-12]

Swiss-Prot Hits      download full data without filtering help

Created with Snap2041628310412514616718820922925027129231333435537639742415sp|Q8XAC3|AGAA_ECO5746415sp|P96166|NAGA_VIBFU77401sp|Q84F86|NAGA_LYSSH77417sp|Q6P0U0|NAGA_DANRE37401sp|O32445|NAGA_VIBCH
Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8XAC3 6.34e-54 42 415 4 373
N-acetylgalactosamine-6-phosphate deacetylase OS=Escherichia coli O157:H7 OX=83334 GN=agaA PE=1 SV=2
P96166 3.14e-43 46 415 32 383
N-acetylglucosamine-6-phosphate deacetylase OS=Vibrio furnissii OX=29494 GN=manD PE=3 SV=1
Q84F86 6.87e-40 77 401 47 367
N-acetylglucosamine-6-phosphate deacetylase OS=Lysinibacillus sphaericus OX=1421 GN=nagA PE=2 SV=1
Q6P0U0 6.91e-39 77 417 56 401
N-acetylglucosamine-6-phosphate deacetylase OS=Danio rerio OX=7955 GN=amdhd2 PE=2 SV=1
O32445 2.98e-38 37 401 4 361
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
1.000052 0.000004 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001159_00265.