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CAZyme Information: MGYG000001356_00440

You are here: Home > Sequence: MGYG000001356_00440

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 Lawsonibacter sp000177015
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; Lawsonibacter; Lawsonibacter sp000177015
CAZyme ID MGYG000001356_00440
CAZy Family CE9
CAZyme Description N-acetylglucosamine-6-phosphate deacetylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
371 MGYG000001356_1|CGC2 39084.62 5.503
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001356 3197155 Isolate not provided not provided
Gene Location Start: 464911;  End: 466026  Strand: -

Full Sequence      Download help

MIIGNANVFV  DGKFQKGSVA  VENGVITAIG  PAGWPCDVDA  QGKYLVPGFI  DVHTHGAMNE60
DFSDGKPEGL  PAMSKHYAAH  GVTSFLATTM  TLKEEVLTPA  METIRGFVRP  ADGAKCAGIH120
LEGPFLSYAK  RGAQAAENLH  KPDAEMFHRL  NAASGGQVRL  VTVAPEEEGA  IPFIEEVSKV180
CTVSIGHTTA  NYETAMAAYA  AGASHATHLY  NGMPSLLHRE  PGVIAAALDS  GATVELICDG240
LHIHPAVIRA  THRMFGKKLV  IISDSLRCAG  MPDGQYELGG  QPIEMKNGRA  TLLGTDTLAG300
SSSNLLQELQ  NVVSFGLPLE  DAITALTSAP  AKAVRLDHEI  GSIAVGKKAD  LLLLTEDLEL360
DSVYIDGNKI  I371

Enzyme Prediction      help

No EC number prediction in MGYG000001356_00440.

CAZyme Signature Domains help

Created with Snap18375574921111291481661852042222412592782963153333525367CE9
Family Start End Evalue family coverage
CE9 5 367 2.7e-124 0.9919571045576407

CDD Domains      download full data without filtering help

Created with Snap18375574921111291481661852042222412592782963153333521349NagA1370NagA13349nagA18349nagA44349Amidohydro_1
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd00854 NagA 1.54e-125 1 349 1 356
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 7.53e-110 1 370 2 378
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism].
TIGR00221 nagA 4.09e-82 13 349 18 361
N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars]
PRK11170 nagA 1.03e-57 18 349 20 358
N-acetylglucosamine-6-phosphate deacetylase; Provisional
pfam01979 Amidohydro_1 4.15e-16 44 349 1 303
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 Snap18375574921111291481661852042222412592782963153333521369QNM02260.1|CE939370QIA31363.1|CE939370ANU41013.1|CE939370QQR06201.1|CE91370QRT50058.1|CE9
Hit ID E-Value Query Start Query End Hit Start Hit End
QNM02260.1 1.07e-107 1 369 1 373
QIA31363.1 5.51e-107 39 370 38 371
ANU41013.1 5.51e-107 39 370 38 371
QQR06201.1 5.51e-107 39 370 38 371
QRT50058.1 4.89e-106 1 370 1 374

PDB Hits      download full data without filtering help

Created with Snap1837557492111129148166185204222241259278296315333352153682VHL_A153716FV3_A153716FV4_A393707NUT_A183711YMY_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
2VHL_A 1.53e-62 15 368 20 385
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]
6FV3_A 3.39e-58 15 371 32 393
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 5.13e-57 15 371 32 393
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]
7NUT_A 3.14e-52 39 370 57 401
ChainA, N-acetylglucosamine-6-phosphate deacetylase [Homo sapiens],7NUT_B Chain B, N-acetylglucosamine-6-phosphate deacetylase [Homo sapiens],7NUU_A Chain A, N-acetylglucosamine-6-phosphate deacetylase [Homo sapiens],7NUU_B Chain B, N-acetylglucosamine-6-phosphate deacetylase [Homo sapiens]
1YMY_A 1.27e-51 18 371 20 380
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]

Swiss-Prot Hits      download full data without filtering help

Created with Snap183755749211112914816618520422224125927829631533335213370sp|P96166|NAGA_VIBFU15368sp|O34450|NAGA_BACSU11367sp|Q8XAC3|AGAA_ECO571360sp|Q84F86|NAGA_LYSSH38370sp|P34480|NAGA_CAEEL
Hit ID E-Value Query Start Query End Hit Start Hit End Description
P96166 1.38e-64 13 370 20 385
N-acetylglucosamine-6-phosphate deacetylase OS=Vibrio furnissii OX=29494 GN=manD PE=3 SV=1
O34450 8.40e-62 15 368 20 385
N-acetylglucosamine-6-phosphate deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=nagA PE=1 SV=1
Q8XAC3 4.72e-59 11 367 14 372
N-acetylgalactosamine-6-phosphate deacetylase OS=Escherichia coli O157:H7 OX=83334 GN=agaA PE=1 SV=2
Q84F86 1.09e-55 1 360 6 372
N-acetylglucosamine-6-phosphate deacetylase OS=Lysinibacillus sphaericus OX=1421 GN=nagA PE=2 SV=1
P34480 9.52e-54 38 370 64 413
N-acetylglucosamine-6-phosphate deacetylase OS=Caenorhabditis elegans OX=6239 GN=F59B2.3 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
1.000053 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001356_00440.