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CAZyme Information: MGYG000003540_00288

You are here: Home > Sequence: MGYG000003540_00288

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 UBA1232 sp900769385
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; UBA932; UBA1232; UBA1232 sp900769385
CAZyme ID MGYG000003540_00288
CAZy Family CE9
CAZyme Description N-acetylglucosamine-6-phosphate deacetylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
385 MGYG000003540_84|CGC1 42090.38 5.4127
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003540 1938484 MAG Fiji Oceania
Gene Location Start: 2908;  End: 4065  Strand: +

Full Sequence      Download help

MLTQIINGKI  HTPQGWLKNG  SVIISDNKIL  EVSNCDLAVV  GAKIVDARGM  YIVPGGVEIH60
VHGGGGRDFM  EGTEEAFRTA  VDAHMQHGTT  SIFPTLSSSS  IPMIRAAAAT  TEKLMAEKDS120
PILGLHLEGH  YFNMKMAGGQ  IPEYIKNPDP  NEYIPLLEET  NCIKRWDASP  ELPGALQFGK180
YVSNKGILVS  VAHTQAEFED  IKAGFDVGYT  HATHFYNAMP  GFHKKNEYKY  EGTVESIYLM240
DDMTVEAIAD  GIHVPPTILR  LIYKVKGVEK  TALITDALAC  AASDSQTAFD  PRVIIEDGVC300
KLADRSALAG  SIATMDRLIQ  TMTLKAEVPL  FDVCRMISET  PAKIMGVYDR  KGSLERGKDA360
DILLLDNNLD  VKAVWAMGNL  VKNFE385

Enzyme Prediction      help

No EC number prediction in MGYG000003540_00288.

CAZyme Signature Domains help

Created with Snap19385777961151341541731922112312502692883083273463656378CE9
Family Start End Evalue family coverage
CE9 6 378 7.9e-105 0.9946380697050938

CDD Domains      download full data without filtering help

Created with Snap19385777961151341541731922112312502692883083273463655378NagA5381NagA5379nagA5383nagA51381Amidohydro_1
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd00854 NagA 1.62e-136 5 378 2 374
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 5.44e-109 5 381 4 378
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism].
TIGR00221 nagA 3.42e-81 5 379 7 380
N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars]
PRK11170 nagA 2.94e-56 5 383 4 381
N-acetylglucosamine-6-phosphate deacetylase; Provisional
pfam01979 Amidohydro_1 1.70e-22 51 381 1 335
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 Snap19385777961151341541731922112312502692883083273463651382QUT49240.1|CE91382QIX66124.1|CE91382QCY55374.1|CE91382QRO17768.1|CE91382BBK89953.1|CE9
Hit ID E-Value Query Start Query End Hit Start Hit End
QUT49240.1 3.50e-242 1 382 1 382
QIX66124.1 3.90e-239 1 382 1 382
QCY55374.1 5.54e-239 1 382 1 382
QRO17768.1 5.54e-239 1 382 1 382
BBK89953.1 5.54e-239 1 382 1 382

PDB Hits      download full data without filtering help

Created with Snap193857779611513415417319221123125026928830832734636553833EGJ_A103802VHL_A303816FV3_A303816FV4_A53811YMY_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
3EGJ_A 1.81e-44 5 383 7 381
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]
2VHL_A 5.13e-42 10 380 12 386
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 8.03e-41 30 381 36 392
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 1.13e-39 30 381 36 392
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]
1YMY_A 1.51e-39 5 381 4 379
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 Snap19385777961151341541731922112312502692883083273463655383sp|O32445|NAGA_VIBCH10380sp|O34450|NAGA_BACSU5383sp|P44537|NAGA_HAEIN5381sp|P0AF18|NAGA_ECOLI5381sp|P0AF19|NAGA_ECO57
Hit ID E-Value Query Start Query End Hit Start Hit End Description
O32445 9.30e-44 5 383 4 378
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
O34450 2.81e-41 10 380 12 386
N-acetylglucosamine-6-phosphate deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=nagA PE=1 SV=1
P44537 1.11e-39 5 383 5 381
N-acetylglucosamine-6-phosphate deacetylase OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=nagA PE=3 SV=1
P0AF18 8.26e-39 5 381 4 379
N-acetylglucosamine-6-phosphate deacetylase OS=Escherichia coli (strain K12) OX=83333 GN=nagA PE=1 SV=1
P0AF19 8.26e-39 5 381 4 379
N-acetylglucosamine-6-phosphate deacetylase OS=Escherichia coli O157:H7 OX=83334 GN=nagA PE=2 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
1.000095 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003540_00288.