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CAZyme Information: MGYG000001317_00340

You are here: Home > Sequence: MGYG000001317_00340

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 Citrobacter portucalensis_A
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter portucalensis_A
CAZyme ID MGYG000001317_00340
CAZy Family CE9
CAZyme Description N-acetylgalactosamine-6-phosphate deacetylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
377 MGYG000001317_6|CGC2 40774.96 6.5444
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001317 5150259 Isolate not provided not provided
Gene Location Start: 141526;  End: 142659  Strand: -

Full Sequence      Download help

MTQVLRAKRL  LTEQGWLDDH  QVRIEDGIIT  AIEPIVSGIM  VRDAELLCPA  YIDTHVHGGA60
GVDVMDDAPD  TLDKLAMHKA  REGVASWLPT  TVTAPLPDIH  RVLKRIARHY  YSGGPGAQVL120
GSYLEGPYFT  PQNKGAHPPE  LFRELDLSEL  DELIAISQQT  LRVVALAPEK  TGALQTIKHL180
KQRNVRVMLG  HSAATWEQTR  AAFDAGADGL  VHCYNGMTGL  HHREPGMVGA  GLTDPRAWLE240
LIADGHHVHP  AAMKLCCCCA  KDRLVLITDA  MQAAGMPDGR  YTLCGEEVEM  RSGIVRTASG300
GLAGSTLSVD  AAVRNMVEFT  GITAEEAIRM  ASLHPARLLG  IDRQRGSLAV  GKCADIIALN360
SGLHMQQIWI  QGQALPL377

Enzyme Prediction      help

EC 3.5.1.25 3.5.1.-

CAZyme Signature Domains help

Created with Snap18375675941131311501691882072262452632823013203393586372CE9
Family Start End Evalue family coverage
CE9 6 372 7.9e-131 0.9946380697050938

CDD Domains      download full data without filtering help

Created with Snap18375675941131311501691882072262452632823013203393584372NagA4373NagA1361nagA9361nagA46360Amidohydro_1
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd00854 NagA 5.88e-173 4 372 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 8.97e-169 4 373 3 376
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism].
TIGR00221 nagA 4.20e-101 1 361 3 368
N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars]
PRK11170 nagA 4.18e-84 9 361 8 365
N-acetylglucosamine-6-phosphate deacetylase; Provisional
pfam01979 Amidohydro_1 1.32e-16 46 360 1 309
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 Snap18375675941131311501691882072262452632823013203393581377QET68103.1|CE91377AYL67737.1|CE91377BBV29087.1|CE91377BBV34101.1|CE91377AHY10503.1|CE9
Hit ID E-Value Query Start Query End Hit Start Hit End
QET68103.1 1.27e-269 1 377 1 377
AYL67737.1 1.04e-268 1 377 1 377
BBV29087.1 2.98e-268 1 377 1 377
BBV34101.1 2.98e-268 1 377 1 377
AHY10503.1 4.23e-268 1 377 1 377

PDB Hits      download full data without filtering help

Created with Snap183756759411313115016918820722624526328230132033935833737NUT_A103612VHL_A53721YMY_A53722P53_A43736FV3_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
7NUT_A 1.81e-66 3 373 19 399
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]
2VHL_A 1.98e-65 10 361 12 373
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]
1YMY_A 1.26e-58 5 372 4 376
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 6.93e-58 5 372 4 376
ChainA, N-acetylglucosamine-6-phosphate deacetylase [Escherichia coli K-12],2P53_B Chain B, N-acetylglucosamine-6-phosphate deacetylase [Escherichia coli K-12]
6FV3_A 6.53e-56 4 373 24 390
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]

Swiss-Prot Hits      download full data without filtering help

Created with Snap18375675941131311501691882072262452632823013203393581373sp|Q8XAC3|AGAA_ECO576373sp|P96166|NAGA_VIBFU211373sp|P42906|AGAA_ECOLI3373sp|Q9Y303|NAGA_HUMAN3373sp|Q8JZV7|NAGA_MOUSE
Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8XAC3 4.89e-236 1 373 1 373
N-acetylgalactosamine-6-phosphate deacetylase OS=Escherichia coli O157:H7 OX=83334 GN=agaA PE=1 SV=2
P96166 7.91e-121 6 373 11 383
N-acetylglucosamine-6-phosphate deacetylase OS=Vibrio furnissii OX=29494 GN=manD PE=3 SV=1
P42906 2.20e-96 211 373 1 163
Putative N-acetylgalactosamine-6-phosphate deacetylase OS=Escherichia coli (strain K12) OX=83333 GN=agaA PE=5 SV=3
Q9Y303 9.90e-66 3 373 19 399
N-acetylglucosamine-6-phosphate deacetylase OS=Homo sapiens OX=9606 GN=AMDHD2 PE=1 SV=2
Q8JZV7 1.96e-65 3 373 19 399
N-acetylglucosamine-6-phosphate deacetylase OS=Mus musculus OX=10090 GN=Amdhd2 PE=1 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
1.000063 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001317_00340.