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CAZyme Information: MGYG000001115_00018

You are here: Home > Sequence: MGYG000001115_00018

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 Agathobaculum sp900544475
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Butyricicoccaceae; Agathobaculum; Agathobaculum sp900544475
CAZyme ID MGYG000001115_00018
CAZy Family CE9
CAZyme Description N-acetylglucosamine-6-phosphate deacetylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
369 MGYG000001115_1|CGC1 39012.19 4.8206
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001115 2249105 MAG China Asia
Gene Location Start: 16837;  End: 17946  Strand: -

Full Sequence      Download help

MEFRNLKIYQ  PDGTFRSGGL  SISGDRITGT  EAGSDAVDMG  GLYAIPGLVD  LHFHGCVGYD60
FCDGTAEAIS  ALASYQAQNG  VAAICPATMT  YPEEKLSEIA  QAAAAWSAEP  HEAALVGINM120
EGPFISEKKK  GAQNAAYLHA  PDAAMFRRVQ  EKAHGLFKLC  DMAPELPGAM  ETIEELSGEV180
RISLAHTEAD  YDTACEAFRR  GARQATHLFN  AMPPFSHRAP  GVIGAAFDSE  NVAVELIADG240
VHIHPSVVRA  VFTLFSGRVI  LISDSMMATG  LADGEYSLGG  QAVTVRGNLA  TLHDGTIAGS300
ATNLMDCVRS  AVRMGIPFGE  AVRSASTTPA  RALGIENDYG  SLEAGRLANV  VLLDEELNIH360
AVLLRGRML369

Enzyme Prediction      help

No EC number prediction in MGYG000001115_00018.

CAZyme Signature Domains help

Created with Snap18365573921101291471661842022212392582762953133323503366CE9
Family Start End Evalue family coverage
CE9 3 366 1.9e-124 0.9973190348525469

CDD Domains      download full data without filtering help

Created with Snap18365573921101291471661842022212392582762953133323503366NagA3366NagA3367nagA32366nagA43354Amidohydro_1
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd00854 NagA 9.98e-130 3 366 3 374
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 2.22e-110 3 366 4 375
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism].
TIGR00221 nagA 1.86e-88 3 367 7 380
N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars]
PRK11170 nagA 2.34e-62 32 366 39 376
N-acetylglucosamine-6-phosphate deacetylase; Provisional
pfam01979 Amidohydro_1 8.57e-12 43 354 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 Snap183655739211012914716618420222123925827629531333235015369ACV56117.1|CE91369BCD35303.1|CE91369QMW71740.1|CE91367QOV19464.1|CE91368QCP34781.1|CE9
Hit ID E-Value Query Start Query End Hit Start Hit End
ACV56117.1 2.51e-149 15 369 5 369
BCD35303.1 4.95e-145 1 369 1 370
QMW71740.1 4.95e-145 1 369 1 370
QOV19464.1 6.55e-145 1 367 1 368
QCP34781.1 7.60e-142 1 368 1 369

PDB Hits      download full data without filtering help

Created with Snap1836557392110129147166184202221239258276295313332350453682VHL_A163666FV3_A53673EGJ_A13687NUT_A163666FV4_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
2VHL_A 1.32e-63 45 368 56 386
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 1.34e-51 16 366 32 389
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]
3EGJ_A 2.31e-51 5 367 9 377
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]
7NUT_A 6.18e-51 1 368 13 400
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]
6FV4_A 1.98e-50 16 366 32 389
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]

Swiss-Prot Hits      download full data without filtering help

Created with Snap183655739211012914716618420222123925827629531333235045368sp|O34450|NAGA_BACSU34368sp|P96166|NAGA_VIBFU1368sp|Q8JZV7|NAGA_MOUSE1368sp|Q5BJY6|NAGA_RAT1368sp|A7MBC0|NAGA_BOVIN
Hit ID E-Value Query Start Query End Hit Start Hit End Description
O34450 7.25e-63 45 368 56 386
N-acetylglucosamine-6-phosphate deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=nagA PE=1 SV=1
P96166 3.55e-56 34 368 47 384
N-acetylglucosamine-6-phosphate deacetylase OS=Vibrio furnissii OX=29494 GN=manD PE=3 SV=1
Q8JZV7 1.76e-55 1 368 13 400
N-acetylglucosamine-6-phosphate deacetylase OS=Mus musculus OX=10090 GN=Amdhd2 PE=1 SV=1
Q5BJY6 9.57e-55 1 368 13 400
N-acetylglucosamine-6-phosphate deacetylase OS=Rattus norvegicus OX=10116 GN=Amdhd2 PE=3 SV=2
A7MBC0 3.71e-54 1 368 13 400
N-acetylglucosamine-6-phosphate deacetylase OS=Bos taurus OX=9913 GN=AMDHD2 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
1.000029 0.000015 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001115_00018.