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CAZyme Information: MGYG000002718_02382

You are here: Home > Sequence: MGYG000002718_02382

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 Butyricicoccus sp900547195
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Butyricicoccaceae; Butyricicoccus; Butyricicoccus sp900547195
CAZyme ID MGYG000002718_02382
CAZy Family CE9
CAZyme Description N-acetylglucosamine-6-phosphate deacetylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
379 MGYG000002718_122|CGC1 41437.19 6.3349
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002718 2757942 MAG Canada North America
Gene Location Start: 1315;  End: 2454  Strand: -

Full Sequence      Download help

MIVQSKRVWV  GGQFLPYQLV  LRHGKIEQIL  PYGARLADKD  YGNARIVPGF  IDVHTHGAYG60
YDTNDAQPDG  LRHWLRSIPE  EGVTALLPTT  VTQLPEVLEP  AVRSVAQVVR  EGYEGAEILG120
IHFEGPYLNM  ERKGAQPPEA  IVPASVEQFQ  RYQQAADGLI  RYITLAPEED  KDLALTRYCS180
SHGVVVSMGH  SSADYDRVME  AVANGARSMT  HVHNGMPPYH  HREPGLVGAA  LRLHGVFGEI240
IGDGCHTHVT  VLNNFFSAKG  RDDAILITDS  LRVKYCPPGG  EYELGGHPIE  VGADGLARLK300
GTDTIAGSTL  RMNQGLRILV  ERAMVPFDAA  LNACTINPAR  CLRIDGRKGR  LCAGYDADLV360
VLDEDYGVQQ  TYCCGKPML379

Enzyme Prediction      help

No EC number prediction in MGYG000002718_02382.

CAZyme Signature Domains help

Created with Snap18375675941131321511701892082272462652843033223413605375CE9
Family Start End Evalue family coverage
CE9 5 375 6.8e-124 0.9919571045576407

CDD Domains      download full data without filtering help

Created with Snap18375675941131321511701892082272462652843033223413601375NagA19376NagA5376nagA17376nagA46365Amidohydro_1
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd00854 NagA 1.72e-149 1 375 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 2.97e-129 19 376 21 376
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism].
TIGR00221 nagA 1.56e-105 5 376 9 380
N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars]
PRK11170 nagA 4.90e-58 17 376 19 377
N-acetylglucosamine-6-phosphate deacetylase; Provisional
pfam01979 Amidohydro_1 3.56e-29 46 365 2 311
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 Snap18375675941131321511701892082272462652843033223413601379ASN95158.1|CE91379QJU20720.1|CE91379QRP40159.1|CE91379QQQ99665.1|CE91379ANU45580.1|CE9
Hit ID E-Value Query Start Query End Hit Start Hit End
ASN95158.1 2.32e-204 1 379 1 379
QJU20720.1 2.32e-204 1 379 1 379
QRP40159.1 2.32e-204 1 379 1 379
QQQ99665.1 9.41e-204 1 379 1 379
ANU45580.1 9.41e-204 1 379 1 379

PDB Hits      download full data without filtering help

Created with Snap1837567594113132151170189208227246265284303322341360463762VHL_A73767NUT_A373766FV3_A373766FV4_A73763EGJ_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
2VHL_A 8.08e-79 46 376 55 385
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]
7NUT_A 1.33e-58 7 376 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]
6FV3_A 1.65e-52 37 376 55 390
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]
6FV4_A 2.45e-51 37 376 55 390
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 8.87e-42 7 376 11 377
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]

Swiss-Prot Hits      download full data without filtering help

Created with Snap183756759411313215117018920822724626528430332234136046376sp|O34450|NAGA_BACSU21376sp|Q84F86|NAGA_LYSSH4376sp|P96166|NAGA_VIBFU19376sp|Q6P0U0|NAGA_DANRE7376sp|A7MBC0|NAGA_BOVIN
Hit ID E-Value Query Start Query End Hit Start Hit End Description
O34450 4.42e-78 46 376 55 385
N-acetylglucosamine-6-phosphate deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=nagA PE=1 SV=1
Q84F86 4.39e-69 21 376 27 380
N-acetylglucosamine-6-phosphate deacetylase OS=Lysinibacillus sphaericus OX=1421 GN=nagA PE=2 SV=1
P96166 1.25e-60 4 376 11 383
N-acetylglucosamine-6-phosphate deacetylase OS=Vibrio furnissii OX=29494 GN=manD PE=3 SV=1
Q6P0U0 4.26e-59 19 376 31 399
N-acetylglucosamine-6-phosphate deacetylase OS=Danio rerio OX=7955 GN=amdhd2 PE=2 SV=1
A7MBC0 5.20e-58 7 376 19 399
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
1.000074 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002718_02382.