NAGB_HAEIN
ID NAGB_HAEIN Reviewed; 270 AA.
AC P44538;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Glucosamine-6-phosphate deaminase;
DE EC=3.5.99.6;
DE AltName: Full=GlcN6P deaminase;
DE Short=GNPDA;
DE AltName: Full=Glucosamine-6-phosphate isomerase;
GN Name=nagB; OrderedLocusNames=HI_0141;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
CC -!- FUNCTION: Catalyzes the reversible isomerization-deamination of
CC glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P)
CC and ammonium ion. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucosamine 6-phosphate + H2O = beta-D-fructose 6-
CC phosphate + NH4(+); Xref=Rhea:RHEA:12172, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:57634, ChEBI:CHEBI:75989; EC=3.5.99.6;
CC -!- ACTIVITY REGULATION: Allosterically activated by N-acetylglucosamine 6-
CC phosphate (GlcNAc6P). {ECO:0000250}.
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation; D-
CC fructose 6-phosphate from N-acetylneuraminate: step 5/5.
CC -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate
CC isomerase family. NagB subfamily. {ECO:0000305}.
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DR EMBL; L42023; AAC21813.1; -; Genomic_DNA.
DR PIR; F64050; F64050.
DR RefSeq; NP_438310.1; NC_000907.1.
DR RefSeq; WP_005668148.1; NC_000907.1.
DR AlphaFoldDB; P44538; -.
DR SMR; P44538; -.
DR STRING; 71421.HI_0141; -.
DR EnsemblBacteria; AAC21813; AAC21813; HI_0141.
DR KEGG; hin:HI_0141; -.
DR PATRIC; fig|71421.8.peg.143; -.
DR eggNOG; COG0363; Bacteria.
DR HOGENOM; CLU_049611_0_1_6; -.
DR OMA; FNEPCSS; -.
DR PhylomeDB; P44538; -.
DR BioCyc; HINF71421:G1GJ1-153-MON; -.
DR UniPathway; UPA00629; UER00684.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004342; F:glucosamine-6-phosphate deaminase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006043; P:glucosamine catabolic process; IBA:GO_Central.
DR GO; GO:0006046; P:N-acetylglucosamine catabolic process; IBA:GO_Central.
DR GO; GO:0019262; P:N-acetylneuraminate catabolic process; IBA:GO_Central.
DR CDD; cd01399; GlcN6P_deaminase; 1.
DR HAMAP; MF_01241; GlcN6P_deamin; 1.
DR InterPro; IPR006148; Glc/Gal-6P_isomerase.
DR InterPro; IPR004547; Glucosamine6P_isomerase.
DR InterPro; IPR018321; Glucosamine6P_isomerase_CS.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR PANTHER; PTHR11280; PTHR11280; 1.
DR Pfam; PF01182; Glucosamine_iso; 1.
DR SUPFAM; SSF100950; SSF100950; 1.
DR TIGRFAMs; TIGR00502; nagB; 1.
DR PROSITE; PS01161; GLC_GALNAC_ISOMERASE; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme; Carbohydrate metabolism; Hydrolase; Reference proteome.
FT CHAIN 1..270
FT /note="Glucosamine-6-phosphate deaminase"
FT /id="PRO_0000160149"
FT ACT_SITE 72
FT /note="Proton acceptor; for enolization step"
FT /evidence="ECO:0000250"
FT ACT_SITE 141
FT /note="For ring-opening step"
FT /evidence="ECO:0000250"
FT ACT_SITE 143
FT /note="Proton acceptor; for ring-opening step"
FT /evidence="ECO:0000250"
FT ACT_SITE 148
FT /note="For ring-opening step"
FT /evidence="ECO:0000250"
FT SITE 151
FT /note="Part of the allosteric site"
FT /evidence="ECO:0000250"
FT SITE 158
FT /note="Part of the allosteric site"
FT /evidence="ECO:0000250"
FT SITE 160
FT /note="Part of the allosteric site"
FT /evidence="ECO:0000250"
FT SITE 161
FT /note="Part of the allosteric site"
FT /evidence="ECO:0000250"
FT SITE 254
FT /note="Part of the allosteric site"
FT /evidence="ECO:0000250"
SQ SEQUENCE 270 AA; 30501 MW; D06C651C1A41C235 CRC64;
MRFIPLQTEQ QVSCWAAQHI INRINDFKPT AERPFVLGLP TGGTPLKTYQ ELIRLYQAGK
VSFKHVVTFN MDEYVALPEE HPESYHSFMY NNFFNHIDIL PENINILNGN TDDHNAECRR
YEEKIKSYGK IHLFMGGVGV DGHIAFNEPA SSLSSRTRIK TLTQDTLIAN SRFFNNDVTQ
VPKYALTIGV GTLLDAEEVM ILATGHQKAL AVQAAVEGSI NHLWTVSALQ MHRHFLLVCD
EAAQQELKVK TVKYFTELEG AVAGTDYQDK
