NAGB_VIBCH
ID NAGB_VIBCH Reviewed; 266 AA.
AC Q9KKS5;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Glucosamine-6-phosphate deaminase {ECO:0000255|HAMAP-Rule:MF_01241};
DE EC=3.5.99.6 {ECO:0000255|HAMAP-Rule:MF_01241};
DE AltName: Full=GlcN6P deaminase {ECO:0000255|HAMAP-Rule:MF_01241};
DE Short=GNPDA {ECO:0000255|HAMAP-Rule:MF_01241};
DE AltName: Full=Glucosamine-6-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_01241};
GN Name=nagB {ECO:0000255|HAMAP-Rule:MF_01241}; OrderedLocusNames=VC_A1025;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
CC -!- FUNCTION: Catalyzes the reversible isomerization-deamination of
CC glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P)
CC and ammonium ion. {ECO:0000255|HAMAP-Rule:MF_01241}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_01241};
CC -!- ACTIVITY REGULATION: Allosterically activated by N-acetylglucosamine 6-
CC phosphate (GlcNAc6P). {ECO:0000255|HAMAP-Rule:MF_01241}.
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation; D-
CC fructose 6-phosphate from N-acetylneuraminate: step 5/5.
CC {ECO:0000255|HAMAP-Rule:MF_01241}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_01241}.
CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate
CC isomerase family. NagB subfamily. {ECO:0000255|HAMAP-Rule:MF_01241}.
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DR EMBL; AE003853; AAF96921.1; -; Genomic_DNA.
DR PIR; H82387; H82387.
DR RefSeq; NP_233409.1; NC_002506.1.
DR RefSeq; WP_001237050.1; NZ_LT906615.1.
DR PDB; 4R7T; X-ray; 2.10 A; A/B/C=1-266.
DR PDB; 5HJ5; X-ray; 1.70 A; A/B/C/D=1-266.
DR PDBsum; 4R7T; -.
DR PDBsum; 5HJ5; -.
DR AlphaFoldDB; Q9KKS5; -.
DR SMR; Q9KKS5; -.
DR STRING; 243277.VC_A1025; -.
DR DNASU; 2612427; -.
DR EnsemblBacteria; AAF96921; AAF96921; VC_A1025.
DR GeneID; 57742378; -.
DR GeneID; 66938947; -.
DR KEGG; vch:VC_A1025; -.
DR PATRIC; fig|243277.26.peg.3630; -.
DR eggNOG; COG0363; Bacteria.
DR HOGENOM; CLU_049611_0_1_6; -.
DR OMA; FNEPCSS; -.
DR BioCyc; VCHO:VCA1025-MON; -.
DR UniPathway; UPA00629; UER00684.
DR Proteomes; UP000000584; Chromosome 2.
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 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; Carbohydrate metabolism; Hydrolase;
KW Reference proteome.
FT CHAIN 1..266
FT /note="Glucosamine-6-phosphate deaminase"
FT /id="PRO_0000160184"
FT ACT_SITE 72
FT /note="Proton acceptor; for enolization step"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT ACT_SITE 141
FT /note="For ring-opening step"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT ACT_SITE 143
FT /note="Proton acceptor; for ring-opening step"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT ACT_SITE 148
FT /note="For ring-opening step"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT SITE 151
FT /note="Part of the allosteric site"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT SITE 158
FT /note="Part of the allosteric site"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT SITE 160
FT /note="Part of the allosteric site"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT SITE 161
FT /note="Part of the allosteric site"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT SITE 254
FT /note="Part of the allosteric site"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:5HJ5"
FT HELIX 9..27
FT /evidence="ECO:0007829|PDB:5HJ5"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:5HJ5"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:5HJ5"
FT HELIX 46..57
FT /evidence="ECO:0007829|PDB:5HJ5"
FT STRAND 66..77
FT /evidence="ECO:0007829|PDB:5HJ5"
FT HELIX 85..92
FT /evidence="ECO:0007829|PDB:5HJ5"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:5HJ5"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:5HJ5"
FT HELIX 114..127
FT /evidence="ECO:0007829|PDB:5HJ5"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:5HJ5"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:5HJ5"
FT HELIX 164..170
FT /evidence="ECO:0007829|PDB:5HJ5"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:5HJ5"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:5HJ5"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:5HJ5"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:5HJ5"
FT HELIX 190..194
FT /evidence="ECO:0007829|PDB:5HJ5"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:5HJ5"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:5HJ5"
FT HELIX 209..216
FT /evidence="ECO:0007829|PDB:5HJ5"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:5HJ5"
FT HELIX 225..231
FT /evidence="ECO:0007829|PDB:5HJ5"
FT STRAND 232..239
FT /evidence="ECO:0007829|PDB:5HJ5"
FT HELIX 241..244
FT /evidence="ECO:0007829|PDB:5HJ5"
FT HELIX 249..258
FT /evidence="ECO:0007829|PDB:5HJ5"
FT HELIX 260..263
FT /evidence="ECO:0007829|PDB:5HJ5"
SQ SEQUENCE 266 AA; 29548 MW; A13B6611DE17213E CRC64;
MRLIPLKAAA QVGKWAAAHI VKRINEFQPT AERPFVLGLP TGGTPLATYK ALIEMHKAGE
VSFKHVVTFN MDEYVGLAAD HPESYRSFMY NNFFNHIDIQ EENINLLNGN TDDHEAECKR
YEDKIKSYGK INLFMGGVGN DGHIAFNEPA SSLSSRTRIK TLTEDTRIAN SRFFDGDINQ
VPKYALTIGV GTLLDAQEIM ILVTGHNKAL ALQAAVEGSV NHLWTVSALQ LHPKAVIVCD
EPSTQELKVK TVKYFTELEA KNIVGF
