GAMA_BACSU
ID GAMA_BACSU Reviewed; 249 AA.
AC O31458;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Probable glucosamine-6-phosphate deaminase 2;
DE EC=3.5.99.6;
DE AltName: Full=GlcN6P deaminase 2;
DE Short=GNPDA 2;
DE AltName: Full=Glucosamine-6-phosphate isomerase 2;
GN Name=gamA; Synonyms=ybfT; OrderedLocusNames=BSU02360;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Haga K., Liu H., Yasumoto K., Takahashi H., Yoshikawa H.;
RT "Sequence analysis of the 70kb region between 17 and 23 degree of the
RT Bacillus subtilis chromosome.";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP INDUCTION.
RX PubMed=24673833; DOI=10.1111/mmi.12544;
RA Gaugue I., Oberto J., Plumbridge J.;
RT "Regulation of amino sugar utilization in Bacillus subtilis by the GntR
RT family regulators, NagR and GamR.";
RL Mol. Microbiol. 92:100-115(2014).
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 -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation; D-
CC fructose 6-phosphate from N-acetylneuraminate: step 5/5.
CC -!- INDUCTION: Expression is repressed by the HTH-type transcriptional
CC regulator GamR. {ECO:0000269|PubMed:24673833}.
CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate
CC isomerase family. NagB subfamily. {ECO:0000305}.
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DR EMBL; AB006424; BAA33133.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12030.1; -; Genomic_DNA.
DR PIR; E69750; E69750.
DR RefSeq; NP_388118.1; NC_000964.3.
DR RefSeq; WP_003246480.1; NZ_JNCM01000030.1.
DR AlphaFoldDB; O31458; -.
DR SMR; O31458; -.
DR STRING; 224308.BSU02360; -.
DR PaxDb; O31458; -.
DR PRIDE; O31458; -.
DR EnsemblBacteria; CAB12030; CAB12030; BSU_02360.
DR GeneID; 938425; -.
DR KEGG; bsu:BSU02360; -.
DR PATRIC; fig|224308.179.peg.242; -.
DR eggNOG; COG0363; Bacteria.
DR InParanoid; O31458; -.
DR OMA; FNEPCSS; -.
DR PhylomeDB; O31458; -.
DR BioCyc; BSUB:BSU02360-MON; -.
DR UniPathway; UPA00629; UER00684.
DR Proteomes; UP000001570; 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 2: Evidence at transcript level;
KW Carbohydrate metabolism; Hydrolase; Reference proteome.
FT CHAIN 1..249
FT /note="Probable glucosamine-6-phosphate deaminase 2"
FT /id="PRO_0000160134"
FT ACT_SITE 67
FT /note="Proton acceptor; for enolization step"
FT /evidence="ECO:0000250"
FT ACT_SITE 136
FT /note="For ring-opening step"
FT /evidence="ECO:0000250"
FT ACT_SITE 138
FT /note="Proton acceptor; for ring-opening step"
FT /evidence="ECO:0000250"
FT ACT_SITE 143
FT /note="For ring-opening step"
FT /evidence="ECO:0000250"
SQ SEQUENCE 249 AA; 27289 MW; 386A7D7301C420D3 CRC64;
MKILIAEHYE ELCKLSAAII KEQIQAKKDA VLGLATGSTP VGLYKQLISD YQAGEIDFSK
VTTFNLDEYA GLSPSHPQSY NHFMHEHLFQ HINMQPDHIH IPQGDNPQLE AACKVYEDLI
RQAGGIDVQI LGIGANGHIG FNEPGSDFED RTRVVKLSES TIQANARFFG GDPVLVPRLA
ISMGIKTIME FSKHIVLLAS GEEKADAIQK MAEGPVTTDV PASILQKHNH VTVIADYKAA
QKLKSASFS
