NAGB_BACSU
ID NAGB_BACSU Reviewed; 242 AA.
AC O35000;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Glucosamine-6-phosphate deaminase 1;
DE EC=3.5.99.6;
DE AltName: Full=GlcN6P deaminase 1;
DE Short=GNPDA 1;
DE AltName: Full=Glucosamine-6-phosphate isomerase 1;
GN Name=nagB; OrderedLocusNames=BSU35020;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Lazarevic V., Soldo B., Rivolta C., Reynolds S., Mauel C., Karamata D.;
RT "Nucleotide sequence of the 300-304 chromosomal segment of Bacillus
RT subtilis.";
RL Submitted (NOV-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=21602348; DOI=10.1128/jb.00264-11;
RA Bertram R., Rigali S., Wood N., Lulko A.T., Kuipers O.P., Titgemeyer F.;
RT "Regulon of the N-acetylglucosamine utilization regulator NagR in Bacillus
RT subtilis.";
RL J. Bacteriol. 193:3525-3536(2011).
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 NagR. {ECO:0000269|PubMed:21602348}.
CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate
CC isomerase family. NagB subfamily. {ECO:0000305}.
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DR EMBL; AF017113; AAC67284.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15507.1; -; Genomic_DNA.
DR PIR; B69664; B69664.
DR RefSeq; NP_391382.1; NC_000964.3.
DR RefSeq; WP_003228092.1; NZ_JNCM01000033.1.
DR PDB; 2BKV; X-ray; 1.50 A; A/B=1-242.
DR PDB; 2BKX; X-ray; 1.40 A; A/B=1-242.
DR PDBsum; 2BKV; -.
DR PDBsum; 2BKX; -.
DR AlphaFoldDB; O35000; -.
DR SMR; O35000; -.
DR STRING; 224308.BSU35020; -.
DR DrugBank; DB02726; 2-Phosphoglycolic Acid.
DR DrugBank; DB04277; Fructose -6-Phosphate.
DR PaxDb; O35000; -.
DR PRIDE; O35000; -.
DR EnsemblBacteria; CAB15507; CAB15507; BSU_35020.
DR GeneID; 936619; -.
DR KEGG; bsu:BSU35020; -.
DR PATRIC; fig|224308.179.peg.3790; -.
DR eggNOG; COG0363; Bacteria.
DR InParanoid; O35000; -.
DR OMA; NSYRYYM; -.
DR PhylomeDB; O35000; -.
DR BioCyc; BSUB:BSU35020-MON; -.
DR BRENDA; 3.5.99.6; 658.
DR SABIO-RK; O35000; -.
DR UniPathway; UPA00629; UER00684.
DR EvolutionaryTrace; O35000; -.
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 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Hydrolase; Reference proteome.
FT CHAIN 1..242
FT /note="Glucosamine-6-phosphate deaminase 1"
FT /id="PRO_0000160133"
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"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:2BKX"
FT HELIX 9..26
FT /evidence="ECO:0007829|PDB:2BKX"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:2BKX"
FT HELIX 41..53
FT /evidence="ECO:0007829|PDB:2BKX"
FT STRAND 62..69
FT /evidence="ECO:0007829|PDB:2BKX"
FT HELIX 80..87
FT /evidence="ECO:0007829|PDB:2BKX"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:2BKX"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:2BKX"
FT HELIX 109..122
FT /evidence="ECO:0007829|PDB:2BKX"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:2BKX"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:2BKX"
FT HELIX 159..165
FT /evidence="ECO:0007829|PDB:2BKX"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:2BKX"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:2BKX"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:2BKX"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:2BKX"
FT HELIX 184..188
FT /evidence="ECO:0007829|PDB:2BKX"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:2BKX"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:2BKX"
FT HELIX 203..211
FT /evidence="ECO:0007829|PDB:2BKX"
FT HELIX 219..225
FT /evidence="ECO:0007829|PDB:2BKX"
FT STRAND 227..234
FT /evidence="ECO:0007829|PDB:2BKX"
FT TURN 235..240
FT /evidence="ECO:0007829|PDB:2BKX"
SQ SEQUENCE 242 AA; 26991 MW; B7979780B8E35C66 CRC64;
MKVMECQTYE ELSQIAARIT ADTIKEKPDA VLGLATGGTP EGTYRQLIRL HQTENLSFQN
ITTVNLDEYA GLSSDDPNSY HFYMNDRFFQ HIDSKPSRHF IPNGNADDLE AECRRYEQLV
DSLGDTDIQL LGIGRNGHIG FNEPGTSFKS RTHVVTLNEQ TRQANARYFP SIDSVPKKAL
TMGIQTILSS KRILLLISGK SKAEAVRKLL EGNISEDFPA SALHLHSDVT VLIDREAASL
RP
