(data stored in ACNUC7421 zone)

SWISSPROT: GUDD_BACSU

ID   GUDD_BACSU              Reviewed;         455 AA.
AC   P42238;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   11-DEC-2019, entry version 130.
DE   RecName: Full=Probable glucarate dehydratase;
DE            Short=GDH;
DE            Short=GlucD;
DE            EC=4.2.1.40;
GN   Name=gudD; Synonyms=ycbF; OrderedLocusNames=BSU02490;
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;
RX   PubMed=7704254; DOI=10.1099/13500872-141-2-269;
RA   Ogawa K., Akagawa E., Nakamura K., Yamane K.;
RT   "Determination of a 21548 bp nucleotide sequence around the 24 degrees
RT   region of the Bacillus subtilis chromosome.";
RL   Microbiology 141:269-275(1995).
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   SEQUENCE REVISION TO 133.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
CC   -!- FUNCTION: Catalyzes the dehydration of glucarate to 5-keto-4-deoxy-D-
CC       glucarate (5-kdGluc). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glucarate = 5-dehydro-4-deoxy-D-glucarate + H2O;
CC         Xref=Rhea:RHEA:14573, ChEBI:CHEBI:15377, ChEBI:CHEBI:30612,
CC         ChEBI:CHEBI:42819; EC=4.2.1.40;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- PATHWAY: Carbohydrate acid metabolism; D-glucarate degradation; 2,5-
CC       dioxopentanoate from D-glucarate: step 1/2.
CC   -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC       enzyme family. GlucD subfamily. {ECO:0000305}.
DR   EMBL; D30808; BAA06470.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12043.2; -; Genomic_DNA.
DR   PIR; A69753; A69753.
DR   RefSeq; NP_388131.2; NC_000964.3.
DR   RefSeq; WP_003234816.1; NZ_JNCM01000030.1.
DR   SMR; P42238; -.
DR   STRING; 224308.BSU02490; -.
DR   PaxDb; P42238; -.
DR   PRIDE; P42238; -.
DR   EnsemblBacteria; CAB12043; CAB12043; BSU02490.
DR   GeneID; 938410; -.
DR   KEGG; bsu:BSU02490; -.
DR   PATRIC; fig|224308.179.peg.256; -.
DR   eggNOG; ENOG4105EQX; Bacteria.
DR   eggNOG; COG4948; LUCA.
DR   HOGENOM; HOG000238021; -.
DR   InParanoid; P42238; -.
DR   KO; K01706; -.
DR   OMA; RVAQMCN; -.
DR   PhylomeDB; P42238; -.
DR   BioCyc; BSUB:BSU02490-MONOMER; -.
DR   UniPathway; UPA00564; UER00627.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0008872; F:glucarate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0042838; P:D-glucarate catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd03323; D-glucarate_dehydratase; 1.
DR   Gene3D; 3.20.20.120; -; 1.
DR   Gene3D; 3.30.390.10; -; 1.
DR   InterPro; IPR036849; Enolase-like_C_sf.
DR   InterPro; IPR029017; Enolase-like_N.
DR   InterPro; IPR029065; Enolase_C-like.
DR   InterPro; IPR017653; Glucarate_dehydratase.
DR   InterPro; IPR034598; GlucD-like.
DR   InterPro; IPR034593; Mandelate_racemase-like.
DR   InterPro; IPR013342; Mandelate_racemase_C.
DR   PANTHER; PTHR43287; PTHR43287; 1.
DR   Pfam; PF13378; MR_MLE_C; 1.
DR   SMART; SM00922; MR_MLE; 1.
DR   SUPFAM; SSF51604; SSF51604; 1.
DR   SUPFAM; SSF54826; SSF54826; 1.
DR   TIGRFAMs; TIGR03247; glucar-dehydr; 1.
PE   3: Inferred from homology;
DR   PRODOM; P42238.
DR   SWISS-2DPAGE; P42238.
KW   Lyase; Magnesium; Metal-binding; Reference proteome.
FT   CHAIN           1..455
FT                   /note="Probable glucarate dehydratase"
FT                   /id="PRO_0000171267"
FT   REGION          245..247
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250"
FT   REGION          349..351
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        217
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        349
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   METAL           245
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000250"
FT   METAL           276
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000250"
FT   METAL           299
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000250"
FT   BINDING         42
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         113
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         160
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         215
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         299
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         378
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         431
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        133
FT                   /note="L -> F (in Ref. 1; BAA06470)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   455 AA;  50749 MW;  075D81418A0A0483 CRC64;
     MSSPIQEQVQ KEKRSNIPSI SEMKVIPVAG HDSMLLNLSG AHSPFFTRNI VILTDSSGNQ
     GVGEVPGGEH IRRTLELSEP LVVGKSIGAY QAILQTVRKQ FGDQDRGGRG NQTFDLRTTV
     HAVTALEAAL LDLLGKFLQE PVAALLGEGK QRDEVKMLGY LFYIGDRNRT TLPYQSDEQS
     DCAWFRLRHE EALTPEAIVR LAESAQERYG FQDFKLKGGV LRGEEEIEAV TALSKRFPEA
     RITLDPNGAW SLEEAIALCK GKQDVLAYAE DPCGDENGYS AREVMAEFRR ATGLPTATNM
     IATDWREMGH AIQLHAVDIP LADPHFWTMQ GSVRVAQMCH DWGLTWGSHS NNHFDISLAM
     FTHVAAAAPG RITAIDTHWI WQDGQRLTKQ PFEISSGCVK VPDKPGLGVD IDMEQVEKAH
     EIYRKMNLGA RNDAIPMQFL ISNWEFDRKR PCLVR
//

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