(data stored in ACNUC7421 zone)

SWISSPROT: RIDA_BACSU

ID   RIDA_BACSU              Reviewed;         125 AA.
AC   P37552;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   11-DEC-2019, entry version 134.
DE   RecName: Full=2-iminobutanoate/2-iminopropanoate deaminase;
DE            EC=3.5.99.10;
DE   AltName: Full=Enamine/imine deaminase;
GN   Name=yabJ; OrderedLocusNames=BSU00480;
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=7584024; DOI=10.1093/dnares/1.1.1;
RA   Ogasawara N., Nakai S., Yoshikawa H.;
RT   "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT   chromosome containing the replication origin.";
RL   DNA Res. 1:1-14(1994).
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   PRELIMINARY FUNCTIONAL ASSIGNMENT.
RX   PubMed=10368157;
RA   Rappu P., Shin B.S., Zalkin H., Maentsaelae P.;
RT   "A role for a highly conserved protein of unknown function in regulation of
RT   Bacillus subtilis purA by the purine repressor.";
RL   J. Bacteriol. 181:3810-3815(1999).
RN   [4]
RP   REVISION OF FUNCTION.
RX   PubMed=14594850; DOI=10.1128/jb.185.22.6728-6731.2003;
RA   Rappu P., Pullinen T., Mantsaelae P.;
RT   "In vivo effect of mutations at the PRPP binding site of the Bacillus
RT   subtilis purine repressor.";
RL   J. Bacteriol. 185:6728-6731(2003).
RN   [5]
RP   FUNCTION AS A DEAMINASE, AND CATALYTIC ACTIVITY.
RC   STRAIN=168;
RX   PubMed=22094463; DOI=10.1074/jbc.m111.304477;
RA   Lambrecht J.A., Flynn J.M., Downs D.M.;
RT   "The conserved YjgF protein family deaminates enamine/imine intermediates
RT   of pyridoxal-5'-phosphate (PLP)-dependent enzyme reactions.";
RL   J. Biol. Chem. 287:3454-3461(2012).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), PROTEIN SEQUENCE OF N-TERMINUS, AND
RP   SUBUNIT.
RX   PubMed=10557275; DOI=10.1073/pnas.96.23.13074;
RA   Sinha S., Rappu P., Lange S.C., Maentsaelae P., Zalkin H., Smith J.L.;
RT   "Crystal structure of Bacillus subtilis YabJ, a purine regulatory protein
RT   and member of the highly conserved YjgF family.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:13074-13079(1999).
CC   -!- FUNCTION: Accelerates the release of ammonia from reactive
CC       enamine/imine intermediates of the PLP-dependent threonine dehydratase
CC       (IlvA) in the low water environment of the cell. It catalyzes the
CC       deamination of enamine/imine intermediates to yield 2-ketobutyrate and
CC       ammonia. It is required for the detoxification of reactive
CC       intermediates of IlvA due to their highly nucleophilic abilities.
CC       Involved in the isoleucine biosynthesis. May have a role in the purine
CC       metabolism. {ECO:0000269|PubMed:22094463}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-iminobutanoate + H2O = 2-oxobutanoate + NH4(+);
CC         Xref=Rhea:RHEA:39975, ChEBI:CHEBI:15377, ChEBI:CHEBI:16763,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:76545; EC=3.5.99.10;
CC         Evidence={ECO:0000269|PubMed:22094463};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-iminopropanoate + H2O = NH4(+) + pyruvate;
CC         Xref=Rhea:RHEA:40671, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:44400; EC=3.5.99.10;
CC         Evidence={ECO:0000269|PubMed:22094463};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC       oxobutanoate from L-threonine.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:10557275}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the RutC family. {ECO:0000305}.
CC   -!- CAUTION: Was originally (PubMed:10368157) thought to have a role in the
CC       purine repressor-mediated regulation of purA or the pur operon. The
CC       effect of yabJ on regulation of purA was due to the orientation of the
CC       marker gene downstream of purR in the yabJ mutant strain used in
CC       PubMed:10368157. {ECO:0000305|PubMed:10368157}.
DR   EMBL; D26185; BAA05283.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11824.1; -; Genomic_DNA.
DR   PIR; S66077; S66077.
DR   RefSeq; NP_387929.1; NC_000964.3.
DR   RefSeq; WP_003226738.1; NZ_JNCM01000028.1.
DR   PDB; 1QD9; X-ray; 1.70 A; A/B/C=2-125.
DR   PDBsum; 1QD9; -.
DR   SMR; P37552; -.
DR   STRING; 224308.BSU00480; -.
DR   jPOST; P37552; -.
DR   PaxDb; P37552; -.
DR   PRIDE; P37552; -.
DR   EnsemblBacteria; CAB11824; CAB11824; BSU00480.
DR   GeneID; 936988; -.
DR   KEGG; bsu:BSU00480; -.
DR   PATRIC; fig|224308.179.peg.48; -.
DR   eggNOG; ENOG4105KME; Bacteria.
DR   eggNOG; COG0251; LUCA.
DR   HOGENOM; HOG000267215; -.
DR   InParanoid; P37552; -.
DR   KO; K09022; -.
DR   OMA; GSYFKEP; -.
DR   PhylomeDB; P37552; -.
DR   BioCyc; BSUB:BSU00480-MONOMER; -.
DR   BRENDA; 3.5.99.10; 658.
DR   EvolutionaryTrace; P37552; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0019239; F:deaminase activity; IDA:UniProtKB.
DR   GO; GO:0046360; P:2-oxobutyrate biosynthetic process; IDA:CACAO.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1330.40; -; 1.
DR   InterPro; IPR006056; RidA.
DR   InterPro; IPR019897; RidA_CS.
DR   InterPro; IPR035959; RutC-like_sf.
DR   InterPro; IPR006175; YjgF/YER057c/UK114.
DR   PANTHER; PTHR11803; PTHR11803; 1.
DR   Pfam; PF01042; Ribonuc_L-PSP; 1.
DR   SUPFAM; SSF55298; SSF55298; 1.
DR   TIGRFAMs; TIGR00004; TIGR00004; 1.
DR   PROSITE; PS01094; UPF0076; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P37552.
DR   SWISS-2DPAGE; P37552.
KW   3D-structure; Amino-acid biosynthesis;
KW   Branched-chain amino acid biosynthesis; Cytoplasm; Detoxification;
KW   Direct protein sequencing; Hydrolase; Isoleucine biosynthesis;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..125
FT                   /note="2-iminobutanoate/2-iminopropanoate deaminase"
FT                   /id="PRO_0000170330"
FT   BINDING         102
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255"
FT   SITE            17
FT                   /note="Stabilizes the substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            117
FT                   /note="Important for catalytic activity at high pH"
FT                   /evidence="ECO:0000250"
FT   STRAND          3..5
FT                   /evidence="ECO:0000244|PDB:1QD9"
FT   STRAND          18..23
FT                   /evidence="ECO:0000244|PDB:1QD9"
FT   STRAND          26..29
FT                   /evidence="ECO:0000244|PDB:1QD9"
FT   HELIX           46..63
FT                   /evidence="ECO:0000244|PDB:1QD9"
FT   HELIX           68..70
FT                   /evidence="ECO:0000244|PDB:1QD9"
FT   STRAND          71..79
FT                   /evidence="ECO:0000244|PDB:1QD9"
FT   HELIX           81..83
FT                   /evidence="ECO:0000244|PDB:1QD9"
FT   HELIX           84..94
FT                   /evidence="ECO:0000244|PDB:1QD9"
FT   STRAND          95..97
FT                   /evidence="ECO:0000244|PDB:1QD9"
FT   STRAND          101..106
FT                   /evidence="ECO:0000244|PDB:1QD9"
FT   HELIX           111..113
FT                   /evidence="ECO:0000244|PDB:1QD9"
FT   STRAND          115..123
FT                   /evidence="ECO:0000244|PDB:1QD9"
SQ   SEQUENCE   125 AA;  13654 MW;  93A9721B82ED3490 CRC64;
     MTKAVHTKHA PAAIGPYSQG IIVNNMFYSS GQIPLTPSGE MVNGDIKEQT HQVFSNLKAV
     LEEAGASFET VVKATVFIAD MEQFAEVNEV YGQYFDTHKP ARSCVEVARL PKDALVEIEV
     IALVK
//

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