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COMC_CHRSD
ID   COMC_CHRSD              Reviewed;         333 AA.
AC   Q1QWN5;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=(2R)-3-sulfolactate dehydrogenase (NADP(+));
DE            EC=1.1.1.338;
DE   AltName: Full=(R)-2-hydroxyacid dehydrogenase;
DE   AltName: Full=(R)-sulfolactate dehydrogenase;
GN   Name=comC; OrderedLocusNames=Csal_1771;
OS   Chromohalobacter salexigens (strain ATCC BAA-138 / DSM 3043 / CIP 106854 /
OS   NCIMB 13768 / 1H11).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Chromohalobacter.
OX   NCBI_TaxID=290398;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11;
RX   PubMed=22675587; DOI=10.4056/sigs.2285059;
RA   Copeland A., O'Connor K., Lucas S., Lapidus A., Berry K.W., Detter J.C.,
RA   Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Bruce D.,
RA   Goodwin L., Han C., Tapia R., Saunders E., Schmutz J., Brettin T.,
RA   Larimer F., Land M., Hauser L., Vargas C., Nieto J.J., Kyrpides N.C.,
RA   Ivanova N., Goker M., Klenk H.P., Csonka L.N., Woyke T.;
RT   "Complete genome sequence of the halophilic and highly halotolerant
RT   Chromohalobacter salexigens type strain (1H11(T)).";
RL   Stand. Genomic Sci. 5:379-388(2011).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11;
RX   PubMed=20007648; DOI=10.1099/mic.0.034736-0;
RA   Denger K., Cook A.M.;
RT   "Racemase activity effected by two dehydrogenases in sulfolactate
RT   degradation by Chromohalobacter salexigens: purification of (S)-
RT   sulfolactate dehydrogenase.";
RL   Microbiology 156:967-974(2010).
CC   -!- FUNCTION: Catalyzes the reduction of sulfopyruvate to (R)-sulfolactate.
CC       Together with SlcC, provides a racemase system that converts (2S)-3-
CC       sulfolactate to (2R)-3-sulfolactate, which is degraded further by (2R)-
CC       sulfolactate sulfo-lyase. {ECO:0000269|PubMed:20007648}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-3-sulfolactate + NADP(+) = 3-sulfopyruvate + H(+) +
CC         NADPH; Xref=Rhea:RHEA:15537, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:57940, ChEBI:CHEBI:58349, ChEBI:CHEBI:58738;
CC         EC=1.1.1.338; Evidence={ECO:0000269|PubMed:20007648};
CC   -!- SIMILARITY: Belongs to the LDH2/MDH2 oxidoreductase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000285; ABE59123.1; -; Genomic_DNA.
DR   RefSeq; WP_011507069.1; NC_007963.1.
DR   AlphaFoldDB; Q1QWN5; -.
DR   SMR; Q1QWN5; -.
DR   STRING; 290398.Csal_1771; -.
DR   EnsemblBacteria; ABE59123; ABE59123; Csal_1771.
DR   KEGG; csa:Csal_1771; -.
DR   eggNOG; COG2055; Bacteria.
DR   HOGENOM; CLU_040452_0_0_6; -.
DR   OMA; TNTEPAM; -.
DR   OrthoDB; 1374098at2; -.
DR   BioCyc; MetaCyc:MON-15868; -.
DR   BRENDA; 1.1.1.338; 8057.
DR   Proteomes; UP000000239; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1530.10; -; 1.
DR   Gene3D; 3.30.1370.60; -; 1.
DR   InterPro; IPR043144; Mal/L-sulf/L-lact_DH-like_ah.
DR   InterPro; IPR043143; Mal/L-sulf/L-lact_DH-like_NADP.
DR   InterPro; IPR036111; Mal/L-sulfo/L-lacto_DH-like_sf.
DR   InterPro; IPR003767; Malate/L-lactate_DH-like.
DR   PANTHER; PTHR11091; PTHR11091; 1.
DR   Pfam; PF02615; Ldh_2; 1.
DR   SUPFAM; SSF89733; SSF89733; 1.
PE   1: Evidence at protein level;
KW   NAD; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..333
FT                   /note="(2R)-3-sulfolactate dehydrogenase (NADP(+))"
FT                   /id="PRO_0000418760"
SQ   SEQUENCE   333 AA;  35182 MW;  86AD2F0EA4F4569B CRC64;
     MSRMISLREA ETLAVAALEA VGVPRWEAEV TARALIDAER DGLASHGLSR LPFYLAQARS
     GKVVADAQAR VEVAGSVIRV DARHGLAFPA IARGVERAIP LARELGLVAV AIGGSHHFGV
     AGAPVERLAR EGLVAMAFSN APSAMAPWGG KRPLYGTNPI AFATPRRGTD PLVIDLSLSK
     VARGKVMLAK KAGEPIPEGW ALDIEGRPTT DPDAAIAGSM VPAGDAKGAS LALMVELLTA
     GLTGSHFGFQ ASSFFEPEGE APSVGHLMLA FDPAHFSDGY LEHIEALFQA MLEQEGVRLP
     GTRRHALRRE RGESLELPEA VVDELRAYAV SRV
 
 
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