ID   SDH_RHIRD               Reviewed;         249 AA.
AC   Q9KWN1;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Serine 3-dehydrogenase;
DE            EC=1.1.1.276 {ECO:0000269|PubMed:9028042};
GN   Name=sdh;
OS   Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium
OS   radiobacter).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC   Agrobacterium tumefaciens complex.
OX   NCBI_TaxID=358;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ICR 1600;
RX   PubMed=12092831; DOI=10.1271/bbb.66.1137;
RA   Fujisawa H., Nagata S., Chowdhury E.K., Matsumoto M., Misono H.;
RT   "Cloning and sequencing of the serine dehydrogenase gene from Agrobacterium
RT   tumefaciens.";
RL   Biosci. Biotechnol. Biochem. 66:1137-1139(2002).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-28; 66-98; 128-194 AND 225-243, FUNCTION, CATALYTIC
RP   ACTIVITY, SUBUNIT, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP   AND CHARACTERIZATION.
RX   PubMed=9028042; DOI=10.1271/bbb.61.152;
RA   Chowdhury E.K., Higuchi K., Nagata S., Misono H.;
RT   "A novel NADP(+)-dependent serine dehydrogenase from Agrobacterium
RT   tumefaciens.";
RL   Biosci. Biotechnol. Biochem. 61:152-157(1997).
CC   -!- FUNCTION: Catalyzes the oxidation of the hydroxyl group of serine to
CC       form 2-aminomalonate semialdehyde which is spontaneously converted into
CC       2-aminoacetaldehyde and CO(2). Also acts on D-serine, L-glycerate, D-
CC       glycerate and 2-methyl-DL-serine. Does not act on O-methyl-DL-serine
CC       and L-threonine. {ECO:0000269|PubMed:9028042}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-serine + NADP(+) = aminoacetaldehyde + CO2 + NADPH;
CC         Xref=Rhea:RHEA:43620, ChEBI:CHEBI:16526, ChEBI:CHEBI:33384,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58213, ChEBI:CHEBI:58349;
CC         EC=1.1.1.276; Evidence={ECO:0000269|PubMed:9028042};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=42 mM for L-serine {ECO:0000269|PubMed:9028042};
CC         KM=44 mM for D-serine {ECO:0000269|PubMed:9028042};
CC         KM=54 mM for L-glycerate {ECO:0000269|PubMed:9028042};
CC         KM=56 mM for D-glycerate {ECO:0000269|PubMed:9028042};
CC         KM=0.029 mM for NADP(+) {ECO:0000269|PubMed:9028042};
CC       pH dependence:
CC         Optimum pH is 9.1. {ECO:0000269|PubMed:9028042};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:9028042}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; AB032242; BAB07807.1; -; Genomic_DNA.
DR   PIR; JC7857; JC7857.
DR   RefSeq; WP_060723420.1; NZ_SMCI01000007.1.
DR   AlphaFoldDB; Q9KWN1; -.
DR   SMR; Q9KWN1; -.
DR   STRING; 1082932.ATCR1_20233; -.
DR   eggNOG; COG4221; Bacteria.
DR   GO; GO:0031132; F:serine 3-dehydrogenase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; NADP; Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9028042"
FT   CHAIN           2..249
FT                   /note="Serine 3-dehydrogenase"
FT                   /id="PRO_0000054773"
FT   ACT_SITE        148
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         6..30
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         135
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   249 AA;  26745 MW;  5DCE3C404C950BDA CRC64;
     MSGTILITGA TSGFGQATAQ RFVKEGWKVI GTGRRAERLE ALSAELGSAF HGVAFDITDE
     EATKKALAGL PDGFRDIDIL VNNAGLALGT APAPQVPLKD WQTMVDTNIT GLLNVTHHLL
     PTLIERKGIV INLSSVAAHY PYLGGNVYGG TKAFLRQFSL GLRSDLHGKG VRVTSIEPGM
     CETEFTLVRT GGNQEASDNL YKGVNPITAD DIANTIHWVA SQPKHININS LELMPVNQSF
     AGFQVYRES