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 24-JAN-2024, entry version 92.
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; Pseudomonadota; 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 eggNOG; COG4221; Bacteria.
DR OrthoDB; 658698at2; -.
DR GO; GO:0031132; F:serine 3-dehydrogenase activity; IEA:UniProtKB-EC.
DR CDD; cd05346; SDR_c5; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR42901; ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR42901:SF1; ALCOHOL DEHYDROGENASE; 1.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SMART; SM00822; PKS_KR; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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
//
