SDH_AGRFC
ID SDH_AGRFC Reviewed; 249 AA.
AC Q8U8I2;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Serine 3-dehydrogenase;
DE EC=1.1.1.276;
GN Name=sdh; OrderedLocusNames=Atu4110; ORFNames=AGR_L_1487;
OS Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS (strain C58)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=176299;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743193; DOI=10.1126/science.1066804;
RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y.,
RA Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P.,
RA Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F.,
RA Gordon M.P., Olson M.V., Nester E.W.;
RT "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT C58.";
RL Science 294:2317-2323(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743194; DOI=10.1126/science.1066803;
RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT "Genome sequence of the plant pathogen and biotechnology agent
RT Agrobacterium tumefaciens C58.";
RL Science 294:2323-2328(2001).
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:0000250|UniProtKB:Q9KWN1}.
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:0000250|UniProtKB:Q9KWN1};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q9KWN1}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AE007870; AAK89321.1; -; Genomic_DNA.
DR PIR; AH3061; AH3061.
DR PIR; G98224; G98224.
DR RefSeq; NP_356536.1; NC_003063.2.
DR RefSeq; WP_010973571.1; NC_003063.2.
DR AlphaFoldDB; Q8U8I2; -.
DR SMR; Q8U8I2; -.
DR STRING; 176299.Atu4110; -.
DR EnsemblBacteria; AAK89321; AAK89321; Atu4110.
DR KEGG; atu:Atu4110; -.
DR PATRIC; fig|176299.10.peg.3928; -.
DR eggNOG; COG4221; Bacteria.
DR HOGENOM; CLU_010194_2_10_5; -.
DR OMA; WRWMWET; -.
DR PhylomeDB; Q8U8I2; -.
DR BioCyc; AGRO:ATU4110-MON; -.
DR Proteomes; UP000000813; Chromosome linear.
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 3: Inferred from homology;
KW NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..249
FT /note="Serine 3-dehydrogenase"
FT /id="PRO_0000054772"
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; 26784 MW; 149E657B94C16EE3 CRC64;
MSGTILITGA TSGFGQATAR RFVKEGWKVI GTGRRAERLE ALAAELGQAF HGIAFDITDE
DATEKALAAL PDGFRDIDIL VNNAGLALGT APAPQVALKD WQTMVDTNIT GLLNITHHLL
PTLIKQKGIV VNLSSVAAHY PYLGGNVYGG TKAFLRQFSL GLRSDLHGKG VRVTSIEPGM
CETEFTLVRT GGNQEASDNL YKGVNPITAD DIANTIYWVA SQPKHININS LELMPVNQSF
AGFQVYRES