ID I4AIQ1_BERLS Unreviewed; 634 AA.
AC I4AIQ1;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000256|ARBA:ARBA00021582};
DE EC=1.1.1.399 {ECO:0000256|ARBA:ARBA00013001};
DE EC=1.1.1.95 {ECO:0000256|ARBA:ARBA00013143};
DE AltName: Full=2-oxoglutarate reductase {ECO:0000256|ARBA:ARBA00030455};
GN OrderedLocusNames=Fleli_1408 {ECO:0000313|EMBL:AFM03836.1};
OS Bernardetia litoralis (strain ATCC 23117 / DSM 6794 / NBRC 15988 / NCIMB
OS 1366 / Fx l1 / Sio-4) (Flexibacter litoralis).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Bernardetiaceae;
OC Bernardetia.
OX NCBI_TaxID=880071 {ECO:0000313|EMBL:AFM03836.1, ECO:0000313|Proteomes:UP000006054};
RN [1] {ECO:0000313|Proteomes:UP000006054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23117 / DSM 6794 / NBRC 15988 / NCIMB 1366 / Sio-4
RC {ECO:0000313|Proteomes:UP000006054};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Lu M.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Spring S., Lang E., Kopitz M., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "The complete genome of Flexibacter litoralis DSM 6794.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible oxidation of 3-phospho-D-glycerate
CC to 3-phosphonooxypyruvate, the first step of the phosphorylated L-
CC serine biosynthesis pathway. Also catalyzes the reversible oxidation of
CC 2-hydroxyglutarate to 2-oxoglutarate. {ECO:0000256|ARBA:ARBA00003800}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phosphoglycerate + NAD(+) = 3-phosphooxypyruvate + H(+)
CC + NADH; Xref=Rhea:RHEA:12641, ChEBI:CHEBI:15378, ChEBI:CHEBI:18110,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58272; EC=1.1.1.95;
CC Evidence={ECO:0000256|ARBA:ARBA00001878};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-2-hydroxyglutarate + NAD(+) = 2-oxoglutarate + H(+) +
CC NADH; Xref=Rhea:RHEA:49612, ChEBI:CHEBI:15378, ChEBI:CHEBI:15801,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.399; Evidence={ECO:0000256|ARBA:ARBA00000646};
CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC 3-phospho-D-glycerate: step 1/3. {ECO:0000256|ARBA:ARBA00005216}.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854}.
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DR EMBL; CP003345; AFM03836.1; -; Genomic_DNA.
DR RefSeq; WP_014797293.1; NC_018018.1.
DR AlphaFoldDB; I4AIQ1; -.
DR STRING; 880071.Fleli_1408; -.
DR KEGG; fli:Fleli_1408; -.
DR PATRIC; fig|880071.3.peg.1385; -.
DR eggNOG; COG0111; Bacteria.
DR eggNOG; COG0560; Bacteria.
DR HOGENOM; CLU_029190_0_0_10; -.
DR OrthoDB; 1522997at2; -.
DR UniPathway; UPA00135; UER00196.
DR Proteomes; UP000006054; Chromosome.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd04901; ACT_3PGDH; 1.
DR CDD; cd12176; PGDH_3; 1.
DR Gene3D; 3.30.70.260; -; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR01488; HAD-SF-IB; 1.
DR PANTHER; PTHR43761:SF1; 2-HACID_DH DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR43761; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR Pfam; PF12710; HAD; 1.
DR SUPFAM; SSF55021; ACT-like; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000006054}.
FT DOMAIN 565..634
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 634 AA; 71664 MW; 17011CCD5FD9F11F CRC64;
MNPTTDKQKY FIIDFDSTFT KVEAMDELCQ IALQNHPEKN ERLSQIQSLT DQAMDGTLSF
RESLHQRIAI LEANKSHLPE LIEKLGEKVS ESFKRNQTFF DTYKDTILIV SSGFKDFIVP
IVTKFGIKTE NIYANEFEFD EDGKIKSFDA SNVLSEDNGK VKLLRNLNLQ GDIYVIGDGY
TDYEIKEAGL ANEFYAFTEN IKRDKVVDKA DREAQNLDEF LYVNKLARNI SYPKNRIKVL
LLENIHQSAK EAMEKEGYQV ELLTSALTED ELIEKIKDIS ILGIRSKTNL TSKVVEHADR
LLAVGAFCIG TNQIDLEACQ DRGIVVFNAP YSNTRSVVEL AIGEMIMLMR GVPKSVMEMH
TGKWNKSATN SFEVRGKKLG IIGYGNIGAQ LSVVAEALGM KVYFYDIVDR LALGNATMCD
SLEELLSISD VISLHVDGRT ENTNIIRKEH FDLMKEGVVF MNLARGQVVD IAALVENLKS
GKILGAGVDV YPEEPKNNQE EFISELRQIP NVILTPHVGG STVEAQENIA QFVPHKMIDY
INAGNTFSSV NFPELQLPKL QNAHRLMHIH KNVPGILAKI NQIFAKNEVN IVGQYLKTNE
KIGYVITDIN QKYHQEVIEE LKNIEDTIRF RILY
//
