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Database: UniProt
Entry: A6EAP2_9SPHI
LinkDB: A6EAP2_9SPHI
Original site: A6EAP2_9SPHI 
ID   A6EAP2_9SPHI            Unreviewed;       432 AA.
AC   A6EAP2;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   RecName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000256|ARBA:ARBA00021582};
DE            EC=1.1.1.399 {ECO:0000256|ARBA:ARBA00013001};
DE            EC=3.1.3.3 {ECO:0000256|ARBA:ARBA00012640};
DE   AltName: Full=2-oxoglutarate reductase {ECO:0000256|ARBA:ARBA00030455};
GN   ORFNames=PBAL39_09826 {ECO:0000313|EMBL:EDM37433.1};
OS   Pedobacter sp. BAL39.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=391596 {ECO:0000313|EMBL:EDM37433.1, ECO:0000313|Proteomes:UP000003664};
RN   [1] {ECO:0000313|EMBL:EDM37433.1, ECO:0000313|Proteomes:UP000003664}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BAL39 {ECO:0000313|EMBL:EDM37433.1,
RC   ECO:0000313|Proteomes:UP000003664};
RA   Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUN-2007) 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=(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   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-D-serine = D-serine + phosphate;
CC         Xref=Rhea:RHEA:24873, ChEBI:CHEBI:15377, ChEBI:CHEBI:35247,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58680; EC=3.1.3.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00001197};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-serine = L-serine + phosphate;
CC         Xref=Rhea:RHEA:21208, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57524; EC=3.1.3.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00000860};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC       3-phospho-D-glycerate: step 3/3. {ECO:0000256|ARBA:ARBA00005135}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EDM37433.1}.
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DR   EMBL; ABCM01000004; EDM37433.1; -; Genomic_DNA.
DR   RefSeq; WP_008239860.1; NZ_ABCM01000004.1.
DR   AlphaFoldDB; A6EAP2; -.
DR   STRING; 391596.PBAL39_09826; -.
DR   eggNOG; COG0560; Bacteria.
DR   OrthoDB; 9777288at2; -.
DR   Proteomes; UP000003664; Unassembled WGS sequence.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd04901; ACT_3PGDH; 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; 1.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   NCBIfam; TIGR01488; HAD-SF-IB; 1.
DR   PANTHER; PTHR43344; PHOSPHOSERINE PHOSPHATASE; 1.
DR   PANTHER; PTHR43344:SF2; PHOSPHOSERINE PHOSPHATASE; 1.
DR   Pfam; PF00389; 2-Hacid_dh; 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   PROSITE; PS51671; ACT; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023299};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003664};
KW   Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299}.
FT   DOMAIN          363..432
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   432 AA;  49400 MW;  F00556DB334AE594 CRC64;
     MSQKNIYIID FDSTFTQVEA LDELARISLK KHPDKEAIFQ KIEDYTNLAM EGKLSFGESL
     AQRVKLLEAS EDHLKQLITR LKKKVSASFS RNAAFFKKHA DEVLIVSGGF KEFITPVVSQ
     YHIKKENIYA NTFVTTGDGK IIDYDHSNPL SEEGGKVKLM KQLNLEGNLY GIGDGYSDFQ
     LRESGLIKKF YAFTENISRE SIVLKADHVT PSFDEFLYVN NLPRAISYPK NRILCLIIGE
     VDPQSIEMLK KDGFSIRHKE TFEEKYVADV HMLLLADGQK IEPETLSRAI TLKTIGYLGS
     AKNKLDLLQC TQQGIVVFDD AKSNPRNNKF IPQRMIDFMN TGTTHLSSNF PNLQLPRIDK
     SHRLIHIHKN VPGIMAKINM AFAYHDINIV GQFLMTNPTI GYVITDINTQ YDKQLFKFLK
     KIEHTIKFRV LY
//
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