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Database: UniProt
Entry: A0A1Y4AIU5_9BACE
LinkDB: A0A1Y4AIU5_9BACE
Original site: A0A1Y4AIU5_9BACE 
ID   A0A1Y4AIU5_9BACE        Unreviewed;       306 AA.
AC   A0A1Y4AIU5;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 11.
DE   SubName: Full=3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:OUO19898.1};
GN   ORFNames=B5F91_07670 {ECO:0000313|EMBL:OUO19898.1};
OS   Bacteroides sp. An322.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1965632 {ECO:0000313|EMBL:OUO19898.1, ECO:0000313|Proteomes:UP000195527};
RN   [1] {ECO:0000313|Proteomes:UP000195527}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An322 {ECO:0000313|Proteomes:UP000195527};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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:OUO19898.1}.
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DR   EMBL; NFIN01000011; OUO19898.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y4AIU5; -.
DR   OrthoDB; 9777288at2; -.
DR   Proteomes; UP000195527; 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   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR42938; FORMATE DEHYDROGENASE 1; 1.
DR   PANTHER; PTHR42938:SF9; FORMATE DEHYDROGENASE 1; 1.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000195527}.
FT   DOMAIN          21..305
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          123..250
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   306 AA;  33270 MW;  FDC7BA3BEE4E06C9 CRC64;
     MKILVATEKP FAKVAVDGIR KEIEAAGYEL ALLEKYTDKA QLLDAIKDAN ALIIRSDIID
     NEVLDAAKEL KIVVRAGAGY DNVDLAAATA HGVCVMNTPG QNSNAVAELA FGMMIMAVRN
     FYDGKSGTEL KGKKLGIHAY GNVGRNVARI AKGIGMEIYA YDAYCPKEAM EADGIIPVDS
     AEALYETCNV ISLHIPATAE TKNSINYDLV NRMPKNGLLV NTARKEVINE ADLLRLMNDR
     PDLKYVTDIM PVHHAEFAEQ FPGRYFSTPK KMGAQTAEAN INAGIAAAKQ IVGFLKDGCE
     KFRVNK
//
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