ID   I3YMW6_ALIFI            Unreviewed;       331 AA.
AC   I3YMW6;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=Phosphoglycerate dehydrogenase-like oxidoreductase {ECO:0000313|EMBL:AFL78334.1};
DE            EC=1.1.1.290 {ECO:0000313|EMBL:AFL78334.1};
GN   OrderedLocusNames=Alfi_2026 {ECO:0000313|EMBL:AFL78334.1};
OS   Alistipes finegoldii (strain DSM 17242 / JCM 16770 / CCUG 46020 / CIP
OS   107999 / KCTC 15236 / AHN 2437).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC   Alistipes.
OX   NCBI_TaxID=679935 {ECO:0000313|EMBL:AFL78334.1, ECO:0000313|Proteomes:UP000006052};
RN   [1] {ECO:0000313|Proteomes:UP000006052}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 17242 / JCM 16770 / AHN 2437 / CCUG 46020 / CIP 107999
RC   {ECO:0000313|Proteomes:UP000006052};
RX   PubMed=23961309; DOI=10.4056/sigs.3527032;
RA   Mavromatis K., Stackebrandt E., Munk C., Lapidus A., Nolan M., Lucas S.,
RA   Hammon N., Deshpande S., Cheng J.F., Tapia R., Goodwin L.A., Pitluck S.,
RA   Liolios K., Pagani I., Ivanova N., Mikhailova N., Huntemann M., Pati A.,
RA   Chen A., Palaniappan K., Land M., Hauser L., Rohde M., Gronow S., Goker M.,
RA   Detter J.C., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Woyke T.;
RT   "Complete genome sequence of the bile-resistant pigment-producing anaerobe
RT   Alistipes finegoldii type strain (AHN2437(T)).";
RL   Stand. Genomic Sci. 8:26-36(2013).
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC       ECO:0000256|RuleBase:RU003719}.
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DR   EMBL; CP003274; AFL78334.1; -; Genomic_DNA.
DR   RefSeq; WP_014775711.1; NC_018011.1.
DR   AlphaFoldDB; I3YMW6; -.
DR   STRING; 679935.Alfi_2026; -.
DR   KEGG; afd:Alfi_2026; -.
DR   PATRIC; fig|679935.3.peg.1956; -.
DR   eggNOG; COG1052; Bacteria.
DR   HOGENOM; CLU_019796_4_0_10; -.
DR   Proteomes; UP000006052; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0033711; F:4-phosphoerythronate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd12158; ErythrP_dh; 1.
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; IPR029753; D-isomer_DH_CS.
DR   InterPro; IPR029752; D-isomer_DH_CS1.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR020921; Erythronate-4-P_DHase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
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   SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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   ECO:0000256|RuleBase:RU003719};
KW   Pyridoxine biosynthesis {ECO:0000256|ARBA:ARBA00023096}.
FT   DOMAIN          31..267
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          107..246
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   331 AA;  36368 MW;  D57F1D5DC47C5E31 CRC64;
     MKIIADSAIP FLQGVLEPWA EVRYLPGAEI APEEVRDADA LLIRTRTRCD ERLLGGSRVR
     LIATATIGFD HIDTAWCAAH GIRVCTAAGC NARGVLQWAG AVLAHLARTQ GWQPAGRTLG
     VVGVGHVGSL VKEYAETWGF RVLCCDPPRE AREHCGFLPL EEVARQADIL TFHTPLDDTT
     RRMAGDALFA RMKPGAVILN SSRGEVVDGA ALLRSGLACV LDVWEHEPAI DRRLLTRTLL
     ATPHIAGYSE QGKANATAMS VDTLARFFGL PLAGWYPPQA APSTPRPISW QELCTTIGGA
     FDIEAQSRSL KARPEDFEPM RDHYRYRREY F
//