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Database: UniProt
Entry: C0QHG2_DESAH
LinkDB: C0QHG2_DESAH
Original site: C0QHG2_DESAH 
ID   C0QHG2_DESAH            Unreviewed;       315 AA.
AC   C0QHG2;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   SubName: Full=SerA2 {ECO:0000313|EMBL:ACN17821.1};
DE            EC=1.1.1.95 {ECO:0000313|EMBL:ACN17821.1};
GN   Name=serA2 {ECO:0000313|EMBL:ACN17821.1};
GN   OrderedLocusNames=HRM2_47720 {ECO:0000313|EMBL:ACN17821.1};
OS   Desulforapulum autotrophicum (strain ATCC 43914 / DSM 3382 / VKM B-1955 /
OS   HRM2) (Desulfobacterium autotrophicum).
OC   Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC   Desulfobacteraceae; Desulforapulum.
OX   NCBI_TaxID=177437 {ECO:0000313|EMBL:ACN17821.1, ECO:0000313|Proteomes:UP000000442};
RN   [1] {ECO:0000313|EMBL:ACN17821.1, ECO:0000313|Proteomes:UP000000442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43914 / DSM 3382 / HRM2
RC   {ECO:0000313|Proteomes:UP000000442};
RX   PubMed=19187283; DOI=10.1111/j.1462-2920.2008.01825.x;
RA   Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J., Andres S.,
RA   Henne A., Fricke W.F., Martinez-Arias R., Bartels D., Goesmann A.,
RA   Krause L., Puehler A., Klenk H.P., Richter M., Schuler M., Gloeckner F.O.,
RA   Meyerdierks A., Gottschalk G., Amann R.;
RT   "Genome sequence of Desulfobacterium autotrophicum HRM2, a marine sulfate
RT   reducer oxidizing organic carbon completely to carbon dioxide.";
RL   Environ. Microbiol. 11:1038-1055(2009).
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR   EMBL; CP001087; ACN17821.1; -; Genomic_DNA.
DR   RefSeq; WP_015906531.1; NC_012108.1.
DR   AlphaFoldDB; C0QHG2; -.
DR   STRING; 177437.HRM2_47720; -.
DR   KEGG; dat:HRM2_47720; -.
DR   eggNOG; COG0111; Bacteria.
DR   HOGENOM; CLU_019796_1_3_7; -.
DR   OrthoDB; 9793626at2; -.
DR   Proteomes; UP000000442; Chromosome.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR   CDD; cd12175; 2-Hacid_dh_11; 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; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR42938:SF25; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN; 1.
DR   PANTHER; PTHR42938; 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.
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   Reference proteome {ECO:0000313|Proteomes:UP000000442}.
FT   DOMAIN          37..311
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          108..283
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   315 AA;  33834 MW;  DA46CB17F894F80A CRC64;
     MNILFAASEN AWGGFLERIR SKLPGHHFRA AGSFHIDSLK GVDVLIPAMT WITREMMETG
     DRLRLIQQCG SGLEGVDIKA ATDQGVSVAN VPAGTSGNAD SVAELGIYMM IGLSRNIQGM
     AQSLRNKKMG EPLGMALPGK TVGIIGLGGI GQALVQRLKP FGVKLMGIKR TNPQQAKDTL
     GLDWAGTPAD LPFLLENCDY VLVCVPATPE SSNMIDGRAF ARMKKTAFLI NLSRGALVNR
     DALEHALESG AIAGVGLDVF WQEPPDPSDP IFNYNVMATP HIAGATDISM ERTADGVAEN
     IRRLAENRPL LHLHQ
//
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