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
//