ID V4HMB3_9EURY Unreviewed; 318 AA.
AC V4HMB3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Glyoxylate reductase {ECO:0000313|EMBL:ESP89069.1};
GN ORFNames=K933_05678 {ECO:0000313|EMBL:ESP89069.1};
OS Candidatus Halobonum tyrrellensis G22.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Halobonum.
OX NCBI_TaxID=1324957 {ECO:0000313|EMBL:ESP89069.1, ECO:0000313|Proteomes:UP000017840};
RN [1] {ECO:0000313|EMBL:ESP89069.1, ECO:0000313|Proteomes:UP000017840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G22 {ECO:0000313|EMBL:ESP89069.1,
RC ECO:0000313|Proteomes:UP000017840};
RX PubMed=24336364;
RA Ugalde J.A., Narasingarao P., Kuo S., Podell S., Allen E.E.;
RT "Draft Genome Sequence of 'Candidatus Halobonum tyrrellensis' Strain G22,
RT Isolated from the Hypersaline Waters of Lake Tyrrell, Australia.";
RL Genome Announc. 1:e01001-13(2013).
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:ESP89069.1}.
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DR EMBL; ASGZ01000018; ESP89069.1; -; Genomic_DNA.
DR RefSeq; WP_023393723.1; NZ_ASGZ01000018.1.
DR AlphaFoldDB; V4HMB3; -.
DR STRING; 1324957.K933_05678; -.
DR PATRIC; fig|1324957.4.peg.1154; -.
DR eggNOG; arCOG01757; Archaea.
DR OrthoDB; 168224at2157; -.
DR Proteomes; UP000017840; 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 CDD; cd05300; 2-Hacid_dh_1; 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; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43333; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43333:SF1; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000017840}.
FT DOMAIN 29..308
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 111..283
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 318 AA; 34310 MW; 7C65AF61BECE5DC0 CRC64;
MRIVLTRQKI HGHSVDEYAA ALRDRLPDHD IVVARTPDEE REAVTGADVV TGEGHSMGRL
LGEVEAPDLK LFAGVYAGTG HLDLDAFREA GVAVTNASGV HAPNIAEYVV GALVSLARDF
RRATRQQDRR EWRAYQTREL KGSTVTVVGV GSIGEAILQR LEPFGVERLA VRHSPEKGGP
AEEVVGFDGL HDALARTDHL VLACPLTDET EGLIDADALR TLPPEATLVN IARGAVVDTD
ALVSAFNVND LGAAFLDVTD PEPLPEEHPL WGFEDVRITP HNAGHTPAYF GRLVDIVAEN
VERIAGTGET GELRNRVV
//
