ID A5MZD1_CLOK5 Unreviewed; 326 AA.
AC A5MZD1;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 24-JAN-2024, entry version 90.
DE SubName: Full=Predicted alpha-keto acid dehydrogenase {ECO:0000313|EMBL:EDK34227.1};
DE EC=1.1.1.- {ECO:0000313|EMBL:EDK34227.1};
GN OrderedLocusNames=CKL_2215 {ECO:0000313|EMBL:EDK34227.1};
OS Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=431943 {ECO:0000313|EMBL:EDK34227.1, ECO:0000313|Proteomes:UP000002411};
RN [1] {ECO:0000313|EMBL:EDK34227.1, ECO:0000313|Proteomes:UP000002411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8527 / DSM 555 / NCIMB 10680
RC {ECO:0000313|Proteomes:UP000002411};
RX PubMed=18218779; DOI=10.1073/pnas.0711093105;
RA Seedorf H., Fricke W.F., Veith B., Brueggemann H., Liesegang H.,
RA Strittmatter A., Miethke M., Buckel W., Hinderberger J., Li F.,
RA Hagemeier C., Thauer R.K., Gottschalk G.;
RT "The genome of Clostridium kluyveri, a strict anaerobe with unique
RT metabolic features.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2128-2133(2008).
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; CP000673; EDK34227.1; -; Genomic_DNA.
DR RefSeq; WP_012102555.1; NC_009706.1.
DR AlphaFoldDB; A5MZD1; -.
DR SMR; A5MZD1; -.
DR STRING; 431943.CKL_2215; -.
DR KEGG; ckl:CKL_2215; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_1_9; -.
DR OMA; AGNWQAT; -.
DR Proteomes; UP000002411; Chromosome.
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; cd12185; HGDH_LDH_like; 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; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43026; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-RELATED; 1.
DR PANTHER; PTHR43026:SF1; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-RELATED; 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; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719,
KW ECO:0000313|EMBL:EDK34227.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002411}.
FT DOMAIN 13..325
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 109..294
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 326 AA; 36766 MW; 0A77EAB2D43468BF CRC64;
MKILAYSYRA DETVYFQEFS KKYKVEVVLC DDAPNMENAE LARGFQCVSI VTTPVSGELV
EKFHEMGVKF ISTRTIGYDH IDIEKARQLD MHVGNVTYSP SSVADHTVMV ILMTIRKMKV
IMQCTSVQDY SLKGVQGREL HNLTVGVIGT GKIGQRVIKN LSGFGCKIIA HSSHENEDVK
KYADYVSLEE LLKSSNIITL HIPARKNNYH IIDKNSIDMM KEGVFIINTA RGSLINTEDL
IEGIEKKKIA GAALDVIEHE SDLYYNDLKC EILNNRQLAI LKSYPNVIIT PHTAFYTDQS
VSDMVENSIL SCTLFMEGEQ NPWQVI
//