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Database: UniProt
Entry: O66939_AQUAE
LinkDB: O66939_AQUAE
Original site: O66939_AQUAE 
ID   O66939_AQUAE            Unreviewed;       334 AA.
AC   O66939;
DT   01-AUG-1998, integrated into UniProtKB/TrEMBL.
DT   01-AUG-1998, sequence version 1.
DT   18-JUL-2018, entry version 120.
DE   SubName: Full=D-lactate dehydrogenase {ECO:0000313|EMBL:AAC06898.1};
GN   Name=ldhA {ECO:0000313|EMBL:AAC06898.1};
GN   OrderedLocusNames=aq_727 {ECO:0000313|EMBL:AAC06898.1};
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324 {ECO:0000313|EMBL:AAC06898.1, ECO:0000313|Proteomes:UP000000798};
RN   [1] {ECO:0000313|EMBL:AAC06898.1, ECO:0000313|Proteomes:UP000000798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5 {ECO:0000313|EMBL:AAC06898.1,
RC   ECO:0000313|Proteomes:UP000000798};
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olson G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex
RT   aeolicus.";
RL   Nature 392:353-358(1998).
RN   [2] {ECO:0000213|PDB:3KB6}
RP   X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) IN COMPLEX WITH LACTATE AND
RP   NAD, AND DISULFIDE BONDS.
RX   PubMed=20054113; DOI=10.1107/S1744309109044935;
RA   Antonyuk S.V., Strange R.W., Ellis M.J., Bessho Y., Kuramitsu S.,
RA   Inoue Y., Yokoyama S., Hasnain S.S.;
RT   "Structure of D-lactate dehydrogenase from Aquifex aeolicus complexed
RT   with NAD(+) and lactic acid (or pyruvate).";
RL   Acta Crystallogr. F Struct. Biol. Commun. 65:1209-1213(2009).
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR   EMBL; AE000657; AAC06898.1; -; Genomic_DNA.
DR   PIR; G70363; G70363.
DR   RefSeq; NP_213499.1; NC_000918.1.
DR   RefSeq; WP_010880437.1; NC_000918.1.
DR   PDB; 3KB6; X-ray; 2.12 A; A/B/C/D=1-334.
DR   PDBsum; 3KB6; -.
DR   ProteinModelPortal; O66939; -.
DR   STRING; 224324.aq_727; -.
DR   EnsemblBacteria; AAC06898; AAC06898; aq_727.
DR   GeneID; 1193388; -.
DR   KEGG; aae:aq_727; -.
DR   PATRIC; fig|224324.8.peg.582; -.
DR   eggNOG; ENOG4105C5I; Bacteria.
DR   eggNOG; COG1052; LUCA.
DR   HOGENOM; HOG000136695; -.
DR   InParanoid; O66939; -.
DR   KO; K03778; -.
DR   OMA; THKAYNR; -.
DR   OrthoDB; POG091H04R6; -.
DR   BioCyc; AAEO224324:G1G15-520-MONOMER; -.
DR   BRENDA; 1.1.1.28; 396.
DR   EvolutionaryTrace; O66939; -.
DR   Proteomes; UP000000798; 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   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   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF51735; SSF51735; 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   1: Evidence at protein level;
KW   3D-structure {ECO:0000213|PDB:3KB6};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000798};
KW   NAD {ECO:0000213|PDB:3KB6};
KW   Nucleotide-binding {ECO:0000213|PDB:3KB6};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000798}.
FT   DOMAIN        3    321       2-Hacid_dh. {ECO:0000259|Pfam:PF00389}.
FT   DOMAIN      106    296       2-Hacid_dh_C. {ECO:0000259|Pfam:PF02826}.
FT   NP_BIND     151    152       NAD. {ECO:0000213|PDB:3KB6}.
FT   NP_BIND     229    231       NAD. {ECO:0000213|PDB:3KB6}.
FT   REGION       73     74       Lactate binding. {ECO:0000213|PDB:3KB6}.
FT   BINDING      96     96       Lactate. {ECO:0000213|PDB:3KB6}.
FT   BINDING     171    171       NAD. {ECO:0000213|PDB:3KB6}.
FT   BINDING     203    203       NAD. {ECO:0000213|PDB:3KB6}.
FT   BINDING     231    231       Lactate. {ECO:0000213|PDB:3KB6}.
FT   BINDING     255    255       NAD. {ECO:0000213|PDB:3KB6}.
FT   BINDING     294    294       Lactate. {ECO:0000213|PDB:3KB6}.
FT   BINDING     297    297       NAD; via amide nitrogen.
FT                                {ECO:0000213|PDB:3KB6}.
FT   DISULFID    169    183       {ECO:0000213|PDB:3KB6}.
SQ   SEQUENCE   334 AA;  38071 MW;  6D4C1C4789CB7B00 CRC64;
     MNVLFTSVPQ EDVPFYQEAL KDLSLKIYTT DVSKVPENEL KKAELISVFV YDKLTEELLS
     KMPRLKLIHT RSVGFDHIDL DYCKKKGILV THIPAYSPES VAEHTFAMIL TLVKRLKRIE
     DRVKKLNFSQ DSEILARELN RLTLGVIGTG RIGSRVAMYG LAFGMKVLCY DVVKREDLKE
     KGCVYTSLDE LLKESDVISL HVPYTKETHH MINEERISLM KDGVYLINTA RGKVVDTDAL
     YRAYQRGKFS GLGLDVFEDE EILILKKYTE GKATDKNLKI LELACKDNVI ITPHIAYYTD
     KSLERIREET VKVVKAFVKG DLEQIKGNFV VGPS
//
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