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MDH_HALVD
ID   MDH_HALVD               Reviewed;         304 AA.
AC   Q9P9L2; D4GYB6; Q0MSE3;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 2.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Malate dehydrogenase {ECO:0000250|UniProtKB:O08349};
DE            EC=1.1.1.37 {ECO:0000250|UniProtKB:O08349};
GN   Name=mdh; OrderedLocusNames=HVO_3007;
OS   Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS   NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=309800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Mevarech M.;
RT   "The gene coding for Haloferax volcanii malate dehydrogenase.";
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC   B-1768 / DS2;
RA   Tetsch L., Galinski E.A.;
RT   "Expression of halophilic malate dehydrogenase of Haloferax volcanii.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC   B-1768 / DS2;
RX   PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA   Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA   Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA   Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT   "The complete genome sequence of Haloferax volcanii DS2, a model
RT   archaeon.";
RL   PLoS ONE 5:E9605-E9605(2010).
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC       {ECO:0000250|UniProtKB:O08349}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate;
CC         Xref=Rhea:RHEA:21432, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589,
CC         ChEBI:CHEBI:16452, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.37;
CC         Evidence={ECO:0000250|UniProtKB:O08349};
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. {ECO:0000305}.
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DR   EMBL; AF236112; AAF43044.1; -; Genomic_DNA.
DR   EMBL; DQ851095; ABH10498.1; -; Genomic_DNA.
DR   EMBL; CP001956; ADE04975.1; -; Genomic_DNA.
DR   RefSeq; WP_004044925.1; NZ_AOHU01000104.1.
DR   PDB; 4BGU; X-ray; 1.49 A; A/B/C/D=2-304.
DR   PDBsum; 4BGU; -.
DR   AlphaFoldDB; Q9P9L2; -.
DR   SMR; Q9P9L2; -.
DR   STRING; 309800.C498_18200; -.
DR   EnsemblBacteria; ADE04975; ADE04975; HVO_3007.
DR   GeneID; 8925993; -.
DR   KEGG; hvo:HVO_3007; -.
DR   eggNOG; arCOG00246; Archaea.
DR   HOGENOM; CLU_045401_1_1_2; -.
DR   OMA; CYIIVLT; -.
DR   OrthoDB; 69007at2157; -.
DR   Proteomes; UP000008243; Chromosome.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.110.10; -; 1.
DR   InterPro; IPR001557; L-lactate/malate_DH.
DR   InterPro; IPR022383; Lactate/malate_DH_C.
DR   InterPro; IPR001236; Lactate/malate_DH_N.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   PRINTS; PR00086; LLDHDRGNASE.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF56327; SSF56327; 1.
PE   1: Evidence at protein level;
KW   3D-structure; NAD; Oxidoreductase; Reference proteome;
KW   Tricarboxylic acid cycle.
FT   CHAIN           1..304
FT                   /note="Malate dehydrogenase"
FT                   /id="PRO_0000113483"
FT   ACT_SITE        176
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         8..14
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:O08349"
FT   BINDING         34
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:O08349"
FT   BINDING         83
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         89
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         96
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:O08349"
FT   BINDING         119..121
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:O08349"
FT   BINDING         121
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         152
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   CONFLICT        17
FT                   /note="A -> G (in Ref. 1; AAF43044)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        285
FT                   /note="Missing (in Ref. 1; AAF43044)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        290
FT                   /note="D -> N (in Ref. 1; AAF43044)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        297
FT                   /note="R -> L (in Ref. 1; AAF43044)"
FT                   /evidence="ECO:0000305"
FT   STRAND          3..8
FT                   /evidence="ECO:0007829|PDB:4BGU"
FT   HELIX           12..24
FT                   /evidence="ECO:0007829|PDB:4BGU"
FT   STRAND          28..33
FT                   /evidence="ECO:0007829|PDB:4BGU"
FT   HELIX           36..38
FT                   /evidence="ECO:0007829|PDB:4BGU"
FT   HELIX           39..53
FT                   /evidence="ECO:0007829|PDB:4BGU"
FT   TURN            54..56
FT                   /evidence="ECO:0007829|PDB:4BGU"
FT   STRAND          60..63
FT                   /evidence="ECO:0007829|PDB:4BGU"
FT   HELIX           66..69
FT                   /evidence="ECO:0007829|PDB:4BGU"
FT   STRAND          73..77
FT                   /evidence="ECO:0007829|PDB:4BGU"
FT   HELIX           89..108
FT                   /evidence="ECO:0007829|PDB:4BGU"
FT   STRAND          115..118
FT                   /evidence="ECO:0007829|PDB:4BGU"
FT   HELIX           123..132
FT                   /evidence="ECO:0007829|PDB:4BGU"
FT   STRAND          134..136
FT                   /evidence="ECO:0007829|PDB:4BGU"
FT   HELIX           138..140
FT                   /evidence="ECO:0007829|PDB:4BGU"
FT   STRAND          141..143
FT                   /evidence="ECO:0007829|PDB:4BGU"
FT   HELIX           146..161
FT                   /evidence="ECO:0007829|PDB:4BGU"
FT   HELIX           165..167
FT                   /evidence="ECO:0007829|PDB:4BGU"
FT   STRAND          172..174
FT                   /evidence="ECO:0007829|PDB:4BGU"
FT   STRAND          180..182
FT                   /evidence="ECO:0007829|PDB:4BGU"
FT   HELIX           184..186
FT                   /evidence="ECO:0007829|PDB:4BGU"
FT   HELIX           198..216
FT                   /evidence="ECO:0007829|PDB:4BGU"
FT   TURN            217..219
FT                   /evidence="ECO:0007829|PDB:4BGU"
FT   HELIX           224..238
FT                   /evidence="ECO:0007829|PDB:4BGU"
FT   STRAND          244..253
FT                   /evidence="ECO:0007829|PDB:4BGU"
FT   HELIX           254..256
FT                   /evidence="ECO:0007829|PDB:4BGU"
FT   STRAND          258..269
FT                   /evidence="ECO:0007829|PDB:4BGU"
FT   STRAND          272..276
FT                   /evidence="ECO:0007829|PDB:4BGU"
FT   HELIX           283..303
FT                   /evidence="ECO:0007829|PDB:4BGU"
SQ   SEQUENCE   304 AA;  32654 MW;  7AD72EDC9C137268 CRC64;
     MTKVSVIGAA GTVGAAAGYN LALRDVCDEL VFVDIPKMED KTVGQAADTN HGIAYDSNTV
     VTQGGYEDTA GSDVVVITAG IPRQPGQTRI DLAGDNAPIM DDIGSSLAEY NDDFVSITTS
     NPVDLLNRHL YETGDRDRHK VIGFGGRLDS ARFRYVLSQR FDVPVKNVDA TILGEHGDAQ
     VPVFSKVRVD GNDPAFSADE KEEILGDLQE SAMDVIERKG ATQWGPATGV AHMVEAVLHD
     TGEVLPGSLV LDGEFGYEDT AFGVPVKLGS NGIEEVVEWD LDDYEADLMD DAAEKLRDQY
     DEIA
 
 
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