MDH_PYRHO
ID MDH_PYRHO Reviewed; 360 AA.
AC O59028;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Malate dehydrogenase;
DE EC=1.1.1.37;
GN Name=mdh; OrderedLocusNames=PH1277;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the LDH2/MDH2 oxidoreductase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000001; BAA30380.1; -; Genomic_DNA.
DR PIR; B71073; B71073.
DR RefSeq; WP_010885364.1; NC_000961.1.
DR PDB; 1V9N; X-ray; 2.10 A; A=1-360.
DR PDBsum; 1V9N; -.
DR AlphaFoldDB; O59028; -.
DR SMR; O59028; -.
DR STRING; 70601.3257697; -.
DR PRIDE; O59028; -.
DR EnsemblBacteria; BAA30380; BAA30380; BAA30380.
DR GeneID; 1443600; -.
DR KEGG; pho:PH1277; -.
DR eggNOG; arCOG04874; Archaea.
DR OMA; TNTEPAM; -.
DR OrthoDB; 32318at2157; -.
DR EvolutionaryTrace; O59028; -.
DR Proteomes; UP000000752; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1530.10; -; 1.
DR Gene3D; 3.30.1370.60; -; 1.
DR InterPro; IPR043144; Mal/L-sulf/L-lact_DH-like_ah.
DR InterPro; IPR043143; Mal/L-sulf/L-lact_DH-like_NADP.
DR InterPro; IPR036111; Mal/L-sulfo/L-lacto_DH-like_sf.
DR InterPro; IPR003767; Malate/L-lactate_DH-like.
DR PANTHER; PTHR11091; PTHR11091; 1.
DR Pfam; PF02615; Ldh_2; 1.
DR SUPFAM; SSF89733; SSF89733; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; NAD; Oxidoreductase; Tricarboxylic acid cycle.
FT CHAIN 1..360
FT /note="Malate dehydrogenase"
FT /id="PRO_0000083829"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:1V9N"
FT HELIX 16..29
FT /evidence="ECO:0007829|PDB:1V9N"
FT HELIX 34..49
FT /evidence="ECO:0007829|PDB:1V9N"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:1V9N"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:1V9N"
FT HELIX 60..68
FT /evidence="ECO:0007829|PDB:1V9N"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:1V9N"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:1V9N"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:1V9N"
FT HELIX 97..115
FT /evidence="ECO:0007829|PDB:1V9N"
FT STRAND 116..125
FT /evidence="ECO:0007829|PDB:1V9N"
FT HELIX 132..139
FT /evidence="ECO:0007829|PDB:1V9N"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:1V9N"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:1V9N"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:1V9N"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:1V9N"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:1V9N"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:1V9N"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:1V9N"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:1V9N"
FT TURN 223..227
FT /evidence="ECO:0007829|PDB:1V9N"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:1V9N"
FT HELIX 242..256
FT /evidence="ECO:0007829|PDB:1V9N"
FT TURN 257..261
FT /evidence="ECO:0007829|PDB:1V9N"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:1V9N"
FT STRAND 278..285
FT /evidence="ECO:0007829|PDB:1V9N"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:1V9N"
FT HELIX 293..308
FT /evidence="ECO:0007829|PDB:1V9N"
FT HELIX 324..336
FT /evidence="ECO:0007829|PDB:1V9N"
FT STRAND 338..341
FT /evidence="ECO:0007829|PDB:1V9N"
FT HELIX 342..355
FT /evidence="ECO:0007829|PDB:1V9N"
SQ SEQUENCE 360 AA; 39751 MW; 6E9D8B16ECDE6E6F CRC64;
MFEKGYVDEN YIRVPKDRLF SFIVRVLTKL GVPEEDAKIV ADNLVMADLR GVESHGVQRL
KRYVDGIISG GVNLHPKIRV IREGPSYALI DGDEGLGQVV GYRSMKLAIK KAKDTGIGIV
IARNSNHYGI AGYYALMAAE EGMIGISMTN SRPLVAPTGG IERILGTNPI ALAAPTKDKP
FLLDMATSVV PIGKLEVYRR KGKDIPEGWA INREGNITTK VEEVFNGGAL LPLGGFGELL
GGHKGYGLSL MVDILSGILS GGTWSKYVKN TSEKGSNVCH FFMVIDIEHF IPLEEFKEKI
SQMIEEIKSS RKHPEFERIW IHGEKGFLTM ETRLKLGIPI YRKVLEELNE IAKRVGVEGL
