COMC_METJA
ID COMC_METJA Reviewed; 344 AA.
AC Q58820;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=L-sulfolactate dehydrogenase;
DE EC=1.1.1.337;
DE AltName: Full=(R)-2-hydroxyacid dehydrogenase;
DE AltName: Full=(R)-sulfolactate dehydrogenase;
DE AltName: Full=L-2-hydroxycarboxylate dehydrogenase (NAD(+));
GN Name=comC; Synonyms=mdh; OrderedLocusNames=MJ1425;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION.
RX PubMed=10850983; DOI=10.1128/jb.182.13.3688-3692.2000;
RA Graupner M., Xu H., White R.H.;
RT "Identification of an archaeal 2-hydroxy acid dehydrogenase catalyzing
RT reactions involved in coenzyme biosynthesis in methanoarchaea.";
RL J. Bacteriol. 182:3688-3692(2000).
CC -!- FUNCTION: Catalyzes the reduction of sulfopyruvate to (R)-sulfolactate
CC much more efficiently than the reverse reaction. Also catalyzes the
CC reduction of oxaloacetate, alpha-ketoglutarate, and to a much lower
CC extent, KHTCA, but not pyruvate. Involved in the biosynthesis of both
CC coenzyme M (with (R)-sulfolactate) and methanopterin (with alpha-
CC ketoglutarate). {ECO:0000269|PubMed:10850983}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (2S)-2-hydroxycarboxylate + NAD(+) = a 2-oxocarboxylate +
CC H(+) + NADH; Xref=Rhea:RHEA:34555, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:35179, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58123; EC=1.1.1.337;
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme M biosynthesis;
CC sulfoacetaldehyde from phosphoenolpyruvate and sulfite: step 3/4.
CC -!- PATHWAY: Cofactor biosynthesis; 5,6,7,8-tetrahydromethanopterin
CC biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the LDH2/MDH2 oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; L77117; AAB99436.1; -; Genomic_DNA.
DR PIR; H64477; H64477.
DR RefSeq; WP_010870943.1; NC_000909.1.
DR PDB; 2X06; X-ray; 2.50 A; A/B/C/D/E/F/G/H=1-344.
DR PDBsum; 2X06; -.
DR AlphaFoldDB; Q58820; -.
DR SMR; Q58820; -.
DR STRING; 243232.MJ_1425; -.
DR EnsemblBacteria; AAB99436; AAB99436; MJ_1425.
DR GeneID; 1452329; -.
DR KEGG; mja:MJ_1425; -.
DR eggNOG; arCOG04874; Archaea.
DR HOGENOM; CLU_040452_3_1_2; -.
DR InParanoid; Q58820; -.
DR OMA; TNTEPAM; -.
DR OrthoDB; 32318at2157; -.
DR PhylomeDB; Q58820; -.
DR BioCyc; MetaCyc:MON-2264; -.
DR BRENDA; 1.1.1.337; 3260.
DR SABIO-RK; Q58820; -.
DR UniPathway; UPA00065; -.
DR UniPathway; UPA00355; UER00471.
DR EvolutionaryTrace; Q58820; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0102443; F:L-2-hydroxycarboxylate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0050545; F:sulfopyruvate decarboxylase activity; IDA:MENGO.
DR GO; GO:0019295; P:coenzyme M biosynthetic process; IEA:UniProtKB-UniPathway.
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; Coenzyme M biosynthesis; Cytoplasm; NAD; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..344
FT /note="L-sulfolactate dehydrogenase"
FT /id="PRO_0000083824"
FT HELIX 5..18
FT /evidence="ECO:0007829|PDB:2X06"
FT HELIX 23..39
FT /evidence="ECO:0007829|PDB:2X06"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:2X06"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:2X06"
FT HELIX 49..57
FT /evidence="ECO:0007829|PDB:2X06"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:2X06"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:2X06"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:2X06"
FT HELIX 86..104
FT /evidence="ECO:0007829|PDB:2X06"
FT STRAND 105..113
FT /evidence="ECO:0007829|PDB:2X06"
FT HELIX 121..128
FT /evidence="ECO:0007829|PDB:2X06"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:2X06"
FT STRAND 132..138
FT /evidence="ECO:0007829|PDB:2X06"
FT STRAND 158..164
FT /evidence="ECO:0007829|PDB:2X06"
FT STRAND 169..179
FT /evidence="ECO:0007829|PDB:2X06"
FT HELIX 182..189
FT /evidence="ECO:0007829|PDB:2X06"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:2X06"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:2X06"
FT HELIX 210..215
FT /evidence="ECO:0007829|PDB:2X06"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:2X06"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:2X06"
FT HELIX 223..236
FT /evidence="ECO:0007829|PDB:2X06"
FT TURN 237..241
FT /evidence="ECO:0007829|PDB:2X06"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:2X06"
FT STRAND 261..267
FT /evidence="ECO:0007829|PDB:2X06"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:2X06"
FT HELIX 275..290
FT /evidence="ECO:0007829|PDB:2X06"
FT HELIX 305..313
FT /evidence="ECO:0007829|PDB:2X06"
FT TURN 314..316
FT /evidence="ECO:0007829|PDB:2X06"
FT HELIX 322..334
FT /evidence="ECO:0007829|PDB:2X06"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:2X06"
SQ SEQUENCE 344 AA; 37358 MW; DD6B9086923CD298 CRC64;
MILKPENEKK LIIDVLKKFG VPEEDAKITA DVFVDADLKG FTSHGIGRFP QYITALKLGN
INPKPDIKIV KESPATAVID GDLGLGQVVG KKAMELAIKK AKNVGVGVVA TRNANHFGIA
GYYSELAMNQ DMIGITITNT EPAMAPFGGK EKILGTNPIA IAFKGNKYKF SLDMATASIA
RGKILEALRK KIKIPEGCAV DKDGKPTTDP AKALEGCILP FGGPKGYGLA LAIEMLSAIG
GAEVGTKVKG TANPEERCTK GDLFIAINPE FFMGKEEFKR KVDELLDEIK NSEPAEGFEI
LIPGEIEERN KMKRKDGFEI DKNLYNQLKE ICNELGLNIE DYIE
