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Protein

L-sulfolactate dehydrogenase

Gene

comC

Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reduction of sulfopyruvate to (R)-sulfolactate much more efficiently than the reverse reaction. Also catalyzes the reduction of oxaloacetate, alpha-ketoglutarate, and to a much lower extent, KHTCA, but not pyruvate. Involved in the biosynthesis of both coenzyme M (with (R)-sulfolactate) and methanopterin (with alpha-ketoglutarate).1 Publication

Catalytic activityi

A (2S)-2-hydroxycarboxylate + NAD+ = a 2-oxocarboxylate + NADH.

Pathwayi: coenzyme M biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes sulfoacetaldehyde from phosphoenolpyruvate and sulfite.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Phosphosulfolactate synthase (comA)
  2. 2-phosphosulfolactate phosphatase (comB)
  3. L-sulfolactate dehydrogenase (comC)
  4. Sulfopyruvate decarboxylase subunit alpha (comD), Sulfopyruvate decarboxylase subunit beta (comE)
This subpathway is part of the pathway coenzyme M biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes sulfoacetaldehyde from phosphoenolpyruvate and sulfite, the pathway coenzyme M biosynthesis and in Cofactor biosynthesis.

Pathwayi: 5,6,7,8-tetrahydromethanopterin biosynthesis

This protein is involved in the pathway 5,6,7,8-tetrahydromethanopterin biosynthesis, which is part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the pathway 5,6,7,8-tetrahydromethanopterin biosynthesis and in Cofactor biosynthesis.

GO - Molecular functioni

  • oxidoreductase activity Source: UniProtKB-KW
  • sulfopyruvate decarboxylase activity Source: MENGO

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Coenzyme M biosynthesis

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-2264.
RETL1328306-WGS:GSTH-4783-MONOMER.
BRENDAi1.1.1.337. 3260.
SABIO-RKQ58820.
UniPathwayiUPA00065.
UPA00355; UER00471.

Names & Taxonomyi

Protein namesi
Recommended name:
L-sulfolactate dehydrogenase (EC:1.1.1.337)
Alternative name(s):
(R)-2-hydroxyacid dehydrogenase
(R)-sulfolactate dehydrogenase
L-2-hydroxycarboxylate dehydrogenase (NAD(+))
Gene namesi
Name:comC
Synonyms:mdh
Ordered Locus Names:MJ1425
OrganismiMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Taxonomic identifieri243232 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus
Proteomesi
  • UP000000805 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 344344L-sulfolactate dehydrogenasePRO_0000083824Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi243232.MJ_1425.

Structurei

Secondary structure

1
344
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1814Combined sources
Helixi23 – 3917Combined sources
Helixi42 – 443Combined sources
Helixi46 – 483Combined sources
Helixi49 – 579Combined sources
Beta strandi60 – 645Combined sources
Beta strandi68 – 725Combined sources
Beta strandi74 – 807Combined sources
Helixi86 – 10419Combined sources
Beta strandi105 – 1139Combined sources
Helixi121 – 1288Combined sources
Turni129 – 1313Combined sources
Beta strandi132 – 1387Combined sources
Beta strandi158 – 1647Combined sources
Beta strandi169 – 17911Combined sources
Helixi182 – 1898Combined sources
Beta strandi198 – 2003Combined sources
Beta strandi202 – 2065Combined sources
Helixi210 – 2156Combined sources
Beta strandi216 – 2183Combined sources
Beta strandi220 – 2223Combined sources
Helixi223 – 23614Combined sources
Turni237 – 2415Combined sources
Helixi245 – 2473Combined sources
Beta strandi261 – 2677Combined sources
Helixi269 – 2713Combined sources
Helixi275 – 29016Combined sources
Helixi305 – 3139Combined sources
Turni314 – 3163Combined sources
Helixi322 – 33413Combined sources
Helixi339 – 3413Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2X06X-ray2.50A/B/C/D/E/F/G/H1-344[»]
ProteinModelPortaliQ58820.
SMRiQ58820. Positions 1-344.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ58820.

Family & Domainsi

Sequence similaritiesi

Belongs to the LDH2/MDH2 oxidoreductase family.Curated

Phylogenomic databases

eggNOGiarCOG04874. Archaea.
COG2055. LUCA.
InParanoidiQ58820.
KOiK05884.
OMAiIPTDWAL.
PhylomeDBiQ58820.

Family and domain databases

InterProiIPR003767. Malate/L-lactate_DH.
[Graphical view]
PANTHERiPTHR11091. PTHR11091. 1 hit.
PfamiPF02615. Ldh_2. 1 hit.
[Graphical view]
SUPFAMiSSF89733. SSF89733. 1 hit.

Sequencei

Sequence statusi: Complete.

Q58820-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MILKPENEKK LIIDVLKKFG VPEEDAKITA DVFVDADLKG FTSHGIGRFP
60 70 80 90 100
QYITALKLGN INPKPDIKIV KESPATAVID GDLGLGQVVG KKAMELAIKK
110 120 130 140 150
AKNVGVGVVA TRNANHFGIA GYYSELAMNQ DMIGITITNT EPAMAPFGGK
160 170 180 190 200
EKILGTNPIA IAFKGNKYKF SLDMATASIA RGKILEALRK KIKIPEGCAV
210 220 230 240 250
DKDGKPTTDP AKALEGCILP FGGPKGYGLA LAIEMLSAIG GAEVGTKVKG
260 270 280 290 300
TANPEERCTK GDLFIAINPE FFMGKEEFKR KVDELLDEIK NSEPAEGFEI
310 320 330 340
LIPGEIEERN KMKRKDGFEI DKNLYNQLKE ICNELGLNIE DYIE
Length:344
Mass (Da):37,358
Last modified:November 1, 1997 - v1
Checksum:iDD6B9086923CD298
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB99436.1.
PIRiH64477.

Genome annotation databases

EnsemblBacteriaiAAB99436; AAB99436; MJ_1425.
KEGGimja:MJ_1425.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB99436.1.
PIRiH64477.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2X06X-ray2.50A/B/C/D/E/F/G/H1-344[»]
ProteinModelPortaliQ58820.
SMRiQ58820. Positions 1-344.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243232.MJ_1425.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB99436; AAB99436; MJ_1425.
KEGGimja:MJ_1425.

Phylogenomic databases

eggNOGiarCOG04874. Archaea.
COG2055. LUCA.
InParanoidiQ58820.
KOiK05884.
OMAiIPTDWAL.
PhylomeDBiQ58820.

Enzyme and pathway databases

UniPathwayiUPA00065.
UPA00355; UER00471.
BioCyciMetaCyc:MONOMER-2264.
RETL1328306-WGS:GSTH-4783-MONOMER.
BRENDAi1.1.1.337. 3260.
SABIO-RKQ58820.

Miscellaneous databases

EvolutionaryTraceiQ58820.

Family and domain databases

InterProiIPR003767. Malate/L-lactate_DH.
[Graphical view]
PANTHERiPTHR11091. PTHR11091. 1 hit.
PfamiPF02615. Ldh_2. 1 hit.
[Graphical view]
SUPFAMiSSF89733. SSF89733. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiCOMC_METJA
AccessioniPrimary (citable) accession number: Q58820
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: September 7, 2016
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Methanococcus jannaschii
    Methanococcus jannaschii: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.