Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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.
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)DescriptionActionsGraphical viewLength
ChainiPRO_00000838241 – 344L-sulfolactate dehydrogenaseAdd BLAST344

Interactioni

Protein-protein interaction databases

STRINGi243232.MJ_1425.

Structurei

Secondary structure

1344
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 18Combined sources14
Helixi23 – 39Combined sources17
Helixi42 – 44Combined sources3
Helixi46 – 48Combined sources3
Helixi49 – 57Combined sources9
Beta strandi60 – 64Combined sources5
Beta strandi68 – 72Combined sources5
Beta strandi74 – 80Combined sources7
Helixi86 – 104Combined sources19
Beta strandi105 – 113Combined sources9
Helixi121 – 128Combined sources8
Turni129 – 131Combined sources3
Beta strandi132 – 138Combined sources7
Beta strandi158 – 164Combined sources7
Beta strandi169 – 179Combined sources11
Helixi182 – 189Combined sources8
Beta strandi198 – 200Combined sources3
Beta strandi202 – 206Combined sources5
Helixi210 – 215Combined sources6
Beta strandi216 – 218Combined sources3
Beta strandi220 – 222Combined sources3
Helixi223 – 236Combined sources14
Turni237 – 241Combined sources5
Helixi245 – 247Combined sources3
Beta strandi261 – 267Combined sources7
Helixi269 – 271Combined sources3
Helixi275 – 290Combined sources16
Helixi305 – 313Combined sources9
Turni314 – 316Combined sources3
Helixi322 – 334Combined sources13
Helixi339 – 341Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2X06X-ray2.50A/B/C/D/E/F/G/H1-344[»]
ProteinModelPortaliQ58820.
SMRiQ58820.
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.
RefSeqiWP_010870943.1. NC_000909.1.

Genome annotation databases

EnsemblBacteriaiAAB99436; AAB99436; MJ_1425.
GeneIDi1452329.
KEGGimja:MJ_1425.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB99436.1.
PIRiH64477.
RefSeqiWP_010870943.1. NC_000909.1.

3D structure databases

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

Protein-protein interaction databases

STRINGi243232.MJ_1425.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB99436; AAB99436; MJ_1425.
GeneIDi1452329.
KEGGimja:MJ_1425.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00065.
UPA00355; UER00471.
BioCyciMetaCyc:MONOMER-2264.
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: November 2, 2016
This is version 111 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.