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Q58540 (COMB_METJA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
2-phosphosulfolactate phosphatase

EC=3.1.3.71
Gene names
Name:comB
Ordered Locus Names:MJ1140
OrganismMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) [Reference proteome] [HAMAP]
Taxonomic identifier243232 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus

Protein attributes

Sequence length224 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes both enantiomers of 2-phosphosulfolactate. Able to hydrolyze both enantiomers of 2-hydroxycarboxylic acids with pseudosymmetric centers of inversion. Specifically hydrolyzes (S)-phospholactate and (S)-phosphoglycerate. HAMAP-Rule MF_00490

Catalytic activity

(2R)-2-phospho-3-sulfolactate + H2O = (2R)-3-sulfolactate + phosphate. HAMAP-Rule MF_00490

Cofactor

Magnesium.

Enzyme regulation

Inhibited by vanadate. HAMAP-Rule MF_00490

Pathway

Cofactor biosynthesis; coenzyme M biosynthesis; sulfoacetaldehyde from phosphoenolpyruvate and sulfite: step 2/4. HAMAP-Rule MF_00490

Subunit structure

Monomer.

Sequence similarities

Belongs to the ComB family.

Biophysicochemical properties

pH dependence:

Optimum pH is 5.5. HAMAP-Rule MF_00490

Temperature dependence:

Optimum temperature is 75 degrees Celsius.

Sequence caution

The sequence AAB99140.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2242242-phosphosulfolactate phosphatase HAMAP-Rule MF_00490
PRO_0000081459

Sequences

Sequence LengthMass (Da)Tools
Q58540 [UniParc].

Last modified December 5, 2001. Version 2.
Checksum: B981C5B5635404E9

FASTA22425,114
        10         20         30         40         50         60 
MITLCNRFTE YKCGNVAIVV DVLRASTTIT TLLSFIDEVY ITTSTSKKEN AIYIGERKGR 

        70         80         90        100        110        120 
KIEGFDFGNS PTEILANKDI IKERYENGEK VILTTTNGTR VLKSLDAEHI FIGAIVNAKY 

       130        140        150        160        170        180 
VAKAVEDFED VSLVPCHREN NFAIDDFIGC GVIAKYLNGE FDEFIKAALE LTKHDWMSLI 

       190        200        210        220 
LNSSSAENLK NLGYEKDVTF AILENSIDAV GIYKKDKSKV VRFK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L77117 Genomic DNA. Translation: AAB99140.1. Different initiation.
PIRC64442.
RefSeqNP_248132.1. NC_000909.1.

3D structure databases

ProteinModelPortalQ58540.
ModBaseSearch...

Protein-protein interaction databases

STRING243232.MJ1140.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB99140; AAB99140; MJ_1140.
GeneID1452036.
KEGGmja:MJ_1140.

Phylogenomic databases

eggNOGCOG2045.
KOK05979.
OMAMKISISF.
ProtClustDBCLSK876468.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-2263.
UniPathwayUPA00355; UER00470.

Family and domain databases

Gene3D3.90.1560.10. 1 hit.
HAMAPMF_00490. ComB.
InterProIPR005238. 2-PSlactate_phosphatase.
IPR022995. Pase_ComB.
[Graphical view]
PfamPF04029. 2-ph_phosp. 1 hit.
[Graphical view]
SUPFAMSSF142823. SSF142823. 1 hit.
TIGRFAMsTIGR00298. TIGR00298. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCOMB_METJA
AccessionPrimary (citable) accession number: Q58540
Entry history
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: December 5, 2001
Last modified: May 29, 2013
This is version 82 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Methanococcus jannaschii

Methanococcus jannaschii: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families