Q58540 (COMB_METJA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
2-phosphosulfolactate phosphatase
EC=3.1.3.71

Gene names

Name:	comB
Ordered Locus Names:	MJ1140

Organism

Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) [Reference proteome] [HAMAP]

Taxonomic identifier

243232 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Euryarchaeota › Methanococci › Methanococcales › Methanocaldococcaceae › Methanocaldococcus › Methanocaldococcus jannaschii

Protein attributes

Sequence length	224 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Coenzyme M biosynthesis
Ligand	Magnesium
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	coenzyme M biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	2-phosphosulfolactate phosphatase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: InterPro sulfopyruvate decarboxylase activity Inferred from direct assay Ref.2. Source: MENGO
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 224	224	2-phosphosulfolactate phosphatase HAMAP-Rule MF_00490		PRO_0000081459

Sequences

	Sequence		Length	Mass (Da)
	Q58540 [UniParc]. Last modified December 5, 2001. Version 2. Checksum: B981C5B5635404E9	FASTA	224	25,114
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii." Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., Kirkness E.F., Weinstock K.G. , Merrick J.M., Glodek A., Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C. Science 273:1058-1073(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
[2]	"Identification of coenzyme M biosynthetic 2-phosphosulfolactate phosphatase. A member of a new class of Mg2+-dependent acid phosphatases." Graham D.E., Graupner M., Xu H., White R.H. Eur. J. Biochem. 268:5176-5188(2001) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION. Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L77117 Genomic DNA. Translation: AAB99140.1. Different initiation.
PIR	C64442.
RefSeq	NP_248132.1. NC_000909.1.
3D structure databases
ProteinModelPortal	Q58540.
ModBase	Search...
Protein-protein interaction databases
STRING	243232.MJ1140.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAB99140; AAB99140; MJ_1140.
GeneID	1452036.
KEGG	mja:MJ_1140.
Phylogenomic databases
eggNOG	COG2045.
KO	K05979.
OMA	MKISISF.
ProtClustDB	CLSK876468.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-2263.
UniPathway	UPA00355; UER00470.
Family and domain databases
Gene3D	3.90.1560.10. 1 hit.
HAMAP	MF_00490. ComB.
InterPro	IPR005238. 2-PSlactate_phosphatase. IPR022995. Pase_ComB. [Graphical view]
Pfam	PF04029. 2-ph_phosp. 1 hit. [Graphical view]
SUPFAM	SSF142823. SSF142823. 1 hit.
TIGRFAMs	TIGR00298. TIGR00298. 1 hit.
ProtoNet	Search...

Entry information

Entry name

COMB_METJA

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program