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InterPro: IPR005238 2-phosphosulpholactate phosphatase

Protein matches Help

UniProtKB

Matches:

272 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR005238 2-PSlactate_phosphatase

Type

Family

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:3.90.1560.10	2-PSlactate_phosphatase	254
Pfam	PF04029	2-ph_phosp	272
TIGRFAMs	TIGR00298	2-ph_phosphatase	74
Signatures in BioMart

GO Term annotation Help

Process

GO:0019295 coenzyme M biosynthetic process

Function

GO:0000287 magnesium ion binding
GO:0050532 2-phosphosulfolactate phosphatase activity

InterPro annotation

Entry Details in BioMart

Abstract

2-phosphosulpholactate phosphatase (ComB; EC:3.1.3) is a magnesium-dependent acid phosphatase that catalyzes the second step in coenzyme M (CoM; 2-mercaptoethanesulphonic acid) biosynthesis, namely, the hydrolysis of (2R)-2-phospho-3-sulpholactate to yield (2R)-3-sulpholactate and phosphate. CoM is an essential cofactor that acts as the terminal methyl carrier in methanogenesis [1]. Homologues of ComB have been identified in all available cyanobacterial genome sequences and in genomes from phylogenetically diverse bacteria and archaea. However, many of these organisms lack homologues of other CoM biosynthetic genes. ComB has a complex alpha/beta topology. The monomer is composed of two domains thought to be related by a common ancestral gene, plus a C-terminal helical and beta-hairpin region [2].

Structural links Help

PDB - click here

SCOP: c.148.1.1

CATH: 3.90.1560.10

Database links Help

Enzyme: EC:3.1.3.71

PANDIT: PF04029

Blocks: IPB005238

Taxonomic coverage Help

Example proteins Help

A2C172 Probable 2-phosphosulfolactate phosphatase

O27250 2-phosphosulfolactate phosphatase

P73849 Probable 2-phosphosulfolactate phosphatase

Q5SID6 Probable 2-phosphosulfolactate phosphatase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR005238	2-phosphosulpholactate phosphatase
	SWISS-MODEL
	PDB Chain
	ModBase

Publications Open in usermanual
1.	Graham DE, Graupner M, Xu H, White RH. Identification of coenzyme M biosynthetic 2-phosphosulfolactate phosphatase. A member of a new class of Mg(2+)-dependent acid phosphatases. Eur. J. Biochem. 268 5176-88 2001 [PubMed: 11589710] http://dx.doi.org/10.1046/j.0014-2956.2001.02451.x
2.	DiDonato M, Krishna SS, Schwarzenbacher R, McMullan D, Agarwalla S, Brittain SM, Miller MD, Abdubek P, Ambing E, Axelrod HL, Canaves JM, Chiu HJ, Deacon AM, Duan L, Elsliger MA, Godzik A, Grzechnik SK, Hale J, Hampton E, Haugen J, Jaroszewski L, Jin KK, Klock HE, Knuth MW, Koesema E, Kreusch A, Kuhn P, Lesley SA, Levin I, Morse AT, Nigoghossian E, Okach L, Oommachen S, Paulsen J, Quijano K, Reyes R, Rife CL, Spraggon G, Stevens RC, van den Bedem H, White A, Wolf G, Xu Q, Hodgson KO, Wooley J, Wilson IA. Crystal structure of 2-phosphosulfolactate phosphatase (ComB) from Clostridium acetobutylicum at 2.6 A resolution reveals a new fold with a novel active site. Proteins 65 771-6 2006 [PubMed: 16927339] http://dx.doi.org/10.1002/prot.20978

InterPro 24.0