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2-phosphosulfolactate phosphatase (EC 3.1.3.71)

 COMB_METJA              Reviewed;         224 AA.
Q58540;
05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
05-DEC-2001, sequence version 2.
05-JUL-2017, entry version 106.
RecName: Full=2-phosphosulfolactate phosphatase;
EC=3.1.3.71;
Name=comB; OrderedLocusNames=MJ1140;
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 /
JCM 10045 / NBRC 100440) (Methanococcus jannaschii).
Archaea; Euryarchaeota; Methanococci; Methanococcales;
Methanocaldococcaceae; Methanocaldococcus.
NCBI_TaxID=243232;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
PubMed=8688087; DOI=10.1126/science.273.5278.1058;
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.;
"Complete genome sequence of the methanogenic archaeon, Methanococcus
jannaschii.";
Science 273:1058-1073(1996).
[2]
CHARACTERIZATION.
STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
PubMed=11589710; DOI=10.1046/j.0014-2956.2001.02451.x;
Graham D.E., Graupner M., Xu H., White R.H.;
"Identification of coenzyme M biosynthetic 2-phosphosulfolactate
phosphatase. A member of a new class of Mg2+-dependent acid
phosphatases.";
Eur. J. Biochem. 268:5176-5188(2001).
-!- 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.
-!- CATALYTIC ACTIVITY: (2R)-2-phospho-3-sulfolactate + H(2)O = (2R)-
3-sulfolactate + phosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- ENZYME REGULATION: Inhibited by vanadate.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 5.5.;
Temperature dependence:
Optimum temperature is 75 degrees Celsius.;
-!- PATHWAY: Cofactor biosynthesis; coenzyme M biosynthesis;
sulfoacetaldehyde from phosphoenolpyruvate and sulfite: step 2/4.
-!- SUBUNIT: Monomer.
-!- SIMILARITY: Belongs to the ComB family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB99140.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; L77117; AAB99140.1; ALT_INIT; Genomic_DNA.
PIR; C64442; C64442.
RefSeq; WP_064496734.1; NC_000909.1.
ProteinModelPortal; Q58540; -.
SMR; Q58540; -.
STRING; 243232.MJ_1140; -.
EnsemblBacteria; AAB99140; AAB99140; MJ_1140.
GeneID; 1452036; -.
KEGG; mja:MJ_1140; -.
eggNOG; arCOG04871; Archaea.
eggNOG; COG2045; LUCA.
InParanoid; Q58540; -.
KO; K05979; -.
OMA; FMSTTNG; -.
OrthoDB; POG093Z07BS; -.
PhylomeDB; Q58540; -.
BioCyc; MetaCyc:MONOMER-2263; -.
UniPathway; UPA00355; UER00470.
Proteomes; UP000000805; Chromosome.
GO; GO:0050532; F:2-phosphosulfolactate phosphatase activity; IEA:UniProtKB-EC.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0050545; F:sulfopyruvate decarboxylase activity; IDA:MENGO.
GO; GO:0019295; P:coenzyme M biosynthetic process; IEA:UniProtKB-UniPathway.
Gene3D; 3.90.1560.10; -; 1.
HAMAP; MF_00490; ComB; 1.
InterPro; IPR005238; ComB-like.
InterPro; IPR027639; ComB_archaeal.
PANTHER; PTHR37311:SF2; PTHR37311:SF2; 1.
Pfam; PF04029; 2-ph_phosp; 1.
SUPFAM; SSF142823; SSF142823; 1.
TIGRFAMs; TIGR00298; TIGR00298; 1.
1: Evidence at protein level;
Coenzyme M biosynthesis; Complete proteome; Hydrolase; Magnesium;
Reference proteome.
CHAIN 1 224 2-phosphosulfolactate phosphatase.
/FTId=PRO_0000081459.
SEQUENCE 224 AA; 25114 MW; B981C5B5635404E9 CRC64;
MITLCNRFTE YKCGNVAIVV DVLRASTTIT TLLSFIDEVY ITTSTSKKEN AIYIGERKGR
KIEGFDFGNS PTEILANKDI IKERYENGEK VILTTTNGTR VLKSLDAEHI FIGAIVNAKY
VAKAVEDFED VSLVPCHREN NFAIDDFIGC GVIAKYLNGE FDEFIKAALE LTKHDWMSLI
LNSSSAENLK NLGYEKDVTF AILENSIDAV GIYKKDKSKV VRFK


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