LOCUS YP_188037 253 aa linear BCT 21-DEC-2012
DEFINITION triosephosphate isomerase [Staphylococcus epidermidis RP62A].
ACCESSION YP_188037
VERSION YP_188037.1 GI:57866429
DBLINK Project: 57663
BioProject: PRJNA57663
DBSOURCE REFSEQ: accession NC_002976.3
KEYWORDS .
SOURCE Staphylococcus epidermidis RP62A
ORGANISM Staphylococcus epidermidis RP62A
Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
REFERENCE 1 (residues 1 to 253)
AUTHORS Gill,S.R., Fouts,D.E., Archer,G.L., Mongodin,E.F., Deboy,R.T.,
Ravel,J., Paulsen,I.T., Kolonay,J.F., Brinkac,L., Beanan,M.,
Dodson,R.J., Daugherty,S.C., Madupu,R., Angiuoli,S.V., Durkin,A.S.,
Haft,D.H., Vamathevan,J., Khouri,H., Utterback,T., Lee,C.,
Dimitrov,G., Jiang,L., Qin,H., Weidman,J., Tran,K., Kang,K.,
Hance,I.R., Nelson,K.E. and Fraser,C.M.
TITLE Insights on evolution of virulence and resistance from the complete
genome analysis of an early methicillin-resistant Staphylococcus
aureus strain and a biofilm-producing methicillin-resistant
Staphylococcus epidermidis strain
JOURNAL J. Bacteriol. 187 (7), 2426-2438 (2005)
PUBMED 15774886
REFERENCE 2 (residues 1 to 253)
AUTHORS Gill,S.R.
TITLE Direct Submission
JOURNAL Submitted (20-OCT-2004) The Institute for Genomic Research, 9712
Medical Center Dr, Rockville, MD 20850, USA
REFERENCE 3 (residues 1 to 253)
CONSRTM NCBI Genome Project
TITLE Direct Submission
JOURNAL Submitted (08-APR-2002) National Center for Biotechnology
Information, NIH, Bethesda, MD 20894, USA
COMMENT PROVISIONAL REFSEQ: This record has not yet been subject to final
NCBI review. The reference sequence was derived from AAW53875.
Method: conceptual translation.
FEATURES Location/Qualifiers
source 1..253
/organism="Staphylococcus epidermidis RP62A"
/strain="RP62A"
/db_xref="taxon:176279"
Protein 1..253
/product="triosephosphate isomerase"
/EC_number="5.3.1.1"
/calculated_mol_wt=27237
Region 4..250
/region_name="TIM"
/note="Triosephosphate isomerase (TIM) is a glycolytic
enzyme that catalyzes the interconversion of
dihydroxyacetone phosphate and
D-glyceraldehyde-3-phosphate. The reaction is very
efficient and requires neither cofactors nor metal ions.
TIM, usually...; cd00311"
/db_xref="CDD:238190"
Region 5..252
/region_name="PRK14565"
/note="triosephosphate isomerase; Provisional"
/db_xref="CDD:237758"
Site order(9,11,97,169,175,215,234,236..237)
/site_type="other"
/note="substrate binding site [chemical binding]"
/db_xref="CDD:238190"
Site order(9,12,43..45,47,50,66,84,87..88,99..100)
/site_type="other"
/note="dimer interface [polypeptide binding]"
/db_xref="CDD:238190"
Site order(11,97,169)
/site_type="active"
/note="catalytic triad [active]"
/db_xref="CDD:238190"
CDS 1..253
/gene="tpiA"
/locus_tag="SERP0444"
/coded_by="NC_002976.3:448998..449759"
/note="Reversibly isomerizes the ketone sugar
dihydroxyacetone phosphate to the aldehyde sugar
glyceraldehyde-3-phosphate"
/transl_table=11
/db_xref="GeneID:3242274"
ORIGIN
1 mrtpiiagnw kmnktvqeak dfvnelptlp dpkevesvic aptiqldalv tavkdgkakg
61 lkigaqnayf eesgaytget spvalselgv kyvvighser rdyfhetdee vnkkahaifn
121 hgmtpiicvg esdeereagk ankivgnqvk kaveglsddq lkevviayep iwaigtgkss
181 tsedanemca hvrqtladls sqevadatri qyggsvkpnn ikeymaqsdi dgalvggasl
241 kvedfvqlle gak
//