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UniProtKB/Swiss-Prot entry Q8CMY5

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ALF1_STAES
Primary accession number Q8CMY5
Secondary accession numbers None
Integrated into Swiss-Prot on November 21, 2003
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 40)
Name and origin of the protein
Protein name Fructose-bisphosphate aldolase class 1
Synonyms EC 4.1.2.13
Fructose-biphosphate aldolase class I
FBP aldolase
Gene name
Name: fda
OrderedLocusNames: SE_2156
From
Staphylococcus epidermidis (strain ATCC 12228) [TaxID: 176280] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Staphylococcus.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1046/j.1365-2958.2003.03671.x; PubMed=12950922 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q., Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H., Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
"Genome-based analysis of virulence genes in a non-biofilm-forming Staphylococcus epidermidis strain (ATCC 12228).";
Mol. Microbiol. 49:1577-1593(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AE015929; AAO05798.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_765711.1; -.
3D structure databases
ModBase Q8CMY5.
Enzyme and pathway databases
BioCyc SEPI176280:SE_2156-MON; -.
Ontologies
GO
GO:0004332; Molecular function: fructose-bisphosphate aldolase activity (inferred from electronic annotation from HAMAP).
GO:0006096; Biological process: glycolysis (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00729; -; 1.
PBIL [Tree]
InterPro IPR000741; Aldolase_I.
IPR013785; Aldolase_TIM.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.70; Aldolase_TIM; 1.
PANTHER PTHR11627; Aldolase_I; 1.
Pfam PF00274; Glycolytic; 1.
Pfam graphical view of domain structure.
ProDom PD001128; Aldolase_I; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00158; ALDOLASE_CLASS_I; FALSE_NEG.
Genome annotation databases
GeneID 1056263; -.
GenomeReviews AE015929_GR; SE_2156.
KEGG sep:SE2156; -.
Phylogenomic databases
HOGENOM Q8CMY5; -.
Genome annotation databases
CMR Q8CMY5; SE_2156.
Other
ProtoNet Q8CMY5.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Glycolysis; Lyase; Schiff base.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   296  295     Fructose-bisphosphate aldolase class 1. PRO_0000216910
ACT_SITE   175   175        Proton acceptor (By similarity). 
ACT_SITE   212   212        Schiff-base intermediate with dihydroxyacetone-P (By similarity). 
Sequence information
Length: 296 AA [This is the length of the unprocessed precursor] Molecular weight: 33052 Da [This is the MW of the unprocessed precursor] CRC64: 13258473A6438CE9 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MNKEQLEKMT HGKGFIAALD QSGGSTPKAL KEYGVNEDQY SNEDEMFQLV HDMRTRVVTS 

        70         80         90        100        110        120 
PSFSPDKILG AILFEQTMDR EVEGKYTGDY LADKGVVPFL KVDKGLAEEK NGVQLMKPID 

       130        140        150        160        170        180 
DLDETLDRAN ERHIFGTKMR SNILELNEQG IKDVVEQQFE FAKKIIAKGL VPIIEPEVNI 

       190        200        210        220        230        240 
NAKDKSEIEK VLKAEIKKGL DSLNDDQLVM LKLTIPTEAN LYKDLADHPN VVRVVVLSGG 

       250        260        270        280        290 
YSRDEANKLL KDNDELIASF SRALASDLRA SQSQEEFDKA LGDAVDSIYD ASVNKN
Q8CMY5 in FASTA format

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