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UniProtKB/Swiss-Prot entry Q9PKH8

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

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Entry information
Entry name ALF1_CHLMU
Primary accession number Q9PKH8
Secondary accession numbers None
Integrated into Swiss-Prot on June 1, 2001
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 43)
Name and origin of the protein
Protein name Probable fructose-bisphosphate aldolase class 1
Synonyms EC 4.1.2.13
Probable fructose-bisphosphate aldolase class I
FBP aldolase
Gene name
Name: fbaB
OrderedLocusNames: TC_0487
From
Chlamydia muridarum [TaxID: 83560] [HAMAP proteome]
Taxonomy Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydia.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=MoPn / Nigg;
DOI=10.1093/nar/28.6.1397; PubMed=10684935 [NCBI, ExPASy, EBI, Israel, Japan]
Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M.;
"Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39.";
Nucleic Acids Res. 28:1397-1406(2000).
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
AE002160; AAF39333.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR G81697; G81697.
RefSeq NP_296864.1; -.
3D structure databases
ModBase Q9PKH8.
Enzyme and pathway databases
BioCyc CMUR243161:TC_0487-MON; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0004332; Molecular function: fructose-bisphosphate aldolase activity (inferred from electronic annotation from EC).
GO:0006096; Biological process: glycolysis (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR013785; Aldolase_TIM.
IPR002915; DeoC/AroFGH_arch.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.70; Aldolase_TIM; 1.
Pfam PF01791; DeoC; 1.
Pfam graphical view of domain structure.
ProtoNet Q9PKH8.
Genome annotation databases
GeneID 1245845; -.
GenomeReviews AE002160_GR; TC_0487.
KEGG cmu:TC0487; -.
TIGR TC_0487; -.
Phylogenomic databases
HOGENOM Q9PKH8; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; Glycolysis; Lyase; Schiff base.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   349  349     Probable fructose-bisphosphate aldolase class 1. PRO_0000138941
ACT_SITE   236   236        Schiff-base intermediate with dihydroxyacetone-P (By similarity). 
Sequence information
Length: 349 AA [This is the length of the unprocessed precursor] Molecular weight: 38226 Da [This is the MW of the unprocessed precursor] CRC64: EFFC4F47708E2686 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MTTILDLLGK DADYLLNHQC IIKKEALTLP SGDFVSRVFA ESDRNNRVLR SLQQMFDHGR 

        70         80         90        100        110        120 
LGGSGYLSIL PVDQGVEHTA GASFAKNPMY FDPENIVRLA IESGCSAVAS SYGVLSILAR 

       130        140        150        160        170        180 
RYAHKIPFLL KLNHNELLSY PTTYHQIFFS QVEDAYNMGA VAVGATVYFG SESSNEEIVS 

       190        200        210        220        230        240 
VAKAFSRARE LGLATVLWCY LRNPHFTRNG VDYHTAADLT GQADHLGATL GADIVKQKLP 

       250        260        270        280        290        300 
TLQEGFKTIN FSKTDDLVYS ELSSNHPIDL CRYQVLNSYC GKVGLINSGG PSSGQNDFTE 

       310        320        330        340 
AAKTAVINKR AGGMGLILGR KAFQRPFSEG VQLLNLIQDI YLDPTISIS
Q9PKH8 in FASTA format

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