2-oxoglutarate decarboxylase, thiamin-requiring - Escherichia coli O45:K1 (strain S88 / ExPEC)

Preferred order of sections

Names and origin

Protein names

Submitted name:
2-oxoglutarate decarboxylase, thiamin-requiring EMBL CAR02090.1
EC=1.2.4.2 EMBL CAR02090.1

Gene names

Name:	sucA EMBL CAR02090.1
Ordered Locus Names:	ECS88_0751 EMBL CAR02090.1

Organism

Escherichia coli O45:K1 (strain S88 / ExPEC) [Complete proteome] [HAMAP] EMBL CAR02090.1

Taxonomic identifier

585035 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	933 AA.
Sequence status	Complete.
Protein existence	Predicted

Ontologies

Keywords
Molecular function	Oxidoreductase EMBL CAR02090.1
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	tricarboxylic acid cycle Inferred from electronic annotation. Source: InterPro
Molecular_function	oxoglutarate dehydrogenase (succinyl-transferring) activity Inferred from electronic annotation. Source: EC thiamine pyrophosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequences

Sequence

Length

Mass (Da)

Tools

B7MFY1 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: EAEF8429EC31E749
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FASTA

933

105,062

        10         20         30         40         50         60 
MQNSALKAWL DSSYLSGANQ SWIEQLYEDF LTDPDSVDAN WRSTFQQLPG TGVKPDQFHS 

        70         80         90        100        110        120 
QTREYFRRLA KDASRYSSTI SDPDTNVKQV KVLQLINAYR FRGHQHANLD PLGLWQQDKV 

       130        140        150        160        170        180 
ADLDPSFHDL TEADFQETFN VGSFASGKET MKLGELLEAL KQTYCGPIGA EYMHITSTEE 

       190        200        210        220        230        240 
KRWIQQRIES GRATFNSEEK KRFLSELTAA EGLERYLGAK FPGAKRFSLE GGDALIPMLK 

       250        260        270        280        290        300 
EMIRHAGNSG TREVVLGMAH RGRLNVLVNV LGKKPQDLFD EFAGKHKEHL GTGDVKYHMG 

       310        320        330        340        350        360 
FSSDFQTDGG LVHLALAFNP SHLEIVSPVV IGSVRARLDR LDEPSSNKVL PITIHGDAAV 

       370        380        390        400        410        420 
TGQGVVQETL NMSKARGYEV GGTVRIVINN QVGFTTSNPL DARSTPYCTD IGKMVQAPIF 

       430        440        450        460        470        480 
HVNADDPEAV AFVTRLALDF RNTFKRDVFI DLVCYRRHGH NEADEPSATQ PLMYQKIKKH 

       490        500        510        520        530        540 
PTPRKIYADK LEQEKVATLE DATEMVNLYR DALDAGDCVV AEWRPMNMHS FTWSPYLNHE 

       550        560        570        580        590        600 
WDEEYPNKVE MKRLQELAKR ISTVPEAVEM QSRVAKIYGD RQAMAAGEKL FDWGGAENLA 

       610        620        630        640        650        660 
YATLVDEGIP VRLSGEDSGR GTFFHRHAVI HNQSNGSTYT PLQHIHNGQG AFRVWDSVLS 

       670        680        690        700        710        720 
EEAVLAFEYG YATAEPRTLT IWEAQFGDFA NGAQVVIDQF ISSGEQKWGR MCGLVMLLPH 

       730        740        750        760        770        780 
GYEGQGPEHS SARLERYLQL CAEQNMQVCV PSTPAQVYHM LRRQALRGMR RPLVVMSPKS 

       790        800        810        820        830        840 
LLRHPLAVSS LEELANGTFL PAIGEIDELD PKGVKRVVMC SGKVYYDLLE QRRKNNQHDV 

       850        860        870        880        890        900 
AIVRIEQLYP FPHKAMQEVL QQFAHVKDFV WCQEEPLNQG AWYCSQHHFR EVIPFGASLR 

       910        920        930 
YAGRPASASP AVGYMSVHQK QQQDLVNDAL NVE

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References

[1]

"Organised genome dynamics in the Escherichia coli species results in highly diverse adaptive paths."
Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.

Denamur E.
PLoS Genet. 5:E1000344-E1000344(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: S88 / ExPEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU928161 Genomic DNA. Translation: CAR02090.1.
RefSeq	YP_002390554.1. NC_011742.1.
3D structure databases
ProteinModelPortal	B7MFY1.
SMR	B7MFY1. Positions 85-933.
ModBase	Search...
Protein-protein interaction databases
STRING	585035.ECS88_0751. B7MFY1.
Proteomic databases
PRIDE	B7MFY1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAR02090; CAR02090; ECS88_0751.
GeneID	7131374.
KEGG	ecz:ECS88_0751.
PATRIC	18409196. VBIEscCol91599_0748.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0567.
HOGENOM	HOG000259587.
KO	K00164.
OMA	IIKRGGA.
ProtClustDB	PRK09404.
Enzyme and pathway databases
BioCyc	ECOL585035:GJWP-748-MONOMER.
Family and domain databases
InterPro	IPR011603. 2oxoglutarate_DH_E1. IPR001017. DH_E1. IPR005475. Transketolase-like_Pyr-bd. [Graphical view]
PANTHER	PTHR23152. PTHR23152. 1 hit.
Pfam	PF00676. E1_dh. 1 hit. PF02779. Transket_pyr. 1 hit. [Graphical view]
PIRSF	PIRSF000157. Oxoglu_dh_E1. 1 hit.
SMART	SM00861. Transket_pyr. 1 hit. [Graphical view]
TIGRFAMs	TIGR00239. 2oxo_dh_E1. 1 hit.
ProtoNet	Search...

Entry information

Entry name

B7MFY1_ECO45

Accession

Primary (citable) accession number: B7MFY1

Entry history

Integrated into UniProtKB/TrEMBL:	March 24, 2009
Last sequence update:	March 24, 2009
Last modified:	May 1, 2013
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

Preferred order of sections

Names and origin

Protein attributes

Ontologies

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information