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UniProtKB/Swiss-Prot entry A8A6V1


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

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Entry information
Entry name FADB_ECOHS
Primary accession number A8A6V1
Secondary accession numbers None
Integrated into Swiss-Prot on February 5, 2008
Sequence was last modified on October 23, 2007 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 11)
Name and origin of the protein
Protein name Fatty acid oxidation complex subunit alpha
Synonyms None
Includes Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase
     (EC 4.2.1.17)
     (EC 5.3.3.8)
     (EC 5.1.2.3)
3-hydroxyacyl-CoA dehydrogenase
     (EC 1.1.1.35)
Gene name
Name: fadB
OrderedLocusNames: EcHS_A4069
From
Escherichia coli O9:H4 (strain HS) [TaxID: 331112] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1128/JB.00619-08; PubMed=18676672 [NCBI, ExPASy, EBI, Israel, Japan]
Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.;
"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates.";
J. Bacteriol. 190:6881-6893(2008).
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
CP000802; ABV08255.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_001460638.1; -.
3D structure databases
ModBase A8A6V1.
Ontologies
GO
GO:0016507; Cellular component: fatty acid beta-oxidation multienzyme complex (inferred from electronic annotation from InterPro).
GO:0003857; Molecular function: 3-hydroxyacyl-CoA dehydrogenase activity (inferred from electronic annotation from HAMAP).
GO:0008692; Molecular function: 3-hydroxybutyryl-CoA epimerase activity (inferred from electronic annotation from HAMAP).
GO:0050662; Molecular function: coenzyme binding (inferred from electronic annotation from InterPro).
GO:0004165; Molecular function: dodecenoyl-CoA delta-isomerase activity (inferred from electronic annotation from HAMAP).
GO:0004300; Molecular function: enoyl-CoA hydratase activity (inferred from electronic annotation from HAMAP).
GO:0009062; Biological process: fatty acid catabolic process (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
HAMAP MF_01621; -; 1.
PBIL [Tree]
InterPro IPR006180; 3-OHacyl-CoA_DHase_CS.
IPR006176; 3-OHacyl-CoA_DHase_NAD-bd.
IPR006108; 3HC_DHase_C.
IPR001753; Crotonase_core.
IPR013328; DHase_multihelical.
IPR012799; FadB.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
G3DSA:1.10.1040.10; Opine_DH; 1.
Pfam PF00725; 3HCDH; 2.
PF02737; 3HCDH_N; 1.
PF00378; ECH; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR02437; FadB; 1.
PROSITE PS00067; 3HCDH; 1.
PS00166; ENOYL_COA_HYDRATASE; 1.
Genome annotation databases
GeneID 5595361; -.
GenomeReviews CP000802_GR; EcHS_A4069.
KEGG ecx:EcHS_A4069; -.
CMR A8A6V1; EcHS_A4069.
Other
ProtoNet A8A6V1.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Fatty acid metabolism; Isomerase; Lipid degradation; Lipid metabolism; Lyase; Multifunctional enzyme; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   729  729     Fatty acid oxidation complex subunit alpha. PRO_1000069561
REGION   1   189  189     Enoyl-CoA hydratase/isomerase (By similarity). 
REGION   311   729  419     3-hydroxyacyl-CoA dehydrogenase (By similarity). 
Sequence information
Length: 729 AA [This is the length of the unprocessed precursor] Molecular weight: 79611 Da [This is the MW of the unprocessed precursor] CRC64: 49418C70238235F9 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLYKGDTLYL DWLEDGIAEL VFDAPGSVNK LDTATVASLG EAIGVLEQQS DLKGLLLRSN 

        70         80         90        100        110        120 
KAAFIVGADI TEFLSLFLVP EEQLSQWLHF ANSVFNRLED LPVPTIAAVN GYALGGGCEC 

       130        140        150        160        170        180 
VLATDYRLAT PDLRIGLPET KLGIMPGFGG SVRMPRMLGA DSALEIIAAG KDVGADQALK 

       190        200        210        220        230        240 
IGLVDGVVKA EKLIEGAMAI LRQAINGDLD WKAKRQPKLE PLKLSKIEAT MSFTIAKGMV 

       250        260        270        280        290        300 
AQTAGKHYPA PITAVKTIEA AARFGREEAL NLENKSFVPL AHTNEARALV GIFLNDQYVK 

       310        320        330        340        350        360 
GKAKKLTKDV ETPKQAAVLG AGIMGGGIAY QSAWKGVPVV MKDINDKSLT LGMTEAAKLL 

       370        380        390        400        410        420 
NKQLERGKID GLKLAGVIST IHPTLDYAGF DRVDVVVEAV VENPKVKKAV LAETEQKVRQ 

       430        440        450        460        470        480 
DTVLASNTST IPISELANAL ERPENFCGMH FFNPVHRMPL VEIIRGEKSS DETIAKVVAW 

       490        500        510        520        530        540 
ASKMGKTPIV VNDCPGFFVN RVLFPYFAGF SQLLRDGADF RKIDKVMEKQ FGWPMGPAYL 

       550        560        570        580        590        600 
LDVVGIDTAH HAQAVMAAGF PQRMQKDYRD AIDALFDANR FGQKNGLGFW RYKEDSKGKP 

       610        620        630        640        650        660 
KKEEDAAVED LLAEVSQPKR DFSEEEIIAR MMIPMVNEVV RCLEEGIIAT PAEADMALVY 

       670        680        690        700        710        720 
GLGFPPFHGG AFRWLDTLGS AKYLDMAQQY QHLGPLYEVP EGLRNKARHN EPYYPPVEPA 


RPVGDLKTA 

A8A6V1 in FASTA format

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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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