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Q8X8I2

- FADB_ECO57

UniProt

Q8X8I2 - FADB_ECO57

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Protein
Fatty acid oxidation complex subunit alpha
Gene
fadB, oldB, Z5367, ECs4774
Organism
Escherichia coli O157:H7
Status
Reviewed - Annotation score: 5 out of 5 - Protein inferred from homologyi

Functioni

Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate By similarity.UniRule annotation

Catalytic activityi

(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH.UniRule annotation
(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O.UniRule annotation
(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA.UniRule annotation
(3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei119 – 1191Important for catalytic activity By similarity
Sitei139 – 1391Important for catalytic activity By similarity
Binding sitei296 – 2961Substrate By similarity
Binding sitei324 – 3241NAD; via amide nitrogen By similarity
Binding sitei343 – 3431NAD By similarity
Binding sitei407 – 4071NAD By similarity
Active sitei450 – 4501For 3-hydroxyacyl-CoA dehydrogenase activity By similarity
Binding sitei453 – 4531NAD By similarity
Binding sitei500 – 5001Substrate By similarity
Binding sitei660 – 6601Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi400 – 4023NAD By similarity
Nucleotide bindingi427 – 4293NAD By similarity

GO - Molecular functioni

  1. 3-hydroxyacyl-CoA dehydrogenase activity Source: UniProtKB-HAMAP
  2. 3-hydroxybutyryl-CoA epimerase activity Source: UniProtKB-HAMAP
  3. coenzyme binding Source: InterPro
  4. dodecenoyl-CoA delta-isomerase activity Source: UniProtKB-HAMAP
  5. enoyl-CoA hydratase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. fatty acid beta-oxidation Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Lyase, Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid degradation, Lipid metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciECOL386585:GJFA-4756-MONOMER.
ECOO157:FADB-MONOMER.
UniPathwayiUPA00659.

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid oxidation complex subunit alpha
Including the following 2 domains:
Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC:4.2.1.17, EC:5.1.2.3, EC:5.3.3.8)
3-hydroxyacyl-CoA dehydrogenase (EC:1.1.1.35)
Gene namesi
Name:fadB
Synonyms:oldB
Ordered Locus Names:Z5367, ECs4774
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000558: Chromosome, UP000002519: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. fatty acid beta-oxidation multienzyme complex Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 729729Fatty acid oxidation complex subunit alphaUniRule annotation
PRO_0000109269Add
BLAST

Interactioni

Subunit structurei

Heterotetramer of two alpha chains (FadB) and two beta chains (FadA) By similarity.

Protein-protein interaction databases

STRINGi155864.Z5367.

Structurei

3D structure databases

ProteinModelPortaliQ8X8I2.
SMRiQ8X8I2. Positions 1-715.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 189189Enoyl-CoA hydratase/isomerase By similarity
Add
BLAST
Regioni311 – 7294193-hydroxyacyl-CoA dehydrogenase By similarity
Add
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.
In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.

Phylogenomic databases

eggNOGiCOG1250.
HOGENOMiHOG000261344.
KOiK01825.
OMAiAKGMVMQ.
OrthoDBiEOG6M9F0M.

Family and domain databases

Gene3Di1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 2 hits.
HAMAPiMF_01621. FadB.
InterProiIPR006180. 3-OHacyl-CoA_DH_CS.
IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR013328. DH_multihelical.
IPR018376. Enoyl-CoA_hyd/isom_CS.
IPR012799. FadB.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00725. 3HCDH. 2 hits.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 2 hits.
SSF52096. SSF52096. 1 hit.
TIGRFAMsiTIGR02437. FadB. 1 hit.
PROSITEiPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8X8I2-1 [UniParc]FASTAAdd to Basket

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MLYKGDTLYL DWLEDGIAEL VFDAPGSVNK LDTATVASLG EAIGVLEQQS    50
DLKGLLLRSN KAAFIVGADI TEFLSLFLVP EEQLSQWLHF ANSVFNRLED 100
LPVPTIAAVN GYALGGGCEC VLATDYRLAT PDLRIGLPET KLGIMPGFGG 150
SVRMPRMLGA DSALEIIAAG KDVGADQALK IGLVDGVVKA EKLIEGAMAI 200
LRQAINGDLD WKAKRQPKLE PLKLSKIEAT MSFTIAKGMV AQTAGKHYPA 250
PITAVKTIEA AARFGREEAL NLENKSFVPL AHTNEARALV GIFLNDQYVK 300
GKAKKLTKDV ETPKQAAVLG AGIMGGGIAY QSAWKGVPVI MKDINDKSLA 350
LGMTEAAKLL NKQLERGKID GLKLAGVIST IHPTLDYAGF ERVDVVVEAI 400
VENPKVKKAV LAETEQKVRP DTVLASNTST IPISELANAL ERPENFCGMH 450
FFNPVHRMPL VEIIRGEKSS DETIAKVVAW ASKMGKTPIV VNDCPGFFVN 500
RVLFPYFAGF SQLLRDGADF RKIDKVMEKQ FGWPMGPAYL LDVVGIDTAH 550
HAQAVMAAGF PQRMQKDYRD AIDALFDANR FGQKNGLGFW HYKEDSKGKP 600
KKEEDAAVDD LLAEVSQPKR DFSEEEIIAR MMIPMVNEVV RCLEEGIIAT 650
PAEADMALVY GLGFPPFHGG AFRWLDTLGS AKYLDMAQQY QHLGPLYEVP 700
EGLRNKARHN EPYYPPVEPA RPVGDLKTA 729
Length:729
Mass (Da):79,559
Last modified:March 1, 2002 - v1
Checksum:iC13EBBFFFA749183
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005174 Genomic DNA. Translation: AAG59040.1.
BA000007 Genomic DNA. Translation: BAB38197.1.
PIRiD86072.
F91225.
RefSeqiNP_290476.1. NC_002655.2.
NP_312801.1. NC_002695.1.

Genome annotation databases

EnsemblBacteriaiAAG59040; AAG59040; Z5367.
BAB38197; BAB38197; BAB38197.
GeneIDi915128.
960314.
KEGGiece:Z5367.
ecs:ECs4774.
PATRICi18359173. VBIEscCol44059_4741.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005174 Genomic DNA. Translation: AAG59040.1 .
BA000007 Genomic DNA. Translation: BAB38197.1 .
PIRi D86072.
F91225.
RefSeqi NP_290476.1. NC_002655.2.
NP_312801.1. NC_002695.1.

3D structure databases

ProteinModelPortali Q8X8I2.
SMRi Q8X8I2. Positions 1-715.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 155864.Z5367.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAG59040 ; AAG59040 ; Z5367 .
BAB38197 ; BAB38197 ; BAB38197 .
GeneIDi 915128.
960314.
KEGGi ece:Z5367.
ecs:ECs4774.
PATRICi 18359173. VBIEscCol44059_4741.

Phylogenomic databases

eggNOGi COG1250.
HOGENOMi HOG000261344.
KOi K01825.
OMAi AKGMVMQ.
OrthoDBi EOG6M9F0M.

Enzyme and pathway databases

UniPathwayi UPA00659 .
BioCyci ECOL386585:GJFA-4756-MONOMER.
ECOO157:FADB-MONOMER.

Family and domain databases

Gene3Di 1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 2 hits.
HAMAPi MF_01621. FadB.
InterProi IPR006180. 3-OHacyl-CoA_DH_CS.
IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR013328. DH_multihelical.
IPR018376. Enoyl-CoA_hyd/isom_CS.
IPR012799. FadB.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
Pfami PF00725. 3HCDH. 2 hits.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view ]
SUPFAMi SSF48179. SSF48179. 2 hits.
SSF52096. SSF52096. 1 hit.
TIGRFAMsi TIGR02437. FadB. 1 hit.
PROSITEi PS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
  2. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
    Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
    , Kuhara S., Shiba T., Hattori M., Shinagawa H.
    DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Entry informationi

Entry nameiFADB_ECO57
AccessioniPrimary (citable) accession number: Q8X8I2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: March 1, 2002
Last modified: June 11, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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