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Q6DAP5

- FADB_PECAS

UniProt

Q6DAP5 - FADB_PECAS

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Protein
Fatty acid oxidation complex subunit alpha
Gene
fadB, ECA0208
Organism
Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia carotovora subsp. atroseptica)
Status
Reviewed - Annotation score: 4 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
Complete GO annotation...

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

BioCyciPATR218491:GJNB-209-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
Ordered Locus Names:ECA0208
OrganismiPectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia carotovora subsp. atroseptica)
Taxonomic identifieri218491 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePectobacterium
ProteomesiUP000007966: 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_0000109267Add
BLAST

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi218491.ECA0208.

Structurei

3D structure databases

ProteinModelPortaliQ6DAP5.
SMRiQ6DAP5. Positions 1-714.

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.
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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6DAP5-1 [UniParc]FASTAAdd to Basket

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MLYQGESLYL NWLEDGIAEL VFSAPGSVNT LDTRTVASLG KALDVLAEQP    50
NLKGLLLRSD KPAFIVGADI TEFLSLFAAP AEKLHEWLVF ANSIFNRLED 100
LPVPTLSAIN SYALGGGCEC VLATDFRLAT PDARIGLPET KLGIMPGFGG 150
TVRLPRLLGA DSALEIIAAG KDVSAADALK VGLVQAVVAN EKLIPAAIKM 200
LKQAINGELD WLGYRRPKLE ALKLNKIEAM MSFTTAKAMV LQTAGKHYPA 250
PMLAVKTIEA AATMTRDEAL QLETQHFVQL ARSNEARALV GIFLNDQYVK 300
GKAKKLVGET PVPQQAAVLG AGIMGGGIAY QSAFKGVPIR MKDINEKPLA 350
LGMNEAAKLL NKQMERGKLD GMKMATILAN IHPTLDYAGF ERTDIVVEAV 400
VENPKIKASV LAETESHISE STILASNTST IPIAVLAAAL KRPQNFCGMH 450
FFNPVHRMPL VEIIRGPKTS DSTIASVVAY ASKMGKTPIV VNDCPGFFVN 500
RVLFPYFAAF SLLLRDGADF REIDNAMEKK FGWPMGPAYL LDVVGIDTAH 550
HAQAVMAEGF PQRMAKDYRD AIDVLFEHQR FGQKNGQGFY RYQTDSKGKQ 600
RKEQDDAVDA LLKNISQPKK AFSAEEIIAR MMIPMINEVA RCLEEGIVAS 650
PAEADMALVY GLGFPPFHGG ACRYLDTLGS ERYVEMAQQL AHLGAIYQVP 700
DGLQQKARSN EGYYPSVAPH ADVSHGQPA 729
Length:729
Mass (Da):79,145
Last modified:August 16, 2004 - v1
Checksum:i997B1F78B0BD52FB
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX950851 Genomic DNA. Translation: CAG73127.1.
RefSeqiYP_048335.1. NC_004547.2.

Genome annotation databases

EnsemblBacteriaiCAG73127; CAG73127; ECA0208.
GeneIDi2883864.
KEGGieca:ECA0208.
PATRICi20475559. VBIPecAtr54885_0207.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX950851 Genomic DNA. Translation: CAG73127.1 .
RefSeqi YP_048335.1. NC_004547.2.

3D structure databases

ProteinModelPortali Q6DAP5.
SMRi Q6DAP5. Positions 1-714.
ModBasei Search...

Protein-protein interaction databases

STRINGi 218491.ECA0208.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAG73127 ; CAG73127 ; ECA0208 .
GeneIDi 2883864.
KEGGi eca:ECA0208.
PATRICi 20475559. VBIPecAtr54885_0207.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00659 .
BioCyci PATR218491:GJNB-209-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.
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.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SCRI 1043 / ATCC BAA-672.

Entry informationi

Entry nameiFADB_PECAS
AccessioniPrimary (citable) accession number: Q6DAP5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: August 16, 2004
Last modified: June 11, 2014
This is version 78 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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