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B6EGU2

- FADB_ALISL

UniProt

B6EGU2 - FADB_ALISL

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Protein
Fatty acid oxidation complex subunit alpha
Gene
fadB, VSAL_I2974
Organism
Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain LFI1238))
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

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

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:VSAL_I2974
OrganismiAliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain LFI1238))
Taxonomic identifieri316275 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeAliivibrio
ProteomesiUP000001730: Chromosome 1

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 – 726726Fatty acid oxidation complex subunit alphaUniRule annotation
PRO_1000186031Add
BLAST

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi316275.VSAL_I2974.

Structurei

3D structure databases

ProteinModelPortaliB6EGU2.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 189189Enoyl-CoA hydratase/isomerase By similarity
Add
BLAST
Regioni311 – 7264163-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. 1 hit.
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.

B6EGU2-1 [UniParc]FASTAAdd to Basket

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MIYQGENLSV DYIENGIAHL VFNAAGSVNK LNIATLRSLG EAIDVLYKQK    50
DLQALLLSSG KSAFIVGADI TEFLGLFDTP EEELSDWLHQ ANVIFSRLED 100
LPVPTLSAIT GFALGGGCEC VLATDFRLAD DTASIGLPET QLGIMPGWGG 150
SVRLPRLIGA DPAMEVITTG KPKRAKDALK IGMVDGIVSR ETLIDASVSM 200
LKQAIDGQLN WQQRREQKKA PIQLSPLEAA MSFNVAKGMI MKMAGKHYPA 250
PLTAVKSIEQ SANMHRDDAL AIENKHFVAL TRTDVAKSLV GIFLNDQLVK 300
SKAKQAVKNS EPVKNAAVLG AGIMGGGIAY QSASKGVPVL MKDIAQASLD 350
LGMNEASKLL NKQLERGRLS GLKMAQVLSS ITPSLNYGGI ETKDVIVEAV 400
VENPTIKAAV LAEVENEVNE HAILASNTST IPISLLAKSL KRPENFCGMH 450
FFNPVHRMPL VEVIRGEKTS QQTIDRVVAY ASQMGKTPIV VNDCPGFFVN 500
RVLFPYFAGF SLLLRDGGNY QQIDKVMEKE FGWPMGPAYL LDVVGIDTAH 550
HAQAVMAQGF PERMAKNGRD VIDAMFEDDR YGQKNGIGFY AYALDKKGKP 600
KKNIDEKTNA IIATITDSTQ PYTSEQISAR MMIPMINEVI RCLDEGIIAS 650
PAEADMALVY GLGFPPFKGG VFRYLDSIGL DTYLDMAKEF EQLSPVYQVP 700
DSIKQKAAAG ECYYPAPKSS VSSPSV 726
Length:726
Mass (Da):78,731
Last modified:November 25, 2008 - v1
Checksum:iE40B3EB8D2AFE361
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
FM178379 Genomic DNA. Translation: CAQ80658.1.
RefSeqiWP_012551375.1. NC_011312.1.
YP_002264299.1. NC_011312.1.

Genome annotation databases

EnsemblBacteriaiCAQ80658; CAQ80658; VSAL_I2974.
GeneIDi6988472.
KEGGivsa:VSAL_I2974.
PATRICi20856496. VBIAliSal95923_3219.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
FM178379 Genomic DNA. Translation: CAQ80658.1 .
RefSeqi WP_012551375.1. NC_011312.1.
YP_002264299.1. NC_011312.1.

3D structure databases

ProteinModelPortali B6EGU2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 316275.VSAL_I2974.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAQ80658 ; CAQ80658 ; VSAL_I2974 .
GeneIDi 6988472.
KEGGi vsa:VSAL_I2974.
PATRICi 20856496. VBIAliSal95923_3219.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00659 .

Family and domain databases

Gene3Di 1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 1 hit.
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. "The genome sequence of the fish pathogen Aliivibrio salmonicida strain LFI1238 shows extensive evidence of gene decay."
    Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N., Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S., Thurston S., Parkhill J., Willassen N.P., Thomson N.R.
    BMC Genomics 9:616-616(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: LFI1238.

Entry informationi

Entry nameiFADB_ALISL
AccessioniPrimary (citable) accession number: B6EGU2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: November 25, 2008
Last modified: September 3, 2014
This is version 49 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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