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B7VGL4

- FADB_VIBSL

UniProt

B7VGL4 - FADB_VIBSL

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Protein

Fatty acid oxidation complex subunit alpha

Gene
fadB, VS_0041
Organism
Vibrio splendidus (strain LGP32) (Vibrio splendidus (strain Mel32))
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 sitei325 – 3251NAD; via amide nitrogen By similarity
Binding sitei344 – 3441NAD By similarity
Binding sitei408 – 4081NAD By similarity
Active sitei451 – 4511For 3-hydroxyacyl-CoA dehydrogenase activity By similarity
Binding sitei454 – 4541NAD By similarity
Binding sitei501 – 5011Substrate By similarity
Binding sitei661 – 6611Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi401 – 4033NAD By similarity
Nucleotide bindingi428 – 4303NAD 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

BioCyciVSPL575788:GH64-41-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:VS_0041
OrganismiVibrio splendidus (strain LGP32) (Vibrio splendidus (strain Mel32))
Taxonomic identifieri575788 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
ProteomesiUP000009100: 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 – 723723Fatty acid oxidation complex subunit alphaUniRule annotationPRO_1000186059Add
BLAST

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi575788.VS_0041.

Structurei

3D structure databases

ProteinModelPortaliB7VGL4.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 189189Enoyl-CoA hydratase/isomerase By similarityAdd
BLAST
Regioni311 – 7234133-hydroxyacyl-CoA dehydrogenase By similarityAdd
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.
OMAiNPIVVND.
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.

B7VGL4-1 [UniParc]FASTAAdd to Basket

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MIYQANTLQV KELQDGIAEL SFCAPASVNK LDLATLESLD KALDALNAHA    50
GLRGLILTSN KDAFIVGADI TEFLGLFAKP EAELDEWLRF ANSIFSKLED 100
LPVPTLSMMR GHALGGGCEC VLATDFRIGD KTTSIGLPET KLGIMPGFGG 150
CVRLPRVIGA DSAMEIITQG KACRADEALK VGLLDAIVET DQLLESAINT 200
VSLAANEKLD WQLRRKQKTS ALSLSKLEAM MSFTMAKGLV AQKAGPHYPA 250
PITSVIAIEE AARSDRDAAL DIERKHFVKL AKSEEAKALV GLFLNDQYIK 300
GLAKHAGKSA NKATERAAVL GAGIMGGGIA YQSALKGVPV MMKDIAQASL 350
ELGMNEASKL LNKRLSRGRL DGFKMAGILS SITPSLHYAG VEQSDVIVEA 400
VVENPKVKAA VLSEVEGLVG EDTVLTSNTS TIPINLLAKS LKRPENFCGM 450
HFFNPVHRMP LVEIIRGEHT SEETINRVVA YAAKMGKSPI VVNDCPGFFV 500
NRVLFPYFGG FSMLLRDGAD FTKIDKVMER KFGWPMGPAY LLDVVGLDTA 550
HHAQAVMAQG FPERMGKEGR DAIDALYVAE KYGQKNGSGF YTYSVDKRGR 600
PKKTFSEDIL PILADVCQQP QDFDDQTIIQ RVMIPMINEV VLCLEEGIIA 650
TPQEADMALV YGLGFPPFRG GVFRYLDSVG IGNFVEMAKS YQDLGAMYQV 700
PQLLLDMAAK GESFYDGQQA SSL 723
Length:723
Mass (Da):78,363
Last modified:February 10, 2009 - v1
Checksum:i9268B0DFE76F707D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
FM954972 Genomic DNA. Translation: CAV17097.1.
RefSeqiWP_012602959.1. NC_011753.2.
YP_002415749.1. NC_011753.2.

Genome annotation databases

EnsemblBacteriaiCAV17097; CAV17097; VS_0041.
GeneIDi7159737.
KEGGivsp:VS_0041.
PATRICi20150830. VBIVibSpl48387_1455.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
FM954972 Genomic DNA. Translation: CAV17097.1 .
RefSeqi WP_012602959.1. NC_011753.2.
YP_002415749.1. NC_011753.2.

3D structure databases

ProteinModelPortali B7VGL4.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 575788.VS_0041.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAV17097 ; CAV17097 ; VS_0041 .
GeneIDi 7159737.
KEGGi vsp:VS_0041.
PATRICi 20150830. VBIVibSpl48387_1455.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00659 .
BioCyci VSPL575788:GH64-41-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. "Vibrio splendidus str. LGP32 complete genome."
    Mazel D., Le Roux F.
    Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: LGP32.

Entry informationi

Entry nameiFADB_VIBSL
AccessioniPrimary (citable) accession number: B7VGL4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 10, 2009
Last modified: September 3, 2014
This is version 45 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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