SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q7MQH9

- FADB_VIBVY

UniProt

Q7MQH9 - FADB_VIBVY

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Fatty acid oxidation complex subunit alpha
Gene
fadB, VV0029
Organism
Vibrio vulnificus (strain YJ016)
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

BioCyciVVUL196600:GJ9W-29-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:VV0029
OrganismiVibrio vulnificus (strain YJ016)
Taxonomic identifieri196600 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
ProteomesiUP000002675: Chromosome I

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 annotation
PRO_0000109294Add
BLAST

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi196600.VV0029.

Structurei

3D structure databases

ProteinModelPortaliQ7MQH9.
SMRiQ7MQH9. Positions 1-716.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 189189Enoyl-CoA hydratase/isomerase By similarity
Add
BLAST
Regioni311 – 7234133-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.
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.
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.

Q7MQH9-1 [UniParc]FASTAAdd to Basket

« Hide

MIYQAETLQV KEVQDGVAEI LFCAQNSVNK LDLATLASLD KALDALTAHS    50
GLKGVMLTSD KEAFIVGADI TEFLGLFAKP EEELDQWLQF ANSIFNKLED 100
LPVPTVAVVK GHTLGGGCEC VLATDLRIGD KTTSIGLPET KLGIMPGFGG 150
CVRLPRVIGA DSAMEIITQG KACRAEEALK IGLLDAVVDS DRLYASALQT 200
LTDAINEKID WKARRQQKTS ALTLSKLEAM MSFTMAKGLV AQVAGPHYPA 250
PMTAVVTIEE GARFARNQAL DIERKHFVKL AKSEEAKALV GLFLNDQYIK 300
GIAKKAAKSA NKETQRAAVL GAGIMGGGIA YQSALKGVPV IMKDIAQASL 350
DLGMTEASKL LNKQLERGKI DGFKMAGILA SITPSLHYAG IDNADIIVEA 400
VVENPKVKAA VLSEVEEQVS EETVLTSNTS TIPINLLAKS LKRPENFCGM 450
HFFNPVHRMP LVEIIRGEHT SDETINRVVA YAAKMGKSPI VVNDCPGFFV 500
NRVLFPYFGG FSMLLRDGAD FTQIDKVMER KFGWPMGPAY LLDVVGIDTA 550
HHAQAVMAQG FPERMGKQGR DAIDALFEAN KYGQKNGSGF YTYTMDKKGK 600
PKKAFSDEIV PILAPVCAAQ QAFDDQTIIQ RMMIPMINEV VLCLQEGIIA 650
SAQEADMALV YGLGFPPFRG GVFRYLDSVG IANFVAMAQQ HVELGAMYQV 700
PQMLIDMAER GQTFYGAQQQ GSI 723
Length:723
Mass (Da):78,361
Last modified:December 15, 2003 - v1
Checksum:i7760103A655D9260
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000037 Genomic DNA. Translation: BAC92793.1.
RefSeqiNP_932822.1. NC_005139.1.

Genome annotation databases

EnsemblBacteriaiBAC92793; BAC92793; BAC92793.
GeneIDi2622777.
KEGGivvy:VV0029.
PATRICi20166886. VBIVibVul40472_0082.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000037 Genomic DNA. Translation: BAC92793.1 .
RefSeqi NP_932822.1. NC_005139.1.

3D structure databases

ProteinModelPortali Q7MQH9.
SMRi Q7MQH9. Positions 1-716.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 196600.VV0029.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAC92793 ; BAC92793 ; BAC92793 .
GeneIDi 2622777.
KEGGi vvy:VV0029.
PATRICi 20166886. VBIVibVul40472_0082.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00659 .
BioCyci VVUL196600:GJ9W-29-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: YJ016.

Entry informationi

Entry nameiFADB_VIBVY
AccessioniPrimary (citable) accession number: Q7MQH9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 15, 2003
Last modified: June 11, 2014
This is version 81 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

Similar proteinsi