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Protein

Fatty acid oxidation complex subunit alpha

Gene

fadB

Organism
Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)
Status
Reviewed-Annotation score: -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.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
A (3Z)-alk-3-enoyl-CoA = a (2E)-alk-2-enoyl-CoA.UniRule annotation
A (3E)-alk-3-enoyl-CoA = a (2E)-alk-2-enoyl-CoA.UniRule annotation

Pathwayi: fatty acid beta-oxidation

This protein is involved in the pathway fatty acid beta-oxidation, which is part of Lipid metabolism.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway fatty acid beta-oxidation and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei119Important for catalytic activityUniRule annotation1
Sitei139Important for catalytic activityUniRule annotation1
Binding sitei296SubstrateUniRule annotation1
Binding sitei325NAD; via amide nitrogenUniRule annotation1
Binding sitei344NADUniRule annotation1
Binding sitei408NADUniRule annotation1
Binding sitei430NADUniRule annotation1
Active sitei451For 3-hydroxyacyl-CoA dehydrogenase activityUniRule annotation1
Binding sitei454NADUniRule annotation1
Binding sitei501SubstrateUniRule annotation1
Binding sitei661SubstrateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi401 – 403NADUniRule annotation3

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionIsomerase, Lyase, Multifunctional enzyme, Oxidoreductase
Biological processFatty acid metabolism, Lipid degradation, Lipid metabolism
LigandNAD

Enzyme and pathway databases

BioCyciVCHO345073:G1GU4-201-MONOMER
UniPathwayiUPA00659

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid oxidation complex subunit alphaUniRule annotation
Including the following 2 domains:
Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimeraseUniRule annotation (EC:4.2.1.17UniRule annotation, EC:5.1.2.3UniRule annotation, EC:5.3.3.8UniRule annotation)
3-hydroxyacyl-CoA dehydrogenaseUniRule annotation (EC:1.1.1.35UniRule annotation)
Gene namesi
Name:fadBUniRule annotation
Ordered Locus Names:VC0395_A2534, VC395_0197
OrganismiVibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)
Taxonomic identifieri345073 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
Proteomesi
  • UP000000249 Componenti: Chromosome 2

Subcellular locationi

GO - Cellular componenti

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000736351 – 723Fatty acid oxidation complex subunit alphaAdd BLAST723

Proteomic databases

PRIDEiA5F465

Interactioni

Subunit structurei

Heterotetramer of two alpha chains (FadB) and two beta chains (FadA).UniRule annotation

Protein-protein interaction databases

STRINGi345073.VC0395_A2534

Structurei

3D structure databases

ProteinModelPortaliA5F465
SMRiA5F465
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 189Enoyl-CoA hydratase/isomeraseUniRule annotationAdd BLAST189
Regioni311 – 7233-hydroxyacyl-CoA dehydrogenaseUniRule annotationAdd BLAST413

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105DYT Bacteria
COG1024 LUCA
COG1250 LUCA
HOGENOMiHOG000261344
KOiK01825
OMAiIDLCMIL
OrthoDBiPOG091H00UW

Family and domain databases

HAMAPiMF_01621 FadB, 1 hit
InterProiView protein in InterPro
IPR006180 3-OHacyl-CoA_DH_CS
IPR006176 3-OHacyl-CoA_DH_NAD-bd
IPR006108 3HC_DH_C
IPR008927 6-PGluconate_DH-like_C_sf
IPR029045 ClpP/crotonase-like_dom_sf
IPR001753 Enoyl-CoA_hydra/iso
IPR012799 FadB
IPR036291 NAD(P)-bd_dom_sf
PfamiView protein in Pfam
PF00725 3HCDH, 2 hits
PF02737 3HCDH_N, 1 hit
PF00378 ECH_1, 1 hit
SUPFAMiSSF48179 SSF48179, 2 hits
SSF51735 SSF51735, 1 hit
SSF52096 SSF52096, 1 hit
TIGRFAMsiTIGR02437 FadB, 1 hit
PROSITEiView protein in PROSITE
PS00067 3HCDH, 1 hit

Sequencei

Sequence statusi: Complete.

A5F465-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIYQAKTLQV KQLANGIAEL SFCAPASVNK LDLHTLESLD KALDALAADS
60 70 80 90 100
SVKGLLLSSD KEAFIVGADI TEFLGLFAKP EAELDEWLQF ANRIFNKLED
110 120 130 140 150
LPFPTLSALK GHTLGGGCEC VLATDFRIGD ATTSIGLPET KLGIMPGFGG
160 170 180 190 200
TVRLPRLIGA DSAMEIITQG KACRAEEALK VGLLDAIVDS DKLIDSAITT
210 220 230 240 250
LTQAIEEKLD WQKRRQQKTS ALTLSKLEAM MSFTMAKGMV AQVAGKHYPA
260 270 280 290 300
PMTSVVTIEE AARLPRDAAL DIERKHFIKL AKSTEAQALV GIFLNDQYIK
310 320 330 340 350
GLAKQSAKAA SQDTQHAAVL GAGIMGGGIA YQSALKGVPV LMKDIAPHSL
360 370 380 390 400
ELGMTEAAKL LNKQLERGKI DGFKMAGILA SITPSLHYAG IDQADVIVEA
410 420 430 440 450
VVENPKVKAA VLSEVEGLVD AETILTSNTS TIPINLLAKS LKRPQNFCGM
460 470 480 490 500
HFFNPVHRMP LVEIIRGEHT SEDTINRVVA YAAKMGKSPI VVNDCPGFFV
510 520 530 540 550
NRVLFPYFAG FSLLMRDGAN FTEIDKVMER QFGWPMGPAY LLDVVGIDTA
560 570 580 590 600
HHAQAVMAEG FPTRMAKSGR EAIDALYEAK KFGQKNGSGF YQYTVDKKGK
610 620 630 640 650
PKKAFSDDVL AILAPVCGAP QNFDPQTLIE RTMIPMINEV VLCLEEGIIA
660 670 680 690 700
SAQEADMALV YGLGFPPFRG GVFRYLDTIG IANYVAMAEK YADLGALYQV
710 720
PQLLKNMAQQ GTSFYSAQQA SAL
Length:723
Mass (Da):78,076
Last modified:June 12, 2007 - v1
Checksum:i9E512BE6A218C80D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000627 Genomic DNA Translation: ABQ19542.1
CP001235 Genomic DNA Translation: ACP08224.1
RefSeqiWP_000640239.1, NC_012582.1

Genome annotation databases

EnsemblBacteriaiABQ19542; ABQ19542; VC0395_A2534
ACP08224; ACP08224; VC395_0197
KEGGivco:VC0395_A2534
vcr:VC395_0197
PATRICifig|345073.21.peg.186

Similar proteinsi

Entry informationi

Entry nameiFADB_VIBC3
AccessioniPrimary (citable) accession number: A5F465
Secondary accession number(s): C3M345
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: June 12, 2007
Last modified: May 23, 2018
This is version 79 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

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

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