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Protein

Fatty acid oxidation complex subunit alpha

Gene

fadB

Organism
Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240)
Status
Reviewed-Annotation score: 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.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: 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

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 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:AHA_0139
OrganismiAeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240)
Taxonomic identifieri380703 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAeromonadalesAeromonadaceaeAeromonas
Proteomesi
  • UP000000756 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000695571 – 715Fatty acid oxidation complex subunit alphaAdd BLAST715

Proteomic databases

PRIDEiA0KEL1.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi380703.AHA_0139.

Structurei

3D structure databases

ProteinModelPortaliA0KEL1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 189Enoyl-CoA hydratase/isomeraseUniRule annotationAdd BLAST189
Regioni311 – 7153-hydroxyacyl-CoA dehydrogenaseUniRule annotationAdd BLAST405

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.
OMAiRSDKPAF.

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. 1 hit.
InterProiIPR006180. 3-OHacyl-CoA_DH_CS.
IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR012799. FadB.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00725. 3HCDH. 2 hits.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH_1. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 2 hits.
SSF51735. SSF51735. 1 hit.
SSF52096. SSF52096. 1 hit.
TIGRFAMsiTIGR02437. FadB. 1 hit.
PROSITEiPS00067. 3HCDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A0KEL1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIYQGETLTV SYLEDGIAEL RFDAPGSVNK LDRATLLSLS EAIAALQQER
60 70 80 90 100
ELKGLILTSG KDAFIVGADI TEFLELFDLP QADLLGWLKK ANDIFSAIED
110 120 130 140 150
LPVPTLSAIK GHALGGGCET ILSTDFRLAD TSAKIGLPET KLGIMPGFGG
160 170 180 190 200
TVRLPRVIGA DNALEWITTG KDYRADDALK VGAIDAVVAP DALQSAAVQM
210 220 230 240 250
IKDAVKGKLD WQGRRAAKKA PLRLSKLEAM MSFTTAAGMV AAVAGKHYPA
260 270 280 290 300
PMTAVKTVEA AAGMSRDEAL AVEAQGFIKL AKTDVAKALV GIFLNDQHIK
310 320 330 340 350
ALAKKAAKQA AKATSHAAVL GAGIMGGGIA YQSASKGIPA VMKDINEKAL
360 370 380 390 400
ALGMGEATKL LNGQLEKGRI DGIKMGQVLS AITPTLSYDN VKHVDVVVEA
410 420 430 440 450
VVENPKVKAA VLGEVEGIIG EDAVLASNTS TIPISLLAKE LKRPQNFCGM
460 470 480 490 500
HFFNPVHRMP LVEIIRGEQT SDETINRVVA YAAAMGKSPV VVNDCPGFFV
510 520 530 540 550
NRVLFPYFFG FNKLVADGAD FAAVDKVMEK EFGWPMGPAY LLDVVGIDTG
560 570 580 590 600
HHAGDVMAQG FPARMSKEGR TAIDVMYEVN RFGQKNGKGF YAYEQDKKGK
610 620 630 640 650
PKKVADAASY ELLAPIAKPK QDFDKDAIIA RMMIPMINEV VLCLEEGIVA
660 670 680 690 700
TPAEADIALV YGLGFPPFRG GVFRYLDTIG LDRYVAMADQ YADLGPLYRV
710
SDKLREMAAQ GKTFY
Length:715
Mass (Da):76,523
Last modified:December 12, 2006 - v1
Checksum:i41DF8B6A84E7751A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000462 Genomic DNA. Translation: ABK38031.1.
RefSeqiWP_011704165.1. NC_008570.1.
YP_854676.1. NC_008570.1.

Genome annotation databases

EnsemblBacteriaiABK38031; ABK38031; AHA_0139.
GeneIDi4490320.
KEGGiaha:AHA_0139.
PATRICi20777742. VBIAerHyd135212_0132.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000462 Genomic DNA. Translation: ABK38031.1.
RefSeqiWP_011704165.1. NC_008570.1.
YP_854676.1. NC_008570.1.

3D structure databases

ProteinModelPortaliA0KEL1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi380703.AHA_0139.

Proteomic databases

PRIDEiA0KEL1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABK38031; ABK38031; AHA_0139.
GeneIDi4490320.
KEGGiaha:AHA_0139.
PATRICi20777742. VBIAerHyd135212_0132.

Phylogenomic databases

eggNOGiENOG4105DYT. Bacteria.
COG1024. LUCA.
COG1250. LUCA.
HOGENOMiHOG000261344.
KOiK01825.
OMAiRSDKPAF.

Enzyme and pathway databases

UniPathwayiUPA00659.

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. 1 hit.
InterProiIPR006180. 3-OHacyl-CoA_DH_CS.
IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR012799. FadB.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00725. 3HCDH. 2 hits.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH_1. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 2 hits.
SSF51735. SSF51735. 1 hit.
SSF52096. SSF52096. 1 hit.
TIGRFAMsiTIGR02437. FadB. 1 hit.
PROSITEiPS00067. 3HCDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFADB_AERHH
AccessioniPrimary (citable) accession number: A0KEL1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: December 12, 2006
Last modified: November 2, 2016
This is version 79 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, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.