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Q6FF68

- FADB_ACIAD

UniProt

Q6FF68 - FADB_ACIAD

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Protein

Fatty acid oxidation complex subunit alpha

Gene

fadB

Organism
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
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.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
Sitei120 – 1201Important for catalytic activityUniRule annotation
Sitei140 – 1401Important for catalytic activityUniRule annotation
Binding sitei298 – 2981SubstrateUniRule annotation
Binding sitei326 – 3261NAD; via amide nitrogenUniRule annotation
Binding sitei345 – 3451NADUniRule annotation
Binding sitei409 – 4091NADUniRule annotation
Active sitei452 – 4521For 3-hydroxyacyl-CoA dehydrogenase activityUniRule annotation
Binding sitei455 – 4551NADUniRule annotation
Binding sitei502 – 5021SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi402 – 4043NADUniRule annotation
Nucleotide bindingi429 – 4313NADUniRule annotation

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

BioCyciASP62977:GJVV-321-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:ACIAD0335
OrganismiAcinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Taxonomic identifieri62977 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter
ProteomesiUP000000430: Chromosome

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 – 717717Fatty acid oxidation complex subunit alphaPRO_0000109264Add
BLAST

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi62977.ACIAD0335.

Structurei

3D structure databases

ProteinModelPortaliQ6FF68.
SMRiQ6FF68. Positions 1-717.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 190190Enoyl-CoA hydratase/isomeraseUniRule annotationAdd
BLAST
Regioni313 – 7174053-hydroxyacyl-CoA dehydrogenaseUniRule annotationAdd
BLAST

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

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.

Q6FF68-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIHAGNAITV QMLSDGIAEF RFDLQGESVN KFNRATIEDF QAAIEAVKNH
60 70 80 90 100
PEVKGLIVTS AKSTFIVGAD ITEFGQNFAQ GEKAIVEWAL PVHDIFNSFE
110 120 130 140 150
DLDIPKVAAI NGMALGGGFE MCLVCDYRVM SDQAQVGLPE IKLGIFPGFG
160 170 180 190 200
GTVRLSRLIG IDNAVEWIAM AAPKKPAAAL KDGAVDAVVS ADKLQEAAID
210 220 230 240 250
LVKQALAGRV DWKAKRQEKL NPVKLNPLEQ MMAFNTAKGA VLAKANPAQY
260 270 280 290 300
PAPKLMLDSL QAGASLGRDE ALKVETEGFA KAAITPQAEA LIGLFLNDQI
310 320 330 340 350
IKKTSKKHEK GAHPVNQAAV LGAGIMGGGI AYQAASKGTP IIMKDIGNPQ
360 370 380 390 400
LALGMQEANG LLTKQVERKK LTPAKMGETL ARIRPTLSYD EFKEVDIVIE
410 420 430 440 450
AVTENPKIKE AVLADTEAKV RDNTIIASNT STISITRLAK ALKRPENFVG
460 470 480 490 500
MHFFNPVHMM PLVEVIRGEQ TSEEAVATTV VLAQKMGKTP IVVNDCPGFL
510 520 530 540 550
VNRVLFPYFG AFDLLLKDGA DFQQIDKVME KFGWPMGPAY LMDVVGIDTG
560 570 580 590 600
VHGAEVMAEG FPDRMKPDYK GSIQTMYEAK RLGQKNDVGF YKYELDKKGK
610 620 630 640 650
KAKTVDSTAY EVIAPVVTSE KREFDAQEII DRMMLALCNE TVRCLEDNIV
660 670 680 690 700
ATPAEADMAM IMGIGFPPFR GGPCRYIDQT GVAEYVALCN KYAHLGKAYE
710
APQLLRDMAE NNKKFYG
Length:717
Mass (Da):77,985
Last modified:July 19, 2004 - v1
Checksum:iC0981AB69CA14483
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR543861 Genomic DNA. Translation: CAG67289.1.
RefSeqiYP_045111.1. NC_005966.1.

Genome annotation databases

EnsemblBacteriaiCAG67289; CAG67289; ACIAD0335.
GeneIDi2881154.
KEGGiaci:ACIAD0335.
PATRICi20738624. VBIAciSp98416_0297.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR543861 Genomic DNA. Translation: CAG67289.1 .
RefSeqi YP_045111.1. NC_005966.1.

3D structure databases

ProteinModelPortali Q6FF68.
SMRi Q6FF68. Positions 1-717.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 62977.ACIAD0335.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAG67289 ; CAG67289 ; ACIAD0335 .
GeneIDi 2881154.
KEGGi aci:ACIAD0335.
PATRICi 20738624. VBIAciSp98416_0297.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00659 .
BioCyci ASP62977:GJVV-321-MONOMER.

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. "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium."
    Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.
    Nucleic Acids Res. 32:5766-5779(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 33305 / BD413 / ADP1.

Entry informationi

Entry nameiFADB_ACIAD
AccessioniPrimary (citable) accession number: Q6FF68
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: July 19, 2004
Last modified: October 1, 2014
This is version 80 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

External Data

Dasty 3