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Q1I7D4

- FADB_PSEE4

UniProt

Q1I7D4 - FADB_PSEE4

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Protein

Fatty acid oxidation complex subunit alpha

Gene

fadB

Organism
Pseudomonas entomophila (strain L48)
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 sitei297 – 2971SubstrateUniRule annotation
Binding sitei325 – 3251NAD; via amide nitrogenUniRule annotation
Binding sitei344 – 3441NADUniRule annotation
Binding sitei408 – 4081NADUniRule annotation
Active sitei451 – 4511For 3-hydroxyacyl-CoA dehydrogenase activityUniRule annotation
Binding sitei454 – 4541NADUniRule annotation
Binding sitei501 – 5011SubstrateUniRule annotation
Binding sitei660 – 6601SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi401 – 4033NADUniRule annotation
Nucleotide bindingi428 – 4303NADUniRule 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

BioCyciPENT384676:GJB8-3529-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:PSEEN3728
OrganismiPseudomonas entomophila (strain L48)
Taxonomic identifieri384676 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000000658: 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 – 715715Fatty acid oxidation complex subunit alphaPRO_1000069567Add
BLAST

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi384676.PSEEN3728.

Structurei

3D structure databases

ProteinModelPortaliQ1I7D4.
SMRiQ1I7D4. Positions 1-714.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 190190Enoyl-CoA hydratase/isomeraseUniRule annotationAdd
BLAST
Regioni312 – 7154043-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.
OMAiNPIVVND.
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. 1 hit.
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.

Q1I7D4 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIYEGKAITV KALESGIVEL KFDLKGESVN KFNRLTLNEL RQAVDAIKAD
60 70 80 90 100
ASVKGVIVSS GKDVFIVGAD ITEFVDNFKL PEAELVAGNL EANRIFSDFE
110 120 130 140 150
DLEVPTVAAI NGIALGGGLE MCLAADYRIM SSSAKIGLPE VKLGIYPGFG
160 170 180 190 200
GTVRLPRLIG SDNAIEWIAA GKENRAEDAL KVGAVDAVVA PELLQAGALD
210 220 230 240 250
LIKRAISGEL DHKAKRQPKL EKLKLNAIEQ MMAFETAKGF VAGQAGPNYP
260 270 280 290 300
APVEAIKTIQ KAANFGRDKA LEVEAAGFAK LARTSVAESL IGLFLNDQEL
310 320 330 340 350
KRKAKAHDEI AHDVKQAAVL GAGIMGGGIA YQSAVKGTPI LMKDIREEAI
360 370 380 390 400
QLGLNEASKL LGKRVEKGRL TPAKMAEALN AIRPTLSYGD FGNVDIVVEA
410 420 430 440 450
VVENPKVKQA VLAEVEGQVK EDAILASNTS TISINLLAKA LKRPENFVGM
460 470 480 490 500
HFFNPVHMMP LVEVIRGEKS SEVAVATTVA YAKKMGKNPI VVNDCPGFLV
510 520 530 540 550
NRVLFPYFGG FAKLVSAGVD FVRIDKVMEK FGWPMGPAYL MDVVGIDTGH
560 570 580 590 600
HGRDVMAEGF PDRMKDDRRS AVDALYEANR LGQKNGKGFY AYETDKRGKP
610 620 630 640 650
KKVADASVLD VLKPVIFEQR EVSDEDIINW MMVPLCLETV RCLEDGIVET
660 670 680 690 700
AAEADMGLVY GIGFPPFRGG ALRYIDSIGV AEFVALADKY ADLGPLYHAT
710
AKLREMAKNG QRFFN
Length:715
Mass (Da):77,256
Last modified:June 13, 2006 - v1
Checksum:iF1333C67E23BDE59
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CT573326 Genomic DNA. Translation: CAK16448.1.
RefSeqiWP_011534825.1. NC_008027.1.
YP_609235.1. NC_008027.1.

Genome annotation databases

EnsemblBacteriaiCAK16448; CAK16448; PSEEN3728.
GeneIDi4090410.
KEGGipen:PSEEN3728.
PATRICi19865530. VBIPseEnt83862_3583.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CT573326 Genomic DNA. Translation: CAK16448.1 .
RefSeqi WP_011534825.1. NC_008027.1.
YP_609235.1. NC_008027.1.

3D structure databases

ProteinModelPortali Q1I7D4.
SMRi Q1I7D4. Positions 1-714.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 384676.PSEEN3728.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAK16448 ; CAK16448 ; PSEEN3728 .
GeneIDi 4090410.
KEGGi pen:PSEEN3728.
PATRICi 19865530. VBIPseEnt83862_3583.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00659 .
BioCyci PENT384676:GJB8-3529-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. 1 hit.
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. "Complete genome sequence of the entomopathogenic and metabolically versatile soil bacterium Pseudomonas entomophila."
    Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C., Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P., Weissenbach J., Lemaitre B., Medigue C., Boccard F.
    Nat. Biotechnol. 24:673-679(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: L48.

Entry informationi

Entry nameiFADB_PSEE4
AccessioniPrimary (citable) accession number: Q1I7D4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: June 13, 2006
Last modified: October 29, 2014
This is version 73 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