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.

B0KH74

- FADB_PSEPG

UniProt

B0KH74 - FADB_PSEPG

(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, PputGB1_1676
Organism
Pseudomonas putida (strain GB-1)
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
Sitei120 – 1201Important for catalytic activity By similarity
Sitei140 – 1401Important for catalytic activity By similarity
Binding sitei297 – 2971Substrate 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 sitei660 – 6601Substrate 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

BioCyciPPUT76869:GIXB-1727-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:PputGB1_1676
OrganismiPseudomonas putida (strain GB-1)
Taxonomic identifieri76869 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000002157: 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 alphaUniRule annotationPRO_1000088080Add
BLAST

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi76869.PputGB1_1676.

Structurei

3D structure databases

ProteinModelPortaliB0KH74.
SMRiB0KH74. Positions 1-714.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 190190Enoyl-CoA hydratase/isomerase By similarityAdd
BLAST
Regioni312 – 7154043-hydroxyacyl-CoA dehydrogenase By similarityAdd
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. 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.

B0KH74-1 [UniParc]FASTAAdd to Basket

« Hide

MIYEGKAITV KALESGIVEL KFDLKGESVN KFNRLTLNEL RQAVEAIQAD    50
ASVKGVIVSS GKDVFIVGAD ITEFVDNFKL PEAELVAGNL EANRIFNAFE 100
DLEVPTVAAI NGIALGGGLE MCLAADYRVM SNSAKIGLPE VKLGIYPGFG 150
GTVRLPRLIG SDNAIEWIAA GKENRAEDAL KVGAVDAVVA PELLLAGALD 200
LIKRAISGEL DYKAKRQPKL EKLKLNAIEQ MMAFETAKGF VAGQAGPNYP 250
APVEAIKSIQ KAANFGRDKA LEVEAAGFAK LAKTSVAESL IGLFLNDQEL 300
KRKAKAHDEI AHDVKQAAVL GAGIMGGGIA YQSAVKGTPI LMKDIREEAI 350
QLGLNEASKL LGNRVEKGRL TPAKMAEALN AIRPTLSYGD FANVDIVVEA 400
VVENPKVKQA VLAEVEGQVK DDAILASNTS TISINLLAKA LKRPENFVGM 450
HFFNPVHMMP LVEVIRGEKS SEVAVATTVA YAKKMGKNPI VVNDCPGFLV 500
NRVLFPYFGG FAKLVSAGVD FVRIDKVMEK FGWPMGPAYL MDVVGIDTGH 550
HGRDVMAEGF PDRMKDERRS AVDALYEANR LGQKNGKGFY AYETDKRGKP 600
KKVFDATVLD VLKPIVFEQR EVTDEDIINW MMVPLCLETV RCLEDGIVET 650
AAEADMGLVY GIGFPPFRGG ALRYIDSIGV AEFVALADQY ADLGPLYHPT 700
AKLREMAKNG QRFFN 715
Length:715
Mass (Da):77,366
Last modified:March 18, 2008 - v1
Checksum:iDE811EBF9BF0B890
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000926 Genomic DNA. Translation: ABY97579.1.
RefSeqiWP_012271342.1. NC_010322.1.
YP_001667915.1. NC_010322.1.

Genome annotation databases

EnsemblBacteriaiABY97579; ABY97579; PputGB1_1676.
GeneIDi5869456.
KEGGippg:PputGB1_1676.
PATRICi19930365. VBIPsePut76638_1680.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000926 Genomic DNA. Translation: ABY97579.1 .
RefSeqi WP_012271342.1. NC_010322.1.
YP_001667915.1. NC_010322.1.

3D structure databases

ProteinModelPortali B0KH74.
SMRi B0KH74. Positions 1-714.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 76869.PputGB1_1676.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABY97579 ; ABY97579 ; PputGB1_1676 .
GeneIDi 5869456.
KEGGi ppg:PputGB1_1676.
PATRICi 19930365. VBIPsePut76638_1680.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00659 .
BioCyci PPUT76869:GIXB-1727-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: GB-1.

Entry informationi

Entry nameiFADB_PSEPG
AccessioniPrimary (citable) accession number: B0KH74
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: March 18, 2008
Last modified: September 3, 2014
This is version 52 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