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Q8EKR9

- FADB_SHEON

UniProt

Q8EKR9 - FADB_SHEON

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Protein

Fatty acid oxidation complex subunit alpha

Gene

fadB

Organism
Shewanella oneidensis (strain MR-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.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
Sitei119 – 1191Important for catalytic activityUniRule annotation
Sitei139 – 1391Important for catalytic activityUniRule annotation
Binding sitei296 – 2961SubstrateUniRule annotation
Binding sitei324 – 3241NAD; via amide nitrogenUniRule annotation
Binding sitei343 – 3431NADUniRule annotation
Binding sitei407 – 4071NADUniRule annotation
Active sitei450 – 4501For 3-hydroxyacyl-CoA dehydrogenase activityUniRule annotation
Binding sitei453 – 4531NADUniRule annotation
Binding sitei500 – 5001SubstrateUniRule annotation
Binding sitei660 – 6601SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi400 – 4023NADUniRule annotation
Nucleotide bindingi427 – 4293NADUniRule 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

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:SO_0021
OrganismiShewanella oneidensis (strain MR-1)
Taxonomic identifieri211586 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
ProteomesiUP000008186: 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 – 716716Fatty acid oxidation complex subunit alphaPRO_0000109288Add
BLAST

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi211586.SO_0021.

Structurei

3D structure databases

ProteinModelPortaliQ8EKR9.
SMRiQ8EKR9. Positions 1-714.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 189189Enoyl-CoA hydratase/isomeraseUniRule annotationAdd
BLAST
Regioni311 – 7164063-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.
PhylomeDBiQ8EKR9.

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.
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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8EKR9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIYQSPTIQV ELLEDNIAKL CFNAPGSVNK FDRETLASLD AALDSIKQQS
60 70 80 90 100
NIQALVLTSG KDTFIVGADI TEFLGLFAQD DAVLLSWVEQ ANAVFNKLED
110 120 130 140 150
LPFPTASAIK GFALGGGCET ILATDFRIAD TTAKIGLPET KLGIIPGFGG
160 170 180 190 200
TVRLPRVIGA DNALEWITTG NEQRAEDALK VGAVDAVVAP EALEVAAIQM
210 220 230 240 250
LKDAVAEKLD WQARRQRKLS PLTLPKLEAM MSFTTAKGMV FSVAGKHYPA
260 270 280 290 300
PMAAVNVVEQ AATKGRSDAL QIEHQAFIKL AKTDVAKALI GIFLNDQFVK
310 320 330 340 350
GKAKKAGKLA KAVNSAAVLG AGIMGGGIAY QSASKGTPIV MKDIAQPALD
360 370 380 390 400
LGLNEAAKLL SAQVARGRST PEKMAKVLNN ITPALEYAPV KHADVVVEAV
410 420 430 440 450
VEHPKVKAQV LAEVEQYVSE DAIIASNTST ISISLLAKSM KKPERFCGMH
460 470 480 490 500
FFNPVHKMPL VEVIRGEHSS EETIASVVAY ASKMGKTPIV VNDCPGFFVN
510 520 530 540 550
RVLFPYFAGF NGLLAEGGDF AAIDKVMEKQ FGWPMGPAYL LDVVGLDTGH
560 570 580 590 600
HAQAVMAEGF PDRMGKSGND AIDVMFENKR LGQKNGKGFY AYSVDSRGKP
610 620 630 640 650
KKDVDPTSYE LLKAAFGEQK AFDADEIIAR TMIPMIIETV RCLEEGIVAS
660 670 680 690 700
PAEADMGLVY GLGFPPFRGG VFRYLDTMGV ANFVALADKY AHLGGLYQVT
710
DAMRALAANN GSYYQA
Length:716
Mass (Da):76,693
Last modified:March 1, 2003 - v1
Checksum:iCD0786FD13FBFC3E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014299 Genomic DNA. Translation: AAN53108.1.
RefSeqiNP_715663.1. NC_004347.2.

Genome annotation databases

EnsemblBacteriaiAAN53108; AAN53108; SO_0021.
GeneIDi1167919.
KEGGison:SO_0021.
PATRICi23519733. VBISheOne101494_0021.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014299 Genomic DNA. Translation: AAN53108.1 .
RefSeqi NP_715663.1. NC_004347.2.

3D structure databases

ProteinModelPortali Q8EKR9.
SMRi Q8EKR9. Positions 1-714.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 211586.SO_0021.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAN53108 ; AAN53108 ; SO_0021 .
GeneIDi 1167919.
KEGGi son:SO_0021.
PATRICi 23519733. VBISheOne101494_0021.

Phylogenomic databases

eggNOGi COG1250.
HOGENOMi HOG000261344.
KOi K01825.
OMAi NPIVVND.
OrthoDBi EOG6M9F0M.
PhylomeDBi Q8EKR9.

Enzyme and pathway databases

UniPathwayi UPA00659 .

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.
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.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MR-1.

Entry informationi

Entry nameiFADB_SHEON
AccessioniPrimary (citable) accession number: Q8EKR9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: March 1, 2003
Last modified: November 26, 2014
This is version 90 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