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Protein

Fatty acid oxidation complex subunit alpha

Gene

fadJ

Organism
Shewanella sp. (strain W3-18-1)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the formation of a hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3-hydroxyacyl-CoA dehydrogenase activities.UniRule annotation

Catalytic activityi

(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O.UniRule annotation
(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH.UniRule annotation
(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei116 – 1161Important for catalytic activityUniRule annotation
Sitei138 – 1381Important for catalytic activityUniRule annotation

GO - Molecular functioni

  1. 3-hydroxyacyl-CoA dehydrogenase activity Source: UniProtKB-HAMAP
  2. 3-hydroxybutyryl-CoA epimerase activity Source: UniProtKB-HAMAP
  3. enoyl-CoA hydratase activity Source: UniProtKB-HAMAP
  4. NAD binding Source: InterPro

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

BioCyciSSP351745:GCOY-1606-MONOMER.
UniPathwayiUPA00659.

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid oxidation complex subunit alphaUniRule annotation
Including the following 2 domains:
Enoyl-CoA hydratase/3-hydroxybutyryl-CoA epimeraseUniRule annotation (EC:4.2.1.17UniRule annotation, EC:5.1.2.3UniRule annotation)
3-hydroxyacyl-CoA dehydrogenaseUniRule annotation (EC:1.1.1.35UniRule annotation)
Gene namesi
Name:fadJUniRule annotation
Ordered Locus Names:Sputw3181_1549
OrganismiShewanella sp. (strain W3-18-1)
Taxonomic identifieri351745 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
ProteomesiUP000002597 Componenti: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 706706Fatty acid oxidation complex subunit alphaPRO_0000323531Add
BLAST

Interactioni

Subunit structurei

Heterotetramer of two alpha chains (FadJ) and two beta chains (FadI).UniRule annotation

Protein-protein interaction databases

STRINGi351745.Sputw3181_1549.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 188188Enoyl-CoA hydrataseUniRule annotationAdd
BLAST
Regioni308 – 7063993-hydroxyacyl-CoA dehydrogenaseUniRule annotationAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.UniRule annotation
In the central section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1250.
HOGENOMiHOG000261346.
KOiK01782.
OMAiMMMLNEA.
OrthoDBiEOG6M9F0M.

Family and domain databases

Gene3Di1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 1 hit.
HAMAPiMF_01617. FadJ.
InterProiIPR006176. 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.
IPR012802. FadJ.
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.
TIGRFAMsiTIGR02440. FadJ. 1 hit.

Sequencei

Sequence statusi: Complete.

A1RI92-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKTFNLTRR DDGIAILTMD VPGETMNTLK AQFGPEISEI LAEIKSDPHI
60 70 80 90 100
RGLVLISGKK DSFVAGADIS MLDACKTAGD AKALSQQGHV VFNELEALKI
110 120 130 140 150
PVVAAIHGAC LGGGLELALA CHQRVCSDDG KTMLGVPEVQ LGLLPGGGGT
160 170 180 190 200
QRLPRLVGIT TALDMMLTGK QIRSKQALKM GLVNDVVPQT ILLQTAVEMA
210 220 230 240 250
LTGKRAPKPV KKSLVNQVLE GTSFGRNIIF DQATKQVEKK TQGNYPAPAK
260 270 280 290 300
IIDCVRQGIA KGMQKGLEVE ASHFAELVVS KESEALRSIF FATTEMKKET
310 320 330 340 350
GAEGATPRKV KKAVILGGGL MGGGIASVTT TKAKIPVRVK DISEKGLSNA
360 370 380 390 400
LAYAYKLLDK GVKRRHMTPA ARDNLMALMT TTTEYKGVKD ADIIVEAVFE
410 420 430 440 450
DLALKHQMVK DIERECGEHT IFASNTSSLP ISQIAEAATR PENVIGLHYF
460 470 480 490 500
SPVEKMPLVE VIAHAKTSPE TIATTVAFAR KQGKTPIVVQ DGAGFYVNRI
510 520 530 540 550
LALYMNEAAQ LLLEGQSVEH LDKALVKFGF PVGPITLLDE VGIDVGAKIS
560 570 580 590 600
PILEKELGER FKAPAAFDKL LGDDRKGRKN GKGFYQYGAS SKKTKAVDET
610 620 630 640 650
VYGVLGIKPG TNKDAKALAE RCVVQMLNEA VRCLDDGIIA SPRDGDIGAI
660 670 680 690 700
FGIGFPPFLG GPFHYIDTLG AANLVKILES YQSQFGNRFE PCERLKTMAR

ENVSFF
Length:706
Mass (Da):75,958
Last modified:February 6, 2007 - v1
Checksum:iC7147BBF7BCC18C4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000503 Genomic DNA. Translation: ABM24387.1.
RefSeqiWP_011788888.1. NC_008750.1.
YP_962941.1. NC_008750.1.

Genome annotation databases

EnsemblBacteriaiABM24387; ABM24387; Sputw3181_1549.
KEGGishw:Sputw3181_1549.
PATRICi23596689. VBISheSp103602_1611.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000503 Genomic DNA. Translation: ABM24387.1.
RefSeqiWP_011788888.1. NC_008750.1.
YP_962941.1. NC_008750.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi351745.Sputw3181_1549.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABM24387; ABM24387; Sputw3181_1549.
KEGGishw:Sputw3181_1549.
PATRICi23596689. VBISheSp103602_1611.

Phylogenomic databases

eggNOGiCOG1250.
HOGENOMiHOG000261346.
KOiK01782.
OMAiMMMLNEA.
OrthoDBiEOG6M9F0M.

Enzyme and pathway databases

UniPathwayiUPA00659.
BioCyciSSP351745:GCOY-1606-MONOMER.

Family and domain databases

Gene3Di1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 1 hit.
HAMAPiMF_01617. FadJ.
InterProiIPR006176. 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.
IPR012802. FadJ.
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.
TIGRFAMsiTIGR02440. FadJ. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: W3-18-1.

Entry informationi

Entry nameiFADJ_SHESW
AccessioniPrimary (citable) accession number: A1RI92
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: February 6, 2007
Last modified: April 1, 2015
This is version 64 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

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 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.