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Protein

Fatty acid oxidation complex subunit alpha

Gene

fadJ

Organism
Serratia proteamaculans (strain 568)
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
Sitei122 – 1221Important for catalytic activityUniRule annotation
Sitei144 – 1441Important 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

BioCyciSPRO399741:GI55-3446-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:Spro_3378
OrganismiSerratia proteamaculans (strain 568)
Taxonomic identifieri399741 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSerratia
ProteomesiUP000007074 Componenti: Chromosome

Subcellular locationi

  1. 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 – 715715Fatty acid oxidation complex subunit alphaPRO_0000335591Add
BLAST

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi399741.Spro_3378.

Structurei

3D structure databases

ProteinModelPortaliA8GH86.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 194194Enoyl-CoA hydrataseUniRule annotationAdd
BLAST
Regioni310 – 7154063-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.
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.
InterProiIPR006180. 3-OHacyl-CoA_DH_CS.
IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
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.
PROSITEiPS00067. 3HCDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A8GH86-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHEQRAKPSA FQLTIRPDNI GVITIDVPGE KVNTLKAEFV EQVNDVLIRA
60 70 80 90 100
QQHPALEGLV IVSGKPDSFI AGADITMIAA CTTAKEAETL AKKGQSTLAQ
110 120 130 140 150
IAAFQVPVVA AIHGACLGGG LELALACHGR VCSLDDKTAL GLPEVQLGLL
160 170 180 190 200
PGSGGTQRLP RLIGASKALD MILTGKHIRA RQALRLGLVD DAVPQSILLQ
210 220 230 240 250
TAIERVKQGW QSRRELPWQE RLLNGPLGKS LLFSIVRKKT LAKTHGNYPA
260 270 280 290 300
AERIIQVVRT GLDSGIASGY EAEARAFGEL AMTPQSAALR SLFFASTALK
310 320 330 340 350
KERGGNAQPH ALHRIGILGG GLMGGGIACV TATRGGLPVR IKDVNETGIN
360 370 380 390 400
HALKYSWDVL SKRVRSKRMR PAERQKQMML ISGSTDYSGF DQVDVVIEAV
410 420 430 440 450
FEDLSLKQQM VAEIEQHAAP HTIFASNTSS LPIGQIAAKA QRPEQVIGLH
460 470 480 490 500
YFSPVDKMPL VEVIPHATTS EETIATTVAL AHKQGKTAIV VADRAGFYVN
510 520 530 540 550
RILAPYINEA ARCLLEGEPI ESLDKALVDF GFPVGPITLL DEVGIDVGTK
560 570 580 590 600
ISPVLVEQLG PRFAAPAAFD AVLKDGRKGR KNGRGFYLYP SEGQQRQRHK
610 620 630 640 650
RADTSVYILL GITPKSHLQQ AVIAQRCVMM MLNEAARCLD EGVIRSARDG
660 670 680 690 700
DIGAVFGIGF PPFLGGPFRY MDQLGVEKVV KTLEYLQRQH GEYFAPCERL
710
QRMAQQGERF YPQGS
Length:715
Mass (Da):77,439
Last modified:May 20, 2008 - v2
Checksum:iA39FA88CFF8406A5
GO

Sequence cautioni

The sequence ABV42476.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000826 Genomic DNA. Translation: ABV42476.1. Different initiation.
RefSeqiYP_001479604.1. NC_009832.1.

Genome annotation databases

EnsemblBacteriaiABV42476; ABV42476; Spro_3378.
KEGGispe:Spro_3378.
PATRICi32419542. VBISerPro44537_3435.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000826 Genomic DNA. Translation: ABV42476.1. Different initiation.
RefSeqiYP_001479604.1. NC_009832.1.

3D structure databases

ProteinModelPortaliA8GH86.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi399741.Spro_3378.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABV42476; ABV42476; Spro_3378.
KEGGispe:Spro_3378.
PATRICi32419542. VBISerPro44537_3435.

Phylogenomic databases

eggNOGiCOG1250.
HOGENOMiHOG000261346.
KOiK01782.
OrthoDBiEOG6M9F0M.

Enzyme and pathway databases

UniPathwayiUPA00659.
BioCyciSPRO399741:GI55-3446-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.
InterProiIPR006180. 3-OHacyl-CoA_DH_CS.
IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
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.
PROSITEiPS00067. 3HCDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 568.

Entry informationi

Entry nameiFADJ_SERP5
AccessioniPrimary (citable) accession number: A8GH86
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: April 29, 2015
This is version 56 of the entry and version 2 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

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.