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Protein

Fatty acid oxidation complex subunit alpha

Gene

fadB

Organism
Shewanella amazonensis (strain ATCC BAA-1098 / SB2B)
Status
Reviewed-Annotation score: 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: fatty acid beta-oxidation

This protein is involved in the pathway fatty acid beta-oxidation, which is part of Lipid metabolism.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway fatty acid beta-oxidation and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei118Important for catalytic activityUniRule annotation1
Sitei138Important for catalytic activityUniRule annotation1
Binding sitei295SubstrateUniRule annotation1
Binding sitei323NAD; via amide nitrogenUniRule annotation1
Binding sitei342NADUniRule annotation1
Binding sitei406NADUniRule annotation1
Binding sitei428NADUniRule annotation1
Active sitei449For 3-hydroxyacyl-CoA dehydrogenase activityUniRule annotation1
Binding sitei452NADUniRule annotation1
Binding sitei499SubstrateUniRule annotation1
Binding sitei659SubstrateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi399 – 401NADUniRule annotation3

GO - Molecular functioni

GO - Biological processi

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:Sama_0032
OrganismiShewanella amazonensis (strain ATCC BAA-1098 / SB2B)
Taxonomic identifieri326297 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
Proteomesi
  • UP000009175 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000695721 – 716Fatty acid oxidation complex subunit alphaAdd BLAST716

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi326297.Sama_0032.

Structurei

3D structure databases

ProteinModelPortaliA1S1I8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 188Enoyl-CoA hydratase/isomeraseUniRule annotationAdd BLAST188
Regioni310 – 7163-hydroxyacyl-CoA dehydrogenaseUniRule annotationAdd BLAST407

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

eggNOGiENOG4105DYT. Bacteria.
COG1024. LUCA.
COG1250. LUCA.
HOGENOMiHOG000261344.
KOiK01825.
OMAiYKAKRQP.
OrthoDBiPOG091H00UW.

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. 1 hit.
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.
IPR012799. FadB.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00725. 3HCDH. 1 hit.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH_1. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 2 hits.
SSF51735. SSF51735. 1 hit.
SSF52096. SSF52096. 1 hit.
TIGRFAMsiTIGR02437. FadB. 1 hit.
PROSITEiPS00067. 3HCDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A1S1I8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIYQSPTIQV ELTADKIARL CFNAPGSVNK FDRETLASLN AALDVLKDSD
60 70 80 90 100
AKAAVLTSGK DTFIVGADIT EFLALFAEED AKLMEWIAQA NVVFNKLEDL
110 120 130 140 150
PFPTVSAIKG FALGGGCEAI LATDFRVADT SAKIGLPETK LGLIPGFGGT
160 170 180 190 200
VRLPRLIGAD NALEWITTGK DQRPEDALKV GAIDAVVAPE NLEAAAIQML
210 220 230 240 250
NDALAGKLDW QARRARKQAP LTLPKLEAMM SFTTAKGMVY AVAGKHYPAP
260 270 280 290 300
MAAVSVVEQA AGMSRAEALV VEHNAFIKLA KTDVATALIG IFLNDQLVKG
310 320 330 340 350
KAKKASKLAK DIKHAAVLGA GIMGGGIAYQ SASKGTPIVM KDINQAALDL
360 370 380 390 400
GVNEAAKLLS AQVARGRSTP DKMAKVLNNI TPALDYAPLK DVNVVVEAVV
410 420 430 440 450
ENPKVKAMVL ADVENVVADD AIIASNTSTI SIDLLAKSLK NPARFCGMHF
460 470 480 490 500
FNPVHKMPLV EVIRGKDTSE ETVASVVAYA SKMGKTPIVV NDCPGFFVNR
510 520 530 540 550
VLFPYFAGFN GLLADGGDFA AIDKVMEKQF GWPMGPAYLL DVVGLDTGHH
560 570 580 590 600
AQAVMADGFP DRMGKSDKDA IDVMYEAGRL GQKNGKGFYQ YSIDKRGKPK
610 620 630 640 650
KDVDPASYTM LAEAFGAQKA FEADEIIART MIPMIIETVR CLEEGIVASP
660 670 680 690 700
AEADMGLVYG LGFPPFRGGV FRYLDTMGVA NFVALADKYA HLGGLYQVTD
710
AMRELASNNG SYYPKA
Length:716
Mass (Da):76,369
Last modified:February 6, 2007 - v1
Checksum:i93251CB6B0C3D409
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000507 Genomic DNA. Translation: ABL98244.1.
RefSeqiWP_011758155.1. NC_008700.1.

Genome annotation databases

EnsemblBacteriaiABL98244; ABL98244; Sama_0032.
KEGGisaz:Sama_0032.
PATRICi23448535. VBISheAma74963_0031.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000507 Genomic DNA. Translation: ABL98244.1.
RefSeqiWP_011758155.1. NC_008700.1.

3D structure databases

ProteinModelPortaliA1S1I8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi326297.Sama_0032.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABL98244; ABL98244; Sama_0032.
KEGGisaz:Sama_0032.
PATRICi23448535. VBISheAma74963_0031.

Phylogenomic databases

eggNOGiENOG4105DYT. Bacteria.
COG1024. LUCA.
COG1250. LUCA.
HOGENOMiHOG000261344.
KOiK01825.
OMAiYKAKRQP.
OrthoDBiPOG091H00UW.

Enzyme and pathway databases

UniPathwayiUPA00659.

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. 1 hit.
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.
IPR012799. FadB.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00725. 3HCDH. 1 hit.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH_1. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 2 hits.
SSF51735. SSF51735. 1 hit.
SSF52096. SSF52096. 1 hit.
TIGRFAMsiTIGR02437. FadB. 1 hit.
PROSITEiPS00067. 3HCDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFADB_SHEAM
AccessioniPrimary (citable) accession number: A1S1I8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 6, 2007
Last modified: November 2, 2016
This is version 78 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

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 one 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.