Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Fatty acid oxidation complex subunit alpha

Gene

fadB

Organism
Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR)
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

Pathway:ifatty 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)LengthDescriptionGraphical viewFeature identifierActions
Sitei118 – 1181Important for catalytic activityUniRule annotation
Sitei138 – 1381Important for catalytic activityUniRule annotation
Binding sitei295 – 2951SubstrateUniRule 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 sitei658 – 6581SubstrateUniRule annotation

Regions

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

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

BioCyciILOI283942:GI0U-11-MONOMER.
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:IL0011
OrganismiIdiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR)
Taxonomic identifieri283942 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesIdiomarinaceaeIdiomarina
ProteomesiUP000001171 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 718718Fatty acid oxidation complex subunit alphaPRO_0000109271Add
BLAST

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi283942.IL0011.

Structurei

3D structure databases

ProteinModelPortaliQ5QXH7.
SMRiQ5QXH7. Positions 1-712.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 188188Enoyl-CoA hydratase/isomeraseUniRule annotationAdd
BLAST
Regioni310 – 7184093-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.
OMAiRSDKPAF.
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.
IPR013328. 6PGD_dom_2.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
IPR012799. FadB.
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.
TIGRFAMsiTIGR02437. FadB. 1 hit.
PROSITEiPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5QXH7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIYQGESIRV DFIEPGFAEL QFDAKGSVNK FDQATLEEFS EALTKLQNTD
60 70 80 90 100
DLRGVIVTSS KSTFIVGADI TEFLTLFSDQ EKTRSWVAKA SRVFDQLEDL
110 120 130 140 150
PVPTVGAVTG FALGGGCEAL LACDYRVADT TATIGLPEVK LGLIPGFGGT
160 170 180 190 200
MRLPRVIGPD NALEWITTGK NNKALDALKV GAVDAVVEPE NLTKAALNLA
210 220 230 240 250
KAAAAGQQDW KAKRQPKLEP LKANDTELMM TLVTAKGMIA AKAGKHYPAP
260 270 280 290 300
HKALEAIENG AREHREGALT AENNAFFDLT QTEACQAQVG IFLADQAVKG
310 320 330 340 350
KSKKYAKAAT KEIKTAGVLG AGIMGGGIAY QSALKGVPAV MKDIKQDALD
360 370 380 390 400
LGMKEAGKIL KKGVERGKVN NEKMIKILSS ITPTLLNDAV KDVDIVVEAV
410 420 430 440 450
VENPKVKGSV LAEIEGVIGD DAILTSNTST ISITELAKNL KRPEKFCGMH
460 470 480 490 500
FFNPVHKMPL VEIIRGEKTS DDTVNAVVAY ALKLGKTPIV VNDCPGFLVN
510 520 530 540 550
RVLFPYLAGF AGMVDEGVDF VGIDKVMEKQ FGWPMGPAYL SDVVGIDTAD
560 570 580 590 600
HCTVVMEAGF PTRMKRDESS AIAKLAAAER YGQKNGKGFY VYGTDKKGKP
610 620 630 640 650
TKEADPATYE LLGCEQGKKL DADEVIARCM IPMVNEVVRC LEEDIVGSAA
660 670 680 690 700
EADMALLYGL GFPPFRGGPF RYLETLGMDN FIQLADKYAH LGEIYQVTDG
710
MREMAKAGKS YFDTTSAK
Length:718
Mass (Da):77,268
Last modified:January 4, 2005 - v1
Checksum:iA870D2CA91816281
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017340 Genomic DNA. Translation: AAV80855.1.
RefSeqiWP_011233275.1. NC_006512.1.

Genome annotation databases

EnsemblBacteriaiAAV80855; AAV80855; IL0011.
KEGGiilo:IL0011.
PATRICi22138027. VBIIdiLoi21852_0011.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017340 Genomic DNA. Translation: AAV80855.1.
RefSeqiWP_011233275.1. NC_006512.1.

3D structure databases

ProteinModelPortaliQ5QXH7.
SMRiQ5QXH7. Positions 1-712.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi283942.IL0011.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAV80855; AAV80855; IL0011.
KEGGiilo:IL0011.
PATRICi22138027. VBIIdiLoi21852_0011.

Phylogenomic databases

eggNOGiCOG1250.
HOGENOMiHOG000261344.
KOiK01825.
OMAiRSDKPAF.
OrthoDBiEOG6M9F0M.

Enzyme and pathway databases

UniPathwayiUPA00659.
BioCyciILOI283942:GI0U-11-MONOMER.

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.
IPR013328. 6PGD_dom_2.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
IPR012799. FadB.
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.
TIGRFAMsiTIGR02437. FadB. 1 hit.
PROSITEiPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-735 / DSM 15497 / L2-TR.

Entry informationi

Entry nameiFADB_IDILO
AccessioniPrimary (citable) accession number: Q5QXH7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: January 4, 2005
Last modified: July 22, 2015
This is version 84 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

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.