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Protein

Fatty acid oxidation complex subunit alpha

Gene

fadB

Organism
Yersinia pseudotuberculosis serotype I (strain IP32953)
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
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

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

BioCyciYPSE273123:GI1M-284-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:YPTB0267
OrganismiYersinia pseudotuberculosis serotype I (strain IP32953)
Taxonomic identifieri273123 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia
ProteomesiUP000001011 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 729729Fatty acid oxidation complex subunit alphaPRO_0000109296Add
BLAST

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliQ66FR8.
SMRiQ66FR8. Positions 1-714.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 189189Enoyl-CoA hydratase/isomeraseUniRule annotationAdd
BLAST
Regioni311 – 7294193-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. 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.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q66FR8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLYQSETLQL HWLENGIAEL VFDAPGSVNK LDTKTVANLG EALNVLEKQS
60 70 80 90 100
ELKGLLLRSA KTALIVGADI TEFLSLFNAP PEKLHQWLVF ANTIFNRLED
110 120 130 140 150
LPVPTISAIN GYALGGGCEC ILATDFRIAS PEARIGLPET KLGIMPGFGG
160 170 180 190 200
SVRLPRLLGA DSALEIIATG KDVTANDALK IGLVDAVVDP EKLVGSALTM
210 220 230 240 250
LKQAIDGKLD WQAARRPKLE PLKLNPTEAA MCFTIAKGRV MQVAGKHYPA
260 270 280 290 300
PLTAVKTIEA AAKFGRTEAL NLETNSFVPL AGSNEARALV GIFLNDQYVK
310 320 330 340 350
AQAKKLSKGV AAPKLAAVLG AGIMGGGIAY QSALKSVPVI MKDINENSLD
360 370 380 390 400
LGMNEAAKLL NKQLERGKVD GLKMASILAT IRPTLDYAGI ERAQVIVEAV
410 420 430 440 450
VENPKVKAAV LAEVEALIGE DTVLASNTST IPIDQLAKSL KRPENFCGMH
460 470 480 490 500
FFNPVHQMPL VEIIRGAKTS DKTLAAVVAY ATQMGKTPIV VNDCPGFFVN
510 520 530 540 550
RVLFPYLAGF GMLVRDGGDF HQIDKVMEKQ FGWPMGPAYL LDVVGIDTAH
560 570 580 590 600
HAQAVMAAGF PERMNKDYRD AVDVMFDNQR FGQKNGQGFY RYTQDAKGKP
610 620 630 640 650
RKENDEQVDK LLAEISQPLQ EFSDEDIIAR TMIPMINEVV RCLEEGIIAS
660 670 680 690 700
AAEGDMALVY GLGFPPFHGG VFRYLDTLGS ANYVEMAQRY AHLGALYHVP
710 720
AGLRAKAEHN ESYYPVAAAL LDVSTNQPA
Length:729
Mass (Da):78,798
Last modified:October 11, 2004 - v1
Checksum:i2CC3F4F962ED3791
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX936398 Genomic DNA. Translation: CAH19507.1.
RefSeqiWP_011191547.1. NZ_CP009712.1.

Genome annotation databases

EnsemblBacteriaiCAH19507; CAH19507; YPTB0267.
KEGGiyps:YPTB0267.
PATRICi18638639. VBIYerPse22266_0432.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX936398 Genomic DNA. Translation: CAH19507.1.
RefSeqiWP_011191547.1. NZ_CP009712.1.

3D structure databases

ProteinModelPortaliQ66FR8.
SMRiQ66FR8. Positions 1-714.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAH19507; CAH19507; YPTB0267.
KEGGiyps:YPTB0267.
PATRICi18638639. VBIYerPse22266_0432.

Phylogenomic databases

eggNOGiCOG1250.
HOGENOMiHOG000261344.
KOiK01825.
OMAiRSDKPAF.
OrthoDBiEOG6M9F0M.

Enzyme and pathway databases

UniPathwayiUPA00659.
BioCyciYPSE273123:GI1M-284-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. 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.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: IP32953.

Entry informationi

Entry nameiFADB_YERPS
AccessioniPrimary (citable) accession number: Q66FR8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: October 11, 2004
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

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.