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A9R754

- FADB_YERPG

UniProt

A9R754 - FADB_YERPG

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Protein

Fatty acid oxidation complex subunit alpha

Gene
fadB, YpAngola_A1912
Organism
Yersinia pestis bv. Antiqua (strain Angola)
Status
Reviewed - 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 By similarity.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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei119 – 1191Important for catalytic activity By similarity
Sitei139 – 1391Important for catalytic activity By similarity
Binding sitei296 – 2961Substrate By similarity
Binding sitei324 – 3241NAD; via amide nitrogen By similarity
Binding sitei343 – 3431NAD By similarity
Binding sitei407 – 4071NAD By similarity
Active sitei450 – 4501For 3-hydroxyacyl-CoA dehydrogenase activity By similarity
Binding sitei453 – 4531NAD By similarity
Binding sitei500 – 5001Substrate By similarity
Binding sitei660 – 6601Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi400 – 4023NAD By similarity
Nucleotide bindingi427 – 4293NAD By similarity

GO - Molecular functioni

  1. 3-hydroxyacyl-CoA dehydrogenase activity Source: UniProtKB-HAMAP
  2. 3-hydroxybutyryl-CoA epimerase activity Source: UniProtKB-HAMAP
  3. coenzyme binding Source: InterPro
  4. dodecenoyl-CoA delta-isomerase activity Source: UniProtKB-HAMAP
  5. enoyl-CoA hydratase activity Source: UniProtKB-HAMAP

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

BioCyciYPES349746:GHPB-1919-MONOMER.
UniPathwayiUPA00659.

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid oxidation complex subunit alpha
Including the following 2 domains:
Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC:4.2.1.17, EC:5.1.2.3, EC:5.3.3.8)
3-hydroxyacyl-CoA dehydrogenase (EC:1.1.1.35)
Gene namesi
Name:fadB
Ordered Locus Names:YpAngola_A1912
OrganismiYersinia pestis bv. Antiqua (strain Angola)
Taxonomic identifieri349746 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia
ProteomesiUP000001204: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. fatty acid beta-oxidation multienzyme complex Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 729729Fatty acid oxidation complex subunit alphaUniRule annotationPRO_1000186061Add
BLAST

Interactioni

Subunit structurei

Heterotetramer of two alpha chains (FadB) and two beta chains (FadA) By similarity.

Protein-protein interaction databases

STRINGi349746.YpAngola_A1912.

Structurei

3D structure databases

ProteinModelPortaliA9R754.
SMRiA9R754. Positions 1-714.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 189189Enoyl-CoA hydratase/isomerase By similarityAdd
BLAST
Regioni311 – 7294193-hydroxyacyl-CoA dehydrogenase By similarityAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1250.
HOGENOMiHOG000261344.
KOiK01825.
OMAiAKGMVMQ.
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.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR013328. DH_multihelical.
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.

A9R754-1 [UniParc]FASTAAdd to Basket

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MLYQSETLQL HWLENGIAEL VFDAPGSVNK LDTKTVANLG EALNVLEKQS    50
ELKGLLLRSA KTALIVGADI TEFLSLFNAP PEKLHQWLVF ANTIFNRLED 100
LPVPTISAIN GYALGGGCEC ILATDFRIAS PEARIGLPET KLGIMPGFGG 150
SVRLPRLLGA DSALEIIATG KDVTANDALK IGLVDAVVDP EKLVGSALTM 200
LKQAIDGKLD WQAARRPKLE PLKLNPTEAA MCFTIAKGRV MQVAGKHYPA 250
PLTAVKTIEA AAKFGRTEAL NLETNSFVPL AGSNEARALV GIFLNDQYVK 300
AQAKKLSKGV AAPKLAAVLG AGIMGGGIAY QSALKSVPVI MKDINENSLD 350
LGMNEAAKLL NKQLERGKVD GLKMASILAT IRPTLDYAGI ERAQVIVEAV 400
VENPKVKAAV LAEVEALIGE DTVLASNTST IPIDQLAKSL KRPENFCGMH 450
FFNPVHRMPL VEIIRGAKTS DKTLAAVVAY ATQMGKTPIV VNDCPGFFVN 500
RVLFPYLAGF GMLVRDGGDF HQIDKVMEKQ FGWPMGPAYL LDVVGIDTAH 550
HAQAVMAAGF PERMNKDYRD AVDVMFDNQR FGQKNGQGFY RYTQDAKGKP 600
RKENDEQVDK LLAEISQPLQ EFSDEDIIAR TMIPMINEVV RCLEEGIIAS 650
AAEGDMALVY GLGFPPFHGG VFRYLDTLGS ANYVEMAQRY AHLGALYHVP 700
AGLRAKAEHN ESYYPVAAAL LDVSTNQPA 729
Length:729
Mass (Da):78,826
Last modified:February 5, 2008 - v1
Checksum:i2C534B2963B09491
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000901 Genomic DNA. Translation: ABX84950.1.
RefSeqiYP_001606393.1. NC_010159.1.

Genome annotation databases

EnsemblBacteriaiABX84950; ABX84950; YpAngola_A1912.
GeneIDi5800383.
KEGGiypg:YpAngola_A1912.
PATRICi18573066. VBIYerPes97331_2317.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000901 Genomic DNA. Translation: ABX84950.1 .
RefSeqi YP_001606393.1. NC_010159.1.

3D structure databases

ProteinModelPortali A9R754.
SMRi A9R754. Positions 1-714.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 349746.YpAngola_A1912.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABX84950 ; ABX84950 ; YpAngola_A1912 .
GeneIDi 5800383.
KEGGi ypg:YpAngola_A1912.
PATRICi 18573066. VBIYerPes97331_2317.

Phylogenomic databases

eggNOGi COG1250.
HOGENOMi HOG000261344.
KOi K01825.
OMAi AKGMVMQ.
OrthoDBi EOG6M9F0M.

Enzyme and pathway databases

UniPathwayi UPA00659 .
BioCyci YPES349746:GHPB-1919-MONOMER.

Family and domain databases

Gene3Di 1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 1 hit.
HAMAPi MF_01621. FadB.
InterProi IPR006180. 3-OHacyl-CoA_DH_CS.
IPR006176. 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.
IPR018376. Enoyl-CoA_hyd/isom_CS.
IPR012799. FadB.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
Pfami PF00725. 3HCDH. 1 hit.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view ]
SUPFAMi SSF48179. SSF48179. 2 hits.
SSF52096. SSF52096. 1 hit.
TIGRFAMsi TIGR02437. FadB. 1 hit.
PROSITEi PS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals new insights into the evolution and pangenome of the plague bacterium."
    Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S., Achtman M., Lindler L.E., Ravel J.
    J. Bacteriol. 192:1685-1699(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Angola.

Entry informationi

Entry nameiFADB_YERPG
AccessioniPrimary (citable) accession number: A9R754
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 5, 2008
Last modified: June 11, 2014
This is version 58 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

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