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A4XSM8

- FADB_PSEMY

UniProt

A4XSM8 - FADB_PSEMY

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Protein

Fatty acid oxidation complex subunit alpha

Gene

fadB

Organism
Pseudomonas mendocina (strain ymp)
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.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
Sitei120 – 1201Important for catalytic activityUniRule annotation
Sitei140 – 1401Important for catalytic activityUniRule annotation
Binding sitei297 – 2971SubstrateUniRule annotation
Binding sitei325 – 3251NAD; via amide nitrogenUniRule annotation
Binding sitei344 – 3441NADUniRule annotation
Binding sitei408 – 4081NADUniRule annotation
Active sitei451 – 4511For 3-hydroxyacyl-CoA dehydrogenase activityUniRule annotation
Binding sitei454 – 4541NADUniRule annotation
Binding sitei501 – 5011SubstrateUniRule annotation
Binding sitei660 – 6601SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi401 – 4033NADUniRule annotation
Nucleotide bindingi428 – 4303NADUniRule annotation

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

BioCyciPMEN399739:GHR6-1600-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:Pmen_1580
OrganismiPseudomonas mendocina (strain ymp)
Taxonomic identifieri399739 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000000229: 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 – 715715Fatty acid oxidation complex subunit alphaPRO_1000069568Add
BLAST

Proteomic databases

PRIDEiA4XSM8.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi399739.Pmen_1580.

Structurei

3D structure databases

ProteinModelPortaliA4XSM8.
SMRiA4XSM8. Positions 1-715.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 190190Enoyl-CoA hydratase/isomeraseUniRule annotationAdd
BLAST
Regioni312 – 7154043-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.
OMAiNPIVVND.
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.
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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A4XSM8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIYEGKAITV KALESGIVEL NFDLKGESVN KFNRLTLNEL RASVDAIKAD
60 70 80 90 100
GSIKGVIVTS GKDVFIVGAD ITEFVDNFKL PDEELVAGNL EANKIFSDFE
110 120 130 140 150
DLAVPTVVAI NGIALGGGFE MCLAGDYRVM SETAKIGLPE VKLGIYPGFG
160 170 180 190 200
GTVRLPRVIG TDNAVEWIAS GKENKAADAL KVGAVDAVVA PAKLKEAALD
210 220 230 240 250
LVKRAISGEL DYKAKRQPKL EKLKLNAIEQ MMCFETAKGF VAGQAGPNYP
260 270 280 290 300
APVEAIKTIQ KAANFGRDKA LEVEAAGFVK LAKTSVAESL IGLFLNDQEL
310 320 330 340 350
KKKAKHHDEI ARDVKLAAVL GAGIMGGGIA YQSASKGTPI LMKDIREEGI
360 370 380 390 400
QMGLTEASKL LGKRVEKGRM TPAKMAEALN AIRPTMSYGD FGNVDIVVEA
410 420 430 440 450
VVENPKVKQI VLAEVEDVVR EDAILASNTS TISISLLAQA LKRPENFVGM
460 470 480 490 500
HFFNPVHMMP LVEVIRGEKS SEVAVATTVA YAKKMGKNPI VVNDCPGFLV
510 520 530 540 550
NRVLFPYFGG FSKLLGFGVD FVRIDKVMEK FGWPMGPAYL SDVVGIDTGH
560 570 580 590 600
HGRDVMAEGF PDRMAVEGKT AVDVMYEANR LGQKNGKGFY AYETDKRGKP
610 620 630 640 650
KKVSDPEAYE LLKSIVVEER EVTDEDIINF MMIPLCLETV RCLEDGIVDT
660 670 680 690 700
AAEADMGLIY GIGFPPFRGG ALRYIDSIGV AEFVALADKY ADLGALYHPT
710
AKLREMAAKG QKFFG
Length:715
Mass (Da):77,226
Last modified:May 29, 2007 - v1
Checksum:i7631223317995368
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000680 Genomic DNA. Translation: ABP84344.1.
RefSeqiYP_001187076.1. NC_009439.1.

Genome annotation databases

EnsemblBacteriaiABP84344; ABP84344; Pmen_1580.
GeneIDi5109238.
KEGGipmy:Pmen_1580.
PATRICi19909647. VBIPseMen131592_1602.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000680 Genomic DNA. Translation: ABP84344.1 .
RefSeqi YP_001187076.1. NC_009439.1.

3D structure databases

ProteinModelPortali A4XSM8.
SMRi A4XSM8. Positions 1-715.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 399739.Pmen_1580.

Proteomic databases

PRIDEi A4XSM8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABP84344 ; ABP84344 ; Pmen_1580 .
GeneIDi 5109238.
KEGGi pmy:Pmen_1580.
PATRICi 19909647. VBIPseMen131592_1602.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00659 .
BioCyci PMEN399739:GHR6-1600-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.
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.
[Graphical view ]
ProtoNeti Search...

Publicationsi

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

Entry informationi

Entry nameiFADB_PSEMY
AccessioniPrimary (citable) accession number: A4XSM8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 29, 2007
Last modified: October 29, 2014
This is version 60 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