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Protein

Carnitine monooxygenase reductase subunit

Gene

yeaX

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Converts carnitine to trimethylamine and malic semialdehyde. Can also use gamma-butyrobetaine, choline and betaine as substrates.1 Publication

Catalytic activityi

L-carnitine + NAD(P)H + H+ + O2 = (3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NAD(P)+ + H2O.UniRule annotation1 Publication

Cofactori

Protein has several cofactor binding sites:
  • FMNUniRule annotation
  • [2Fe-2S] clusterUniRule annotationNote: Binds 1 2Fe-2S cluster.UniRule annotation

Pathwayi: carnitine metabolism

This protein is involved in the pathway carnitine metabolism, which is part of Amine and polyamine metabolism.UniRule annotation1 Publication
View all proteins of this organism that are known to be involved in the pathway carnitine metabolism and in Amine and polyamine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi270Iron-sulfur (2Fe-2S)UniRule annotation1
Metal bindingi275Iron-sulfur (2Fe-2S)UniRule annotation1
Metal bindingi278Iron-sulfur (2Fe-2S)UniRule annotation1
Metal bindingi308Iron-sulfur (2Fe-2S)UniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Ligand2Fe-2S, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, NAD, NADP

Enzyme and pathway databases

BioCyciEcoCyc:G6989-MONOMER.
MetaCyc:G6989-MONOMER.
UniPathwayiUPA00117.

Names & Taxonomyi

Protein namesi
Recommended name:
Carnitine monooxygenase reductase subunitUniRule annotationCurated (EC:1.14.13.-UniRule annotation1 Publication)
Alternative name(s):
Carnitine monooxygenase beta subunitUniRule annotationCurated
Gene namesi
Name:yeaX
Ordered Locus Names:b1803, JW1792
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13510. yeaX.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001894051 – 321Carnitine monooxygenase reductase subunitAdd BLAST321

Proteomic databases

PaxDbiP76254.
PRIDEiP76254.

Interactioni

Subunit structurei

Composed of an oxygenase subunit (yeaW) and a reductase subunit (yeaX).By similarity

Protein-protein interaction databases

BioGridi4260337. 16 interactors.
STRINGi316385.ECDH10B_1941.

Structurei

3D structure databases

ProteinModelPortaliP76254.
SMRiP76254.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini4 – 109FAD-binding FR-typeUniRule annotationAdd BLAST106
Domaini233 – 3212Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST89

Sequence similaritiesi

Belongs to the PDR/VanB family. CntB subfamily.UniRule annotationCurated

Phylogenomic databases

eggNOGiENOG4105E3J. Bacteria.
COG1018. LUCA.
HOGENOMiHOG000141052.
InParanoidiP76254.
OMAiVICCCVS.
PhylomeDBiP76254.

Family and domain databases

CDDicd00207. fer2. 1 hit.
Gene3Di3.10.20.30. 1 hit.
HAMAPiMF_02098. Carnitine_monoox_B. 1 hit.
InterProiView protein in InterPro
IPR036010. 2Fe-2S_ferredoxin-like_sf.
IPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR012675. Beta-grasp_dom_sf.
IPR017927. Fd_Rdtase_FAD-bd.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR000951. Ph_dOase_redase.
IPR017938. Riboflavin_synthase-like_b-brl.
PfamiView protein in Pfam
PF00970. FAD_binding_6. 1 hit.
PF00111. Fer2. 1 hit.
PF00175. NAD_binding_1. 1 hit.
PRINTSiPR00409. PHDIOXRDTASE.
SUPFAMiSSF54292. SSF54292. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiView protein in PROSITE
PS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51384. FAD_FR. 1 hit.

Sequencei

Sequence statusi: Complete.

P76254-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDYQMFEVQ VSQVEPLTEQ VKRFTLVATD GKPLPAFTGG SHVIVQMSDG
60 70 80 90 100
DNQYSNAYSL LSSPHDTSCY QIAVRLEENS RGGSRFLHQQ VKVGDRLTIS
110 120 130 140 150
TPNNLFALIP SARKHLFIAG GIGITPFLSH MAELQHSDVD WQLHYCSRNP
160 170 180 190 200
ESCAFRDELV QHPQAEKVHL HHSSTGTRLE LARLLADIEP GTHVYTCGPE
210 220 230 240 250
ALIEAVRSEA ARLDIAADTL HFEQFAIEDK TGDAFTLVLA RSGKEFVVPE
260 270 280 290 300
EMTILQVIEN NKAAKVECLC REGVCGTCET AILEGEADHR DQYFSDEERA
310 320
SQQSMLICCS RAKGKRLVLD L
Length:321
Mass (Da):35,661
Last modified:February 1, 1997 - v1
Checksum:iBD34122B24C08DBC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74873.1.
AP009048 Genomic DNA. Translation: BAA15598.1.
PIRiC64941.
RefSeqiNP_416317.1. NC_000913.3.
WP_001287026.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74873; AAC74873; b1803.
BAA15598; BAA15598; BAA15598.
GeneIDi946329.
KEGGiecj:JW1792.
eco:b1803.
PATRICifig|1411691.4.peg.450.

Similar proteinsi

Entry informationi

Entry nameiCNTB_ECOLI
AccessioniPrimary (citable) accession number: P76254
Secondary accession number(s): O07970, O07972
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: February 1, 1997
Last modified: March 28, 2018
This is version 139 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome