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UniProtKB - P0ABR7 (CNTA_ECOLI)
Protein
Carnitine monooxygenase oxygenase subunit
Gene
yeaW
Organism
Escherichia coli (strain K12)
Status
Functioni
Converts carnitine to trimethylamine and malic semialdehyde. Can also use gamma-butyrobetaine, choline and betaine as substrates.
1 PublicationCatalytic activityi
- (R)-carnitine + H+ + NADH + O2 = (3R)-3-hydroxy-4-oxobutanoate + H2O + NAD+ + trimethylamineUniRule annotation1 PublicationEC:1.14.13.239UniRule annotation1 Publication
- (R)-carnitine + H+ + NADPH + O2 = (3R)-3-hydroxy-4-oxobutanoate + H2O + NADP+ + trimethylamineUniRule annotation1 PublicationEC:1.14.13.239UniRule annotation1 Publication
Cofactori
Protein has several cofactor binding sites:- [2Fe-2S] clusterUniRule annotationNote: Binds 1 [2Fe-2S] cluster per subunit.UniRule annotation
- Fe cationUniRule annotationNote: Binds 1 Fe cation per subunit.UniRule annotation
: carnitine metabolism Pathwayi
This protein is involved in the pathway carnitine metabolism, which is part of Amine and polyamine metabolism.UniRule annotation1 PublicationView all proteins of this organism that are known to be involved in the pathway carnitine metabolism and in Amine and polyamine metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 89 | Iron-sulfur (2Fe-2S)UniRule annotation | 1 | |
Metal bindingi | 91 | Iron-sulfur (2Fe-2S); via pros nitrogenUniRule annotation | 1 | |
Metal bindingi | 109 | Iron-sulfur (2Fe-2S)UniRule annotation | 1 | |
Metal bindingi | 112 | Iron-sulfur (2Fe-2S); via pros nitrogenUniRule annotation | 1 | |
Metal bindingi | 211 | Iron; via tele nitrogenUniRule annotation | 1 | |
Metal bindingi | 216 | Iron; via tele nitrogenUniRule annotation | 1 | |
Metal bindingi | 325 | IronUniRule annotation | 1 |
GO - Molecular functioni
- 2 iron, 2 sulfur cluster binding Source: EcoCyc
- identical protein binding Source: EcoCyc
- iron ion binding Source: InterPro
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen Source: UniProtKB-UniRule
GO - Biological processi
- carnitine metabolic process Source: UniProtKB-UniPathway
Keywordsi
Molecular function | Oxidoreductase |
Ligand | 2Fe-2S, Iron, Iron-sulfur, Metal-binding, NAD, NADP |
Enzyme and pathway databases
BioCyci | EcoCyc:G6988-MONOMER |
UniPathwayi | UPA00117 |
Names & Taxonomyi
Protein namesi | Recommended name: Carnitine monooxygenase oxygenase subunitUniRule annotationCurated (EC:1.14.13.239UniRule annotation1 Publication)Alternative name(s): Carnitine monooxygenase alpha subunitUniRule annotationCurated |
Gene namesi | Name:yeaW Ordered Locus Names:b1802, JW5294 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000085063 | 1 – 374 | Carnitine monooxygenase oxygenase subunitAdd BLAST | 374 |
Proteomic databases
PaxDbi | P0ABR7 |
PRIDEi | P0ABR7 |
Interactioni
Subunit structurei
Composed of an oxygenase subunit (yeaW) and a reductase subunit (yeaX).
By similarityGO - Molecular functioni
- identical protein binding Source: EcoCyc
Protein-protein interaction databases
BioGRIDi | 4259149, 7 interactors |
STRINGi | 511145.b1802 |
Chemistry databases
BindingDBi | P0ABR7 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 47 – 155 | RieskeUniRule annotationAdd BLAST | 109 |
Sequence similaritiesi
Belongs to the bacterial ring-hydroxylating dioxygenase alpha subunit family. CntA subfamily.UniRule annotationCurated
Phylogenomic databases
eggNOGi | COG4638, Bacteria |
HOGENOMi | CLU_026244_3_0_6 |
InParanoidi | P0ABR7 |
PhylomeDBi | P0ABR7 |
Family and domain databases
Gene3Di | 2.102.10.10, 1 hit |
HAMAPi | MF_02097, Carnitine_monoox_A, 1 hit |
InterProi | View protein in InterPro IPR039004, Carnitine_monoox_A IPR044637, RHO IPR017941, Rieske_2Fe-2S IPR036922, Rieske_2Fe-2S_sf IPR015881, Ring-hydroxy_dOase_2Fe2S_BS IPR015879, Ring_hydroxy_dOase_asu_C_dom IPR001663, Rng_hydr_dOase-A |
PANTHERi | PTHR43756, PTHR43756, 1 hit |
Pfami | View protein in Pfam PF00355, Rieske, 1 hit PF00848, Ring_hydroxyl_A, 1 hit |
PRINTSi | PR00090, RNGDIOXGNASE |
SUPFAMi | SSF50022, SSF50022, 1 hit |
PROSITEi | View protein in PROSITE PS51296, RIESKE, 1 hit PS00570, RING_HYDROXYL_ALPHA, 1 hit |
i Sequence
Sequence statusi: Complete.
P0ABR7-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSNLSPDFVL PENFCANPQE AWTIPARFYT DQNAFEHEKE NVFAKSWICV
60 70 80 90 100
AHSSELANAN DYVTREIIGE SIVLVRGRDK VLRAFYNVCP HRGHQLLSGE
110 120 130 140 150
GKAKNVITCP YHAWAFKLDG NLAHARNCEN VANFDSDKAQ LVPVRLEEYA
160 170 180 190 200
GFVFINMDPN ATSVEDQLPG LGAKVLEACP EVHDLKLAAR FTTRTPANWK
210 220 230 240 250
NIVDNYLECY HCGPAHPGFS DSVQVDRYWH TMHGNWTLQY GFAKPSEQSF
260 270 280 290 300
KFEEGTDAAF HGFWLWPCTM LNVTPIKGMM TVIYEFPVDS ETTLQNYDIY
310 320 330 340 350
FTNEELTDEQ KSLIEWYRDV FRPEDLRLVE SVQKGLKSRG YRGQGRIMAD
360 370
SSGSGISEHG IAHFHNLLAQ VFKD
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U00096 Genomic DNA Translation: AAC74872.1 AP009048 Genomic DNA Translation: BAA15597.2 |
PIRi | B64941 |
RefSeqi | NP_416316.1, NC_000913.3 WP_000067822.1, NZ_SSZK01000001.1 |
Genome annotation databases
EnsemblBacteriai | AAC74872; AAC74872; b1802 BAA15597; BAA15597; BAA15597 |
GeneIDi | 66674309 946325 |
KEGGi | ecj:JW5294 eco:b1802 |
PATRICi | fig|1411691.4.peg.451 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U00096 Genomic DNA Translation: AAC74872.1 AP009048 Genomic DNA Translation: BAA15597.2 |
PIRi | B64941 |
RefSeqi | NP_416316.1, NC_000913.3 WP_000067822.1, NZ_SSZK01000001.1 |
3D structure databases
SMRi | P0ABR7 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 4259149, 7 interactors |
STRINGi | 511145.b1802 |
Chemistry databases
BindingDBi | P0ABR7 |
Proteomic databases
PaxDbi | P0ABR7 |
PRIDEi | P0ABR7 |
Genome annotation databases
EnsemblBacteriai | AAC74872; AAC74872; b1802 BAA15597; BAA15597; BAA15597 |
GeneIDi | 66674309 946325 |
KEGGi | ecj:JW5294 eco:b1802 |
PATRICi | fig|1411691.4.peg.451 |
Organism-specific databases
EchoBASEi | EB3282 |
Phylogenomic databases
eggNOGi | COG4638, Bacteria |
HOGENOMi | CLU_026244_3_0_6 |
InParanoidi | P0ABR7 |
PhylomeDBi | P0ABR7 |
Enzyme and pathway databases
UniPathwayi | UPA00117 |
BioCyci | EcoCyc:G6988-MONOMER |
Miscellaneous databases
PROi | PR:P0ABR7 |
Family and domain databases
Gene3Di | 2.102.10.10, 1 hit |
HAMAPi | MF_02097, Carnitine_monoox_A, 1 hit |
InterProi | View protein in InterPro IPR039004, Carnitine_monoox_A IPR044637, RHO IPR017941, Rieske_2Fe-2S IPR036922, Rieske_2Fe-2S_sf IPR015881, Ring-hydroxy_dOase_2Fe2S_BS IPR015879, Ring_hydroxy_dOase_asu_C_dom IPR001663, Rng_hydr_dOase-A |
PANTHERi | PTHR43756, PTHR43756, 1 hit |
Pfami | View protein in Pfam PF00355, Rieske, 1 hit PF00848, Ring_hydroxyl_A, 1 hit |
PRINTSi | PR00090, RNGDIOXGNASE |
SUPFAMi | SSF50022, SSF50022, 1 hit |
PROSITEi | View protein in PROSITE PS51296, RIESKE, 1 hit PS00570, RING_HYDROXYL_ALPHA, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | CNTA_ECOLI | |
Accessioni | P0ABR7Primary (citable) accession number: P0ABR7 Secondary accession number(s): P76253 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 8, 2005 |
Last sequence update: | November 8, 2005 | |
Last modified: | February 23, 2022 | |
This is version 117 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families