(data stored in ACNUC10821 zone)

SWISSPROT: C8U1B1_ECO10

ID   C8U1B1_ECO10            Unreviewed;       517 AA.
AC   C8U1B1;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 53.
DE   RecName: Full=Crotonobetaine/carnitine--CoA ligase {ECO:0000256|HAMAP-Rule:MF_01524};
DE            EC=6.2.1.48 {ECO:0000256|HAMAP-Rule:MF_01524};
GN   Name=caiC {ECO:0000256|HAMAP-Rule:MF_01524,
GN   ECO:0000313|EMBL:BAI28919.1};
GN   OrderedLocusNames=ECO103_0039 {ECO:0000313|EMBL:BAI28919.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI28919.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI28919.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- FUNCTION: Catalyzes the transfer of CoA to carnitine, generating
CC       the initial carnitinyl-CoA needed for the CaiB reaction cycle.
CC       Also has activity toward crotonobetaine and gamma-butyrobetaine.
CC       {ECO:0000256|HAMAP-Rule:MF_01524}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-carnitine + ATP + CoA = (R)-carnitinyl-CoA + AMP +
CC         diphosphate; Xref=Rhea:RHEA:28514, ChEBI:CHEBI:16347,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:60932, ChEBI:CHEBI:456215; EC=6.2.1.48;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01524};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-(trimethylamino)butanoate + ATP + CoA = AMP +
CC         diphosphate + gamma-butyrobetainyl-CoA; Xref=Rhea:RHEA:55960,
CC         ChEBI:CHEBI:16244, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:61513, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01524};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CoA + crotonobetaine = AMP + crotonobetainyl-CoA +
CC         diphosphate; Xref=Rhea:RHEA:30079, ChEBI:CHEBI:17237,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:60933, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01524};
CC   -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC       {ECO:0000256|HAMAP-Rule:MF_01524}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC       family. {ECO:0000256|HAMAP-Rule:MF_01524}.
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DR   EMBL; AP010958; BAI28919.1; -; Genomic_DNA.
DR   RefSeq; WP_001399722.1; NC_013353.1.
DR   EnsemblBacteria; BAI28919; BAI28919; ECO103_0039.
DR   KEGG; eoh:ECO103_0039; -.
DR   HOGENOM; HOG000230001; -.
DR   KO; K02182; -.
DR   OMA; WLMQRAF; -.
DR   BioCyc; ECOL585395:ECO103_RS00205-MONOMER; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0016878; F:acid-thiol ligase activity; IEA:InterPro.
DR   GO; GO:0051108; F:carnitine-CoA ligase activity; IEA:InterPro.
DR   GO; GO:0051109; F:crotonobetaine-CoA ligase activity; IEA:InterPro.
DR   GO; GO:0009437; P:carnitine metabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   HAMAP; MF_01524; CaiC; 1.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; AMP-dep_Synthh-like_sf.
DR   InterPro; IPR023456; CaiC.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8U1B1.
DR   SWISS-2DPAGE; C8U1B1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01524, ECO:0000313|EMBL:BAI28919.1}.
FT   DOMAIN       17    426       AMP-binding. {ECO:0000259|Pfam:PF00501}.
FT   DOMAIN      435    510       AMP-binding_C. {ECO:0000259|Pfam:
FT                                PF13193}.
SQ   SEQUENCE   517 AA;  58591 MW;  06A973F272067826 CRC64;
     MDIIGGQHLR QMWDDLADVY GHKTALIYES SGGVVNRYSY LELNQEINRT ANLFYTLGIR
     KGDKVALHLD NCPEFIFCWF GLAKIGAIMV PINARLLREE SAWILQNSQA CLLVTSAQFY
     PMYQQIQQED ATQLRHICLT DVALPADDGV SSFTQLKNQQ PATLCYAPPL STDDTAEILF
     TSGTTSRPKG VVITHYNLRF AGYYSAWQCA LRDDDVYLTV MPAFHIDCQC TAAMAAFSAG
     ATFVLVEKYS ARAFWGQVQK YRATITECIP MMIRTLMVQP PSANDRQHRL REVMFYLNLS
     EQEKDAFCER FGVRLLTSYG MTETIVGIIG DRPGDKRRWP SIGRAGFCYE AEIRDDHNRP
     LPAGEIGEIC IKGVPGKTIF KEYFLNPKAT AKVLEADGWL HTGDTGYCDE EGFFYFVDRR
     CNMIKRGGEN VSCVELENII ATHPKIQDIV VVGIKDSIRD EAIKAFVVLN EGETLSEEEF
     FRFCEQNMAK FKVPSYLEIR KDLPRNCSGK IIRKNLK
//

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