(data stored in ACNUC7421 zone)

SWISSPROT: CAIC_ECODH

ID   CAIC_ECODH              Reviewed;         517 AA.
AC   B1XBG2;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   05-JUL-2017, entry version 60.
DE   RecName: Full=Probable crotonobetaine/carnitine-CoA ligase {ECO:0000255|HAMAP-Rule:MF_01524};
DE            EC=6.2.1.- {ECO:0000255|HAMAP-Rule:MF_01524};
GN   Name=caiC {ECO:0000255|HAMAP-Rule:MF_01524};
GN   OrderedLocusNames=ECDH10B_0038;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/JB.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into
RT   the biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(2008).
CC   -!- FUNCTION: Could catalyze the transfer of CoA to carnitine,
CC       generating the initial carnitinyl-CoA needed for the CaiB reaction
CC       cycle. {ECO:0000255|HAMAP-Rule:MF_01524}.
CC   -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC       {ECO:0000255|HAMAP-Rule:MF_01524}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC       family. {ECO:0000255|HAMAP-Rule:MF_01524}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACB01242.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; CP000948; ACB01242.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001350478.1; NC_010473.1.
DR   ProteinModelPortal; B1XBG2; -.
DR   SMR; B1XBG2; -.
DR   EnsemblBacteria; ACB01242; ACB01242; ECDH10B_0038.
DR   KEGG; ecd:ECDH10B_0038; -.
DR   eggNOG; ENOG4105CEY; Bacteria.
DR   eggNOG; COG0318; LUCA.
DR   HOGENOM; HOG000230001; -.
DR   KO; K02182; -.
DR   UniPathway; UPA00117; -.
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   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; 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; B1XBG2.
DR   SWISS-2DPAGE; B1XBG2.
KW   Ligase.
FT   CHAIN         1    517       Probable crotonobetaine/carnitine-CoA
FT                                ligase.
FT                                /FTId=PRO_0000383396.
SQ   SEQUENCE   517 AA;  58559 MW;  C7A307D16200D8E9 CRC64;
     MDIIGGQHLR QMWDDLADVY GHKTALICES SGGVVNRYSY LELNQEINRT ANLFYTLGIR
     KGDKVALHLD NCPEFIFCWF GLAKIGAIMV PINARLLCEE SAWILQNSQA CLLVTSAQFY
     PMYQQIQQED ATQLRHICLT DVALPADDGV SSFTQLKNQQ PATLCYAPPL STDDTAEILF
     TSGTTSRPKG VVITHYNLRF AGYYSAWQCA LRDDDVYLTV MPAFHIDCQC TAAMAAFSAG
     ATFVLVEKYS ARAFWGQVQK YRATVTECIP MMIRTLMVQP PSANDQQHRL REVMFYLNLS
     EQEKDAFCER FGVRLLTSYG MTETIVGIIG DRPGDKRRWP SIGRVGFCYE AEIRDDHNRP
     LPAGEIGEIC IKGIPGKTIF KEYFLNPQAT AKVLEADGWL HTGDTGYRDE EDFFYFVDRR
     CNMIKRGGEN VSCVELENII AAHPKIQDIV VVGIKDSIRD EAIKAFVVLN EGETLSEEEF
     FRFCEQNMAK FKVPSYLEIR KDLPRNCSGK IIRKNLK
//

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