CAID_SALPB
ID CAID_SALPB Reviewed; 261 AA.
AC A9MYJ5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Carnitinyl-CoA dehydratase {ECO:0000255|HAMAP-Rule:MF_01051};
DE EC=4.2.1.149 {ECO:0000255|HAMAP-Rule:MF_01051};
DE AltName: Full=Crotonobetainyl-CoA hydratase {ECO:0000255|HAMAP-Rule:MF_01051};
GN Name=caiD {ECO:0000255|HAMAP-Rule:MF_01051}; OrderedLocusNames=SPAB_00086;
OS Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=1016998;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1250 / SPB7;
RG The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible dehydration of L-carnitinyl-CoA to
CC crotonobetainyl-CoA. {ECO:0000255|HAMAP-Rule:MF_01051}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitinyl-CoA = crotonobetainyl-CoA + H2O;
CC Xref=Rhea:RHEA:28338, ChEBI:CHEBI:15377, ChEBI:CHEBI:60932,
CC ChEBI:CHEBI:60933; EC=4.2.1.149; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01051};
CC -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC {ECO:0000255|HAMAP-Rule:MF_01051}.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000255|HAMAP-Rule:MF_01051}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000886; ABX65529.1; -; Genomic_DNA.
DR RefSeq; WP_000004383.1; NC_010102.1.
DR AlphaFoldDB; A9MYJ5; -.
DR SMR; A9MYJ5; -.
DR KEGG; spq:SPAB_00086; -.
DR PATRIC; fig|1016998.12.peg.83; -.
DR HOGENOM; CLU_009834_7_6_6; -.
DR OMA; AMEMIMT; -.
DR BioCyc; SENT1016998:SPAB_RS00345-MON; -.
DR UniPathway; UPA00117; -.
DR Proteomes; UP000008556; Chromosome.
DR GO; GO:0016836; F:hydro-lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009437; P:carnitine metabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.12.10; -; 1.
DR HAMAP; MF_01051; CaiD; 1.
DR InterPro; IPR022852; Carnitinyl_CoA_dehydratase.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR InterPro; IPR014748; Enoyl-CoA_hydra_C.
DR Pfam; PF00378; ECH_1; 1.
DR SUPFAM; SSF52096; SSF52096; 1.
DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE 3: Inferred from homology;
KW Lyase.
FT CHAIN 1..261
FT /note="Carnitinyl-CoA dehydratase"
FT /id="PRO_1000084427"
FT ACT_SITE 111
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01051"
FT ACT_SITE 131
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01051"
SQ SEQUENCE 261 AA; 28092 MW; 114133D2A22A0FEA CRC64;
MSESLHLTRN GPILEITLDR PKANAIDAKT SFAMGEAFLN FRDDPELRVA IITGGGEKFF
SAGWDLKAAA EGEAPDADFG PGGFAGLTEI FDLDKPVIAA VNGYAFGGGF ELALAADFIV
CAENASFALP EAKLGIVPDS GGVLRLPKLL PPAIVNEMVM TGRRMSAEEA LRWGVVNRVV
SQSELMDSAR ELAQQLVNSA PLAIAALKEI YRATSEMPVE EGYRYIRSGV LKHYPSVLHS
EDALEGPQAF AEKRDPVWKG R