ID   CARA_ACEWO              Reviewed;         524 AA.
AC   F1CYZ5;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   25-MAY-2022, entry version 29.
DE   RecName: Full=Caffeate CoA-transferase {ECO:0000303|PubMed:23315745};
DE            EC=2.8.3.23 {ECO:0000269|PubMed:23315745};
DE   AltName: Full=Hydrocaffeyl-CoA:caffeate CoA transferase {ECO:0000303|PubMed:21131487};
GN   Name=carA {ECO:0000303|PubMed:21131487};
OS   Acetobacterium woodii.
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Acetobacterium.
OX   NCBI_TaxID=33952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM1030;
RX   PubMed=17873051; DOI=10.1128/jb.01017-07;
RA   Imkamp F., Biegel E., Jayamani E., Buckel W., Muller V.;
RT   "Dissection of the caffeate respiratory chain in the acetogen
RT   Acetobacterium woodii: identification of an Rnf-type NADH dehydrogenase as
RT   a potential coupling site.";
RL   J. Bacteriol. 189:8145-8153(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC   STRAIN=DSM1030;
RX   PubMed=21131487; DOI=10.1128/jb.01126-10;
RA   Hess V., Vitt S., Muller V.;
RT   "A caffeyl-coenzyme A synthetase initiates caffeate activation prior to
RT   caffeate reduction in the acetogenic bacterium Acetobacterium woodii.";
RL   J. Bacteriol. 193:971-978(2011).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP   SPECIFICITY, SUBUNIT, AND REACTION MECHANISM.
RX   PubMed=23315745; DOI=10.1128/aem.03604-12;
RA   Hess V., Gonzalez J.M., Parthasarathy A., Buckel W., Mueller V.;
RT   "Caffeate respiration in the acetogenic bacterium Acetobacterium woodii: a
RT   coenzyme A loop saves energy for caffeate activation.";
RL   Appl. Environ. Microbiol. 79:1942-1947(2013).
CC   -!- FUNCTION: Involved in caffeate respiration, which consists in the
CC       reduction of the C-C double bond of caffeate. CarA catalyzes an energy-
CC       saving CoA loop for caffeate activation in the steady state of caffeate
CC       respiration. It catalyzes the formation of caffeyl-CoA from caffeate
CC       with hydrocaffeyl-CoA as the CoA donor via a ping-pong mechanism. In
CC       addition to caffeate, the enzyme can utilize 4-coumarate or ferulate as
CC       CoA acceptor. Neither acetyl-CoA nor butyryl-CoA served as the CoA
CC       donor. {ECO:0000269|PubMed:23315745}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-caffeate + hydrocaffeoyl-CoA = (E)-caffeoyl-CoA + 3-(3,4-
CC         dihydroxyphenyl)propanoate; Xref=Rhea:RHEA:38027, ChEBI:CHEBI:57770,
CC         ChEBI:CHEBI:58744, ChEBI:CHEBI:87136, ChEBI:CHEBI:87137; EC=2.8.3.23;
CC         Evidence={ECO:0000269|PubMed:23315745};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2 uM for hydrocaffeyl-CoA {ECO:0000269|PubMed:23315745};
CC         KM=75 uM for caffeate {ECO:0000269|PubMed:23315745};
CC         Vmax=125 umol/min/mg enzyme {ECO:0000269|PubMed:23315745};
CC         Note=kcat is 120 sec(-1) for transferase activity with caffeate as
CC         substrate. {ECO:0000269|PubMed:23315745};
CC       pH dependence:
CC         Optimum pH is 7.5. {ECO:0000269|PubMed:23315745};
CC       Temperature dependence:
CC         Optimum temperature is 40 degrees Celsius.
CC         {ECO:0000269|PubMed:23315745};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:23315745}.
CC   -!- INDUCTION: Induced by cinnamate and sinapate.
CC       {ECO:0000269|PubMed:21131487}.
CC   -!- SIMILARITY: Belongs to the 3-oxoacid CoA-transferase family.
CC       {ECO:0000305}.
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DR   EMBL; HQ616211; ADX43861.1; -; Genomic_DNA.
DR   AlphaFoldDB; F1CYZ5; -.
DR   SMR; F1CYZ5; -.
DR   OMA; AARIRYY; -.
DR   BRENDA; 2.8.3.23; 52.
DR   GO; GO:0008410; F:CoA-transferase activity; IEA:InterPro.
DR   GO; GO:0016782; F:transferase activity, transferring sulphur-containing groups; IDA:UniProtKB.
DR   GO; GO:0046952; P:ketone body catabolic process; IEA:InterPro.
DR   InterPro; IPR014388; 3-oxoacid_CoA-transferase.
DR   InterPro; IPR004165; CoA_trans_fam_I.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   Pfam; PF01144; CoA_trans; 1.
DR   PIRSF; PIRSF000858; SCOT-t; 1.
DR   SMART; SM00882; CoA_trans; 2.
DR   SUPFAM; SSF100950; SSF100950; 2.
PE   1: Evidence at protein level;
KW   Transferase.
FT   CHAIN           1..524
FT                   /note="Caffeate CoA-transferase"
FT                   /id="PRO_0000435660"
FT   ACT_SITE        323
FT                   /note="5-glutamyl coenzyme A thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10034"
SQ   SEQUENCE   524 AA;  56205 MW;  597140576F31AA1B CRC64;
     MAKFISAKEA AKLIPDGSTV GVAGMGLAGW PEEVAVAIAD NFKETGHPCN LTMKQGSAMG
     DWRERGMTRL GLEGLVTKWS AAHIGSAFAM NDLVRAEKMA CHCLPQGVIV NLWREIAAKR
     PGLITKVGLG TFVDPRLEGG KMNKVTTEDL VELIEFNGEE YLFYKSFKLD VAMLRGTTAD
     ENGNITFENE GPINEGLAVA QAAKNSGGIV IVQVEYQALK NTLKPKDVKI PGALVDYVVV
     ATDKNACWQT EGVYYEPAFA GNLRKPLSAI PILPLTERKV MARRAAMELS KGDLVNLGVG
     IPSDVASIVS EAGYIEEITM TTEIGGFGGI PASLPNFGSS YNAEANIDHG SMFDLYDGGG
     IDVAVLGLAQ ADEAGNINVS KFTIPGLGDR LTGPGGFINI TQSTQKVVFA GSFNAKCEVE
     ISDGKLIIKK EGRGKKLLKE VEQVTFSGKY AAENGQEILY VTERCVFKLI NGKMTVIEIA
     PGIDLQKDIL DQMDFTPAIS ADLKEMDSGL FSEKWDGLDT IMGK