ID   SMTA_CHLAA              Reviewed;         455 AA.
AC   A9WC40;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Succinyl-CoA--L-malate CoA-transferase alpha subunit;
DE            EC=2.8.3.22;
GN   Name=smtA; OrderedLocusNames=Caur_0179;
OS   Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl).
OC   Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae;
OC   Chloroflexaceae; Chloroflexus.
OX   NCBI_TaxID=324602;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29366 / DSM 635 / J-10-fl;
RX   PubMed=21714912; DOI=10.1186/1471-2164-12-334;
RA   Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J.,
RA   Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W.,
RA   Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.;
RT   "Complete genome sequence of the filamentous anoxygenic phototrophic
RT   bacterium Chloroflexus aurantiacus.";
RL   BMC Genomics 12:334-334(2011).
CC   -!- FUNCTION: Involved in the 3-hydroxypropionate cycle used for
CC       autotrophic carbon dioxide fixation. Catalyzes the transfer of CoA
CC       moiety from succinyl-CoA to L-malate to yield L-malyl-CoA (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-malate + succinyl-CoA = (S)-malyl-CoA + succinate;
CC         Xref=Rhea:RHEA:38255, ChEBI:CHEBI:15589, ChEBI:CHEBI:30031,
CC         ChEBI:CHEBI:57292, ChEBI:CHEBI:57317; EC=2.8.3.22;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3S)-citramalate + succinyl-CoA = (3S)-citramalyl-CoA +
CC         succinate; Xref=Rhea:RHEA:38287, ChEBI:CHEBI:30031,
CC         ChEBI:CHEBI:30936, ChEBI:CHEBI:57292, ChEBI:CHEBI:58668; EC=2.8.3.22;
CC   -!- SUBUNIT: Forms a large complex composed of six heterodimers (alpha,
CC       beta). {ECO:0000250}.
CC   -!- INDUCTION: Under autotrophic growth conditions. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the CoA-transferase III family. {ECO:0000305}.
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DR   EMBL; CP000909; ABY33433.1; -; Genomic_DNA.
DR   RefSeq; WP_012256089.1; NC_010175.1.
DR   RefSeq; YP_001633822.1; NC_010175.1.
DR   AlphaFoldDB; A9WC40; -.
DR   SMR; A9WC40; -.
DR   STRING; 324602.Caur_0179; -.
DR   EnsemblBacteria; ABY33433; ABY33433; Caur_0179.
DR   KEGG; cau:Caur_0179; -.
DR   PATRIC; fig|324602.8.peg.208; -.
DR   eggNOG; COG1804; Bacteria.
DR   HOGENOM; CLU_033975_2_0_0; -.
DR   InParanoid; A9WC40; -.
DR   OMA; ATYLGEF; -.
DR   BioCyc; MetaCyc:MON-13599; -.
DR   Proteomes; UP000002008; Chromosome.
DR   GO; GO:0008410; F:CoA-transferase activity; ISS:UniProtKB.
DR   GO; GO:0047370; F:succinate-citramalate CoA-transferase activity; IEA:RHEA.
DR   GO; GO:0043427; P:carbon fixation by 3-hydroxypropionate cycle; ISS:UniProtKB.
DR   Gene3D; 3.30.1540.10; -; 1.
DR   Gene3D; 3.40.50.10540; -; 1.
DR   InterPro; IPR003673; CoA-Trfase_fam_III.
DR   InterPro; IPR044855; CoA-Trfase_III_dom3_sf.
DR   InterPro; IPR023606; CoA-Trfase_III_dom_1_sf.
DR   Pfam; PF02515; CoA_transf_3; 1.
DR   SUPFAM; SSF89796; SSF89796; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation; Reference proteome; Transferase.
FT   CHAIN           1..455
FT                   /note="Succinyl-CoA--L-malate CoA-transferase alpha
FT                   subunit"
FT                   /id="PRO_0000429592"
FT   REGION          1..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        227
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   455 AA;  49514 MW;  02E3785CFACC9A21 CRC64;
     MAKASRLTRS TGQPTEVSEG QVTGTSEMPP TGEEPSGHAE SKPPASDPMS TPGTGQEQLP
     LSGIRVIDVG NFLAGPYAAS ILGEFGAEVL KIEHPLGGDP MRRFGTATAR HDATLAWLSE
     ARNRKSVTID LRQQEGVALF LKLVAKSDIL IENFRPGTME EWGLSWPVLQ ATNPGLIMLR
     VSGYGQTGPY RRRSGFAHIA HAFSGLSYLA GFPGETPVLP GTAPLGDYIA SLFGAIGILI
     ALRHKEQTGR GQLIDVGIYE AVFRILDEIA PAYGLFGKIR EREGAGSFIA VPHGHFRSKD
     GKWVAIACTT DKMFERLAEA MERPELASPE LYGDQRKRLA ARDIVNQITI EWVGSLTRDE
     VMRRCLEKEV PVGPLNSIAD MFNDEHFLAR GNFACIEAEG IGEVVVPNVI PRLSETPGRV
     TNLGPPLGNA TYEVLRELLD ISAEEIKRLR SRKII