ID   SMTA_CHLAU              Reviewed;         428 AA.
AC   Q1KLK1;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 47.
DE   RecName: Full=Succinyl-CoA--L-malate CoA-transferase alpha subunit;
DE            EC=2.8.3.22;
GN   Name=smtA;
OS   Chloroflexus aurantiacus.
OC   Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae;
OC   Chloroflexaceae; Chloroflexus.
OX   NCBI_TaxID=1108;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-4, FUNCTION,
RP   CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, SUBSTRATE
RP   SPECIFICITY, SUBUNIT, AND NOMENCLATURE.
RC   STRAIN=DSM 636 / OK-70-fl;
RX   PubMed=16547052; DOI=10.1128/jb.188.7.2646-2655.2006;
RA   Friedmann S., Steindorf A., Alber B.E., Fuchs G.;
RT   "Properties of succinyl-coenzyme A:L-malate coenzyme A transferase and its
RT   role in the autotrophic 3-hydroxypropionate cycle of Chloroflexus
RT   aurantiacus.";
RL   J. Bacteriol. 188:2646-2655(2006).
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. It is highly
CC       specific for succinyl-CoA as the CoA donor, however it can accept L-
CC       citramalate instead of L-malate as the CoA acceptor.
CC       {ECO:0000269|PubMed:16547052}.
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         Evidence={ECO:0000269|PubMed:16547052};
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         Evidence={ECO:0000269|PubMed:16547052};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.5 mM for succinyl-CoA {ECO:0000269|PubMed:16547052};
CC         KM=1.1 mM for L-citramalate {ECO:0000269|PubMed:16547052};
CC         KM=1.3 mM for L-malate {ECO:0000269|PubMed:16547052};
CC       pH dependence:
CC         Optimum pH is 6.5. {ECO:0000269|PubMed:16547052};
CC       Temperature dependence:
CC         Optimum temperature is 55 degrees Celsius.
CC         {ECO:0000269|PubMed:16547052};
CC   -!- SUBUNIT: Forms a large complex composed of six heterodimers (alpha,
CC       beta). {ECO:0000269|PubMed:16547052}.
CC   -!- INDUCTION: Under autotrophic growth conditions.
CC       {ECO:0000269|PubMed:16547052}.
CC   -!- SIMILARITY: Belongs to the CoA-transferase III family. {ECO:0000305}.
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DR   EMBL; DQ472736; ABF14399.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1KLK1; -.
DR   SMR; Q1KLK1; -.
DR   KEGG; ag:ABF14399; -.
DR   GO; GO:0008410; F:CoA-transferase activity; IDA:UniProtKB.
DR   GO; GO:0047370; F:succinate-citramalate CoA-transferase activity; IEA:RHEA.
DR   GO; GO:0043427; P:carbon fixation by 3-hydroxypropionate cycle; IDA: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   1: Evidence at protein level;
KW   Carbon dioxide fixation; Direct protein sequencing; Transferase.
FT   CHAIN           1..428
FT                   /note="Succinyl-CoA--L-malate CoA-transferase alpha
FT                   subunit"
FT                   /id="PRO_0000429591"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        200
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   428 AA;  46723 MW;  A616A04416CB9A9F CRC64;
     MPPTGEEPSG HAESKPPASD PMSTPGTGQE QLPLSGIRVI DVGNFLAGPY AASILGEFGA
     EVLKIEHPLG GDPMRRFGTA TARHDATLAW LSEARNRKSV TIDLRQQEGV ALFLKLVAKS
     DILIENFRPG TMEEWGLSWP VLQATNPGLI MLRVSGYGQT GPYRRRSGFA HIAHAFSGLS
     YLAGFPGETP VLPGTAPLGD YIASLFGAIG ILIALRHKEQ TGRGQLIDVG IYEAVFRILD
     EIAPAYGLFG KIREREGAGS FIAVPHGHFR SKDGKWVAIA CTTDKMFERL AEAMERPELA
     SPELYGDQRK RLAARDIVNQ ITIEWVGSLT RDEVMRRCLE KEVPVGPLNS IADMFNDEHF
     LARGNFACIE AEGIGEVVVP NVIPRLSETP GRVTNLGPPL GNATYEVLRE LLDISAEEIK
     RLRSRKII