ID   SMTB_CHLAU              Reviewed;         405 AA.
AC   Q1KLK0;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Succinyl-CoA--L-malate CoA-transferase beta subunit;
DE            EC=2.8.3.22;
GN   Name=smtB;
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=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; DQ472737; ABF14400.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1KLK0; -.
DR   SMR; Q1KLK0; -.
DR   PRIDE; Q1KLK0; -.
DR   KEGG; ag:ABF14400; -.
DR   OMA; PGAMEGW; -.
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..405
FT                   /note="Succinyl-CoA--L-malate CoA-transferase beta subunit"
FT                   /id="PRO_0000429593"
FT   ACT_SITE        175
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   405 AA;  44384 MW;  58041E71692E2F4E CRC64;
     MDGTTTTLPL AGIRVIDAAT VIAAPFCATL LGEFGADVLK VEHPIGGDAL RRFGTPTARG
     DTLTWLSESR NKRSVTLNLQ HPEGARVFKE LIAHSDVLCE NFRPGTLEKW GLGWDVLSKI
     NPRLIMLRVT GYGQTGPYRD RPGFARIAHA VGGIAYLAGM PKGTPVTPGS TTLADYMTGL
     YGCIGVLLAL RHREQTGRGQ YIDAALYESV FRCSDELVPA YGMYRKVRER HGSHYNEFAC
     PHGHFQTKDG KWVAISCATD KLFARLANAM GRPELASSSV YGDQKVRLAH ASDVNEIVRD
     WCSSLTRAEV LERCYATATP AAPLNDIADF FGDRHVHARR NLVAIDAEDL GETLIMPNVV
     PKLSETPGSI RSLGPKLGEH TEEVLKEILG MCDEQINDLR SKRVI