MCT_HALHT
ID MCT_HALHT Reviewed; 396 AA.
AC G0HQ31;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 25-MAY-2022, entry version 54.
DE RecName: Full=Succinyl-CoA:mesaconate CoA-transferase {ECO:0000303|PubMed:28932214};
DE EC=2.8.3.26 {ECO:0000269|PubMed:28932214};
DE AltName: Full=Mesaconate CoA-transferase {ECO:0000303|PubMed:28932214};
GN Name=mct {ECO:0000303|PubMed:28932214};
GN OrderedLocusNames=HAH_1336 {ECO:0000312|EMBL:AEM56950.1};
OS Haloarcula hispanica (strain ATCC 33960 / DSM 4426 / JCM 8911 / NBRC 102182
OS / NCIMB 2187 / VKM B-1755).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=634497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33960 / DSM 4426 / JCM 8911 / NBRC 102182 / NCIMB 2187 / VKM
RC B-1755;
RX PubMed=21994921; DOI=10.1128/jb.05953-11;
RA Liu H., Wu Z., Li M., Zhang F., Zheng H., Han J., Liu J., Zhou J., Wang S.,
RA Xiang H.;
RT "Complete genome sequence of Haloarcula hispanica, a model haloarchaeon for
RT studying genetics, metabolism, and virus-host interaction.";
RL J. Bacteriol. 193:6086-6087(2011).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RX PubMed=28932214; DOI=10.3389/fmicb.2017.01683;
RA Borjian F., Johnsen U., Schoenheit P., Berg I.A.;
RT "Succinyl-CoA:mesaconate CoA-transferase and mesaconyl-CoA hydratase,
RT enzymes of the methylaspartate cycle in Haloarcula hispanica.";
RL Front. Microbiol. 8:1683-1683(2017).
CC -!- FUNCTION: Involved in the methylaspartate cycle. Catalyzes the transfer
CC of the CoA moiety from succinyl-CoA to mesaconate to generate
CC mesaconyl-CoA (2-methylfumaryl-CoA) and succinate (PubMed:28932214).
CC Shows also high activity with methylsuccinate as CoA-acceptor, and only
CC low activity with glutarate, acrylate and itaconate (PubMed:28932214).
CC Cannot use other CoA donors like acetyl-CoA, propionyl-CoA, butyryl-CoA
CC or acetoacetyl-CoA (PubMed:28932214). {ECO:0000269|PubMed:28932214}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=mesaconate + succinyl-CoA = 2-methylfumaryl-CoA + succinate;
CC Xref=Rhea:RHEA:45820, ChEBI:CHEBI:30031, ChEBI:CHEBI:36986,
CC ChEBI:CHEBI:57292, ChEBI:CHEBI:75635; EC=2.8.3.26;
CC Evidence={ECO:0000269|PubMed:28932214};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45821;
CC Evidence={ECO:0000269|PubMed:28932214};
CC -!- ACTIVITY REGULATION: Shows highest activity at 4 M KCl. Does not
CC require divalent ions for activity. {ECO:0000269|PubMed:28932214}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.8 mM for succinyl-CoA (in the presence of 10 mM mesaconate)
CC {ECO:0000269|PubMed:28932214};
CC KM=1.3 mM for mesaconate (in the presence of 1 mM succinyl-CoA)
CC {ECO:0000269|PubMed:28932214};
CC KM=7.1 mM for mesaconate (in the presence of 5 mM succinyl-CoA)
CC {ECO:0000269|PubMed:28932214};
CC KM=0.6 mM for methylsuccinate (in the presence of 1 mM succinyl-CoA)
CC {ECO:0000269|PubMed:28932214};
CC KM=2.9 mM for methylsuccinate (in the presence of 5 mM succinyl-CoA)
CC {ECO:0000269|PubMed:28932214};
CC KM=40.9 mM for glutarate (in the presence of 1 mM succinyl-CoA)
CC {ECO:0000269|PubMed:28932214};
CC KM=39.3 mM for acrylate (in the presence of 1 mM succinyl-CoA)
CC {ECO:0000269|PubMed:28932214};
CC Vmax=69.2 umol/min/mg enzyme with succinyl-CoA as substrate (in the
CC presence of 10 mM mesaconate) {ECO:0000269|PubMed:28932214};
CC Vmax=17.0 umol/min/mg enzyme with mesaconate as substrate (in the
CC presence of 1 mM succinyl-CoA) {ECO:0000269|PubMed:28932214};
CC Vmax=45.0 umol/min/mg enzyme with mesaconate as substrate (in the
CC presence of 5 mM succinyl-CoA) {ECO:0000269|PubMed:28932214};
CC Vmax=11.0 umol/min/mg enzyme with methylsuccinate as substrate (in
CC the presence of 1 mM succinyl-CoA) {ECO:0000269|PubMed:28932214};
CC Vmax=36.8 umol/min/mg enzyme with methylsuccinate as substrate (in
CC the presence of 5 mM succinyl-CoA) {ECO:0000269|PubMed:28932214};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:28932214}.
CC -!- SIMILARITY: Belongs to the CoA-transferase III family. {ECO:0000305}.
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DR EMBL; CP002921; AEM56950.1; -; Genomic_DNA.
DR RefSeq; WP_014040202.1; NC_015948.1.
DR AlphaFoldDB; G0HQ31; -.
DR SMR; G0HQ31; -.
DR STRING; 634497.HAH_1336; -.
DR EnsemblBacteria; AEM56950; AEM56950; HAH_1336.
DR GeneID; 23803956; -.
DR KEGG; hhi:HAH_1336; -.
DR eggNOG; arCOG02304; Archaea.
DR HOGENOM; CLU_033975_0_0_2; -.
DR OMA; HRPGFGT; -.
DR OrthoDB; 20007at2157; -.
DR BRENDA; 2.8.3.26; 8340.
DR Proteomes; UP000005629; Chromosome I.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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 Transferase.
FT CHAIN 1..396
FT /note="Succinyl-CoA:mesaconate CoA-transferase"
FT /id="PRO_0000451974"
FT ACT_SITE 175
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P69902"
SQ SEQUENCE 396 AA; 42996 MW; 97010EA7B48BAB66 CRC64;
MGALDDLRVL DLTQVLAGPY CTMLLADMGA DVVKVERPGG DLIRSNPPFV SDGDEEAYGG
YFQSVNRGKR SLELDLGTDE DREAFLSLVE RADVVVENFK AGTMEKFDCG YETLREHNPD
LIYSSIRGFG DPRTGETHRQ GQPSFDLIAQ ALGGVMEITG QSDGPPTKVG PGVGDLFTAV
LNAVGILAAV HHRERTGEGQ YVDTAMYDSM VSLCERTVYQ YSCDGESPTR QGNSHPTLFP
YDSFEAADGH VVIAAFADGH WETLCEAMER PDLAADYPDA GSRIANRESL RREIADWTAT
IDSETLLDLL EGRVPAAPVQ NTADIFDDPH IHDREMLTDV DQPGADEQIT IAGSPIKMTE
TMPSPGGRAP LLDEHRAELL DEAGVGTGTN RVESDD
