MCT_HALMA
ID MCT_HALMA Reviewed; 396 AA.
AC Q5V468;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 11-JUN-2014, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Succinyl-CoA:mesaconate CoA-transferase {ECO:0000303|PubMed:21252347};
DE EC=2.8.3.26 {ECO:0000305|PubMed:21252347};
GN Name=mct {ECO:0000303|PubMed:21252347}; OrderedLocusNames=rrnAC0683;
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=21252347; DOI=10.1126/science.1196544;
RA Khomyakova M., Bukmez O., Thomas L.K., Erb T.J., Berg I.A.;
RT "A methylaspartate cycle in haloarchaea.";
RL Science 331:334-337(2011).
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.
CC {ECO:0000269|PubMed:21252347}.
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:0000305|PubMed:21252347};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45821;
CC Evidence={ECO:0000305|PubMed:21252347};
CC -!- SIMILARITY: Belongs to the CoA-transferase III family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAV45684.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY596297; AAV45684.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_049938816.1; NZ_CP039138.1.
DR AlphaFoldDB; Q5V468; -.
DR SMR; Q5V468; -.
DR STRING; 272569.rrnAC0683; -.
DR EnsemblBacteria; AAV45684; AAV45684; rrnAC0683.
DR GeneID; 40151723; -.
DR KEGG; hma:rrnAC0683; -.
DR PATRIC; fig|272569.17.peg.1433; -.
DR eggNOG; arCOG02304; Archaea.
DR HOGENOM; CLU_033975_0_0_2; -.
DR BioCyc; MetaCyc:MON-16256; -.
DR Proteomes; UP000001169; 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 Reference proteome; Transferase.
FT CHAIN 1..396
FT /note="Succinyl-CoA:mesaconate CoA-transferase"
FT /id="PRO_0000429369"
FT ACT_SITE 175
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P69902"
SQ SEQUENCE 396 AA; 42956 MW; E746A1C95A091142 CRC64;
MGALDDLRVL DLTQVLAGPY CTMLLADMGA DVVKVERPGG DLIRSNPPFV SDGDEEAYGG
YFQSVNRGKR SLELNLGTDE DREAFLSLVE RADVVVENFK AGTMEKFDCG YETLREHNPD
LIYSSIRGFG DPRTGETHRQ GQPSFDLIAQ ALGGVMEITG QSDGPPTKVG PGVGDLFTAV
LNAVGILAAV HHRERTGEGQ YVDTAMYDSM VSLCERTVYQ YSCDGESPTR QGNSHPTLFP
YDSFEAADGH VVIAAFADGH WEALCEAMER PDLAAEYPDA GSRIANRESL RAEIAEWTTA
IDSETLLDLL EGRVPAAPVQ NTADIFDDPH IHDREMLAEV DQPGADDQMT IAGSPIKMTE
TMPSPGGRAP LLDEHKTELL DEAGVDTGTN RVESDD
