MCH_HALMA
ID MCH_HALMA Reviewed; 358 AA.
AC Q5V464;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 11-JUN-2014, sequence version 2.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Mesaconyl-CoA hydratase {ECO:0000303|PubMed:21252347};
DE EC=4.2.1.148 {ECO:0000305|PubMed:21252347};
DE AltName: Full=2-methylfumaryl-CoA hydratase;
DE AltName: Full=Beta-methylmalyl-CoA dehydratase;
GN Name=mch {ECO:0000303|PubMed:21252347}; OrderedLocusNames=rrnAC0688;
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
CC reversible hydration of mesaconyl-CoA (2-methylfumaryl-CoA) to yield
CC beta-methylmalyl-CoA ((2R,3S)-beta-methylmalyl-CoA).
CC {ECO:0000269|PubMed:21252347}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3S)-beta-methylmalyl-CoA = 2-methylfumaryl-CoA + H2O;
CC Xref=Rhea:RHEA:38263, ChEBI:CHEBI:15377, ChEBI:CHEBI:75634,
CC ChEBI:CHEBI:75635; EC=4.2.1.148;
CC Evidence={ECO:0000305|PubMed:21252347};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:38265;
CC Evidence={ECO:0000305|PubMed:21252347};
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAV45688.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY596297; AAV45688.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_049938818.1; NZ_CP039138.1.
DR AlphaFoldDB; Q5V464; -.
DR SMR; Q5V464; -.
DR STRING; 272569.rrnAC0688; -.
DR EnsemblBacteria; AAV45688; AAV45688; rrnAC0688.
DR GeneID; 40151727; -.
DR KEGG; hma:rrnAC0688; -.
DR PATRIC; fig|272569.17.peg.1437; -.
DR eggNOG; arCOG00774; Archaea.
DR eggNOG; arCOG00775; Archaea.
DR HOGENOM; CLU_777564_0_0_2; -.
DR BioCyc; MetaCyc:MON-16257; -.
DR Proteomes; UP000001169; Chromosome I.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR045672; MC_hydratase.
DR Pfam; PF19315; MC_hydratase; 1.
DR SUPFAM; SSF54637; SSF54637; 2.
PE 1: Evidence at protein level;
KW Lyase; Reference proteome.
FT CHAIN 1..358
FT /note="Mesaconyl-CoA hydratase"
FT /id="PRO_0000429370"
FT DOMAIN 44..148
FT /note="MaoC-like"
FT /evidence="ECO:0000255"
SQ SEQUENCE 358 AA; 39997 MW; C72E996AF5DE0231 CRC64;
MTDWADPDAL DLSDGETFDS LLDRADTREK GHFFEFFAEG DELAHDPGLR LTHHGSEQWM
GQTLNHDPAY WRADTARERD FEERPVHPDY LLACVMGITV EDLSEKGGYF LGRDDVTFHQ
PVTAGTPLSV TSTVVDTKTS SSRPQYGIVT WETEGRDRET GETLVSYRRT NMIPRREPAA
TDGGAVGEQD EDGPMLPDTP ISPDGEYFED FQAALERADT ENAAVAYRHE RGRTMDDQLV
AGLPLATLNT ARQHHNRDEM ADSPSGDIVA YGDVTRSVAL AHARSDEATY RERRFADEQF
HDFVTLGDTV YGFTRVLDCD PDAGPERAGA VTFEHVAFNQ DQTPVYSGRR TALIQRDT
