MCAL_HALMA
ID MCAL_HALMA Reviewed; 346 AA.
AC Q5V463;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=L-malyl-CoA/beta-methylmalyl-CoA lyase;
DE EC=4.1.3.24;
DE AltName: Full=(3S)-malyl-CoA/beta-methylmalyl-CoA lyase;
GN Name=citE1; OrderedLocusNames=rrnAC0690;
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, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, AND COFACTOR.
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 cleavage of beta-methylmalyl-CoA to propionyl-CoA and
CC glyoxylate, as well as the reversible cleavage of (S)-malyl-CoA to
CC acetyl-CoA and glyoxylate. In addition, it has a small malyl-CoA
CC thioesterase activity. It can also catalyzes the cleavage of (S)-
CC citramalyl-CoA to acetyl-CoA and pyruvate.
CC {ECO:0000269|PubMed:21252347}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malyl-CoA = acetyl-CoA + glyoxylate; Xref=Rhea:RHEA:16629,
CC ChEBI:CHEBI:36655, ChEBI:CHEBI:57288, ChEBI:CHEBI:57317; EC=4.1.3.24;
CC Evidence={ECO:0000269|PubMed:21252347};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3S)-beta-methylmalyl-CoA = glyoxylate + propanoyl-CoA;
CC Xref=Rhea:RHEA:38259, ChEBI:CHEBI:36655, ChEBI:CHEBI:57392,
CC ChEBI:CHEBI:75634; EC=4.1.3.24;
CC Evidence={ECO:0000269|PubMed:21252347};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:21252347};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:21252347};
CC Note=Divalent cations such as magnesium or manganese.
CC {ECO:0000269|PubMed:21252347};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.016 mM for (S)-malyl-CoA (cleavage reaction)
CC {ECO:0000269|PubMed:21252347};
CC KM=0.05 mM for acetyl-CoA (condensation reaction with glyoxylate)
CC {ECO:0000269|PubMed:21252347};
CC KM=0.08 mM for erythro-beta-methylmalyl-CoA (cleavage reaction)
CC {ECO:0000269|PubMed:21252347};
CC KM=0.2 mM for propionyl-CoA (condensation reaction with glyoxylate)
CC {ECO:0000269|PubMed:21252347};
CC KM=1 mM for (S)-citramalyl-CoA (cleavage reaction)
CC {ECO:0000269|PubMed:21252347};
CC KM=17.1 mM for glyoxylate (condensation reaction with propionyl-CoA)
CC {ECO:0000269|PubMed:21252347};
CC KM=26.8 mM for glyoxylate (condensation reaction with acetyl-CoA)
CC {ECO:0000269|PubMed:21252347};
CC Vmax=9.3 umol/min/mg enzyme toward propionyl-CoA (condensation
CC reaction with glyoxylate) {ECO:0000269|PubMed:21252347};
CC Vmax=3.6 umol/min/mg enzyme toward (S)-citramalyl-CoA (cleavage
CC reaction) {ECO:0000269|PubMed:21252347};
CC Vmax=1.9 umol/min/mg enzyme toward acetyl-CoA (condensation reaction
CC with glyoxylate) {ECO:0000269|PubMed:21252347};
CC Vmax=0.3 umol/min/mg enzyme toward erythro-beta-methylmalyl-CoA
CC (cleavage reaction) {ECO:0000269|PubMed:21252347};
CC Vmax=0.07 umol/min/mg enzyme toward (S)-malyl-CoA (cleavage reaction)
CC {ECO:0000269|PubMed:21252347};
CC -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family. {ECO:0000305}.
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DR EMBL; AY596297; AAV45689.1; -; Genomic_DNA.
DR RefSeq; WP_011223176.1; NZ_CP039138.1.
DR AlphaFoldDB; Q5V463; -.
DR SMR; Q5V463; -.
DR STRING; 272569.rrnAC0690; -.
DR DNASU; 3127901; -.
DR EnsemblBacteria; AAV45689; AAV45689; rrnAC0690.
DR GeneID; 40151728; -.
DR KEGG; hma:rrnAC0690; -.
DR PATRIC; fig|272569.17.peg.1438; -.
DR eggNOG; arCOG00760; Archaea.
DR HOGENOM; CLU_800782_0_0_2; -.
DR OMA; FQAPDWL; -.
DR BioCyc; MetaCyc:MON-16252; -.
DR SABIO-RK; Q5V463; -.
DR Proteomes; UP000001169; Chromosome I.
DR GO; GO:0043959; F:L-erythro-3-methylmalyl-CoA lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0050083; F:malyl-CoA lyase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IDA:UniProtKB.
DR Gene3D; 3.20.20.60; -; 1.
DR InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR Pfam; PF03328; HpcH_HpaI; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
PE 1: Evidence at protein level;
KW Lyase; Magnesium; Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..346
FT /note="L-malyl-CoA/beta-methylmalyl-CoA lyase"
FT /id="PRO_0000429371"
FT BINDING 148
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305"
FT BINDING 176..177
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305"
FT BINDING 253..254
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 346 AA; 37951 MW; 91020FABBE519EA8 CRC64;
MTRLCRTFQT APAAIPNDNS AKFLVSGLTS KGFQAPDWLV PDIEDGTAPS MKDEAVDNII
EHIPDHADDF AGDILPRVEW AYDDANARER GIEQVTRLAE AVGEELDGFV FPKVGRLDDV
RDAAGVIADA ERDAGLPEGT LEMAIILETA PGRSDLREIC QYATDSRLSG LVFGPVDYTA
ELGGRTLDGE RPRWDGLLEA LSNETSAADI VAIGGPFDQL FHERAGVTYY NAEGYADQVA
YEATIGIDGS WSLHPKQTEQ ANRIHMPTVE EMERDLHKIE SFNEAKREGT GAVVVDGQMV
DEATYKNFAN TVKTVRAIDE THPAQTEAYY DDDLLARARD VELIFG
