AMASY_HALMA
ID AMASY_HALMA Reviewed; 435 AA.
AC Q5V0X0;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Apparent malate synthase;
DE AltName: Full=(3S)-malyl-CoA thioesterase;
DE EC=3.1.2.30;
DE AltName: Full=(S)-malyl-CoA lyase;
DE EC=4.1.3.24;
GN Name=aceB; OrderedLocusNames=rrnAC1965;
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 biosynthesis of malate in two steps. In the first reaction acetyl-CoA
CC is condensed reversibly with glyoxylate to form (S)-malyl-CoA. In the
CC second reaction (S)-malyl-CoA is hydrolyzed to malate and CoA. It can
CC also catalyzes the condensation of propionyl-CoA with glyoxylate and of
CC acetyl-CoA with pyruvate, however the CoA-ester hydrolysis reaction is
CC highly specific for (S)-malyl-CoA. {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=(S)-malyl-CoA + H2O = (S)-malate + CoA + H(+);
CC Xref=Rhea:RHEA:38291, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15589, ChEBI:CHEBI:57287, ChEBI:CHEBI:57317; EC=3.1.2.30;
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 Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:21252347};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:21252347};
CC Note=Divalent cations. Mg(2+) and to a lesser extent, Mn(2+), Co(2+)
CC and Ca(2+). {ECO:0000269|PubMed:21252347};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.09 mM for (S)-malyl-CoA (cleavage reaction)
CC {ECO:0000269|PubMed:21252347};
CC KM=0.4 mM for acetyl-CoA (condensation reaction with glyoxylate)
CC {ECO:0000269|PubMed:21252347};
CC KM=0.48 mM for glyoxylate (condensation reaction with acetyl-CoA)
CC {ECO:0000269|PubMed:21252347};
CC KM=0.58 mM for (S)-citramalyl-CoA (cleavage reaction)
CC {ECO:0000269|PubMed:21252347};
CC KM=0.78 mM for erythro-beta-methylmalyl-CoA (cleavage reaction)
CC {ECO:0000269|PubMed:21252347};
CC KM=0.8 mM for glyoxylate (condensation reaction with propionyl-CoA)
CC {ECO:0000269|PubMed:21252347};
CC KM=8.9 mM for propionyl-CoA (condensation reaction with glyoxylate)
CC {ECO:0000269|PubMed:21252347};
CC KM=30.2 mM for pyruvate (condensation reaction with acetyl-CoA)
CC {ECO:0000269|PubMed:21252347};
CC Vmax=28.4 umol/min/mg enzyme toward acetyl-CoA (condensation reaction
CC with glyoxylate) {ECO:0000269|PubMed:21252347};
CC Vmax=3 umol/min/mg enzyme toward (S)-citramalyl-CoA (cleavage
CC reaction) {ECO:0000269|PubMed:21252347};
CC Vmax=0.72 umol/min/mg enzyme toward propionyl-CoA (condensation
CC reaction with glyoxylate) {ECO:0000269|PubMed:21252347};
CC Vmax=0.31 umol/min/mg enzyme toward (S)-malyl-CoA (cleavage reaction)
CC {ECO:0000269|PubMed:21252347};
CC Vmax=0.2 umol/min/mg enzyme toward erythro-beta-methylmalyl-CoA (for
CC cleavage reaction) {ECO:0000269|PubMed:21252347};
CC Vmax=0.12 umol/min/mg enzyme toward acetyl-CoA (for condensation
CC reaction with pyruvate) {ECO:0000269|PubMed:21252347};
CC -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family. {ECO:0000305}.
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DR EMBL; AY596297; AAV46833.1; -; Genomic_DNA.
DR RefSeq; WP_011223954.1; NZ_CP039138.1.
DR AlphaFoldDB; Q5V0X0; -.
DR SMR; Q5V0X0; -.
DR STRING; 272569.rrnAC1965; -.
DR EnsemblBacteria; AAV46833; AAV46833; rrnAC1965.
DR GeneID; 40152892; -.
DR KEGG; hma:rrnAC1965; -.
DR PATRIC; fig|272569.17.peg.2622; -.
DR eggNOG; arCOG00760; Archaea.
DR HOGENOM; CLU_629476_0_0_2; -.
DR OMA; DVYENRP; -.
DR BioCyc; MetaCyc:MON-16262; -.
DR SABIO-RK; Q5V0X0; -.
DR Proteomes; UP000001169; Chromosome I.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0043959; F:L-erythro-3-methylmalyl-CoA lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0050083; F:malyl-CoA lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Calcium; Cobalt; Hydrolase; Lyase; Magnesium; Manganese; Metal-binding;
KW Reference proteome.
FT CHAIN 1..435
FT /note="Apparent malate synthase"
FT /id="PRO_0000429372"
FT BINDING 159
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 435 AA; 48112 MW; 5408A301B3A841EB CRC64;
MSVTRHYDRE FVRTFFTSPT AVDGEEDSAK MLRSAGQLRG LQAPDVWVPD NEDATAPNMR
AEGVENIIDV VANQGAEFPG EIHPRVVWHR ESPATRYKGF QQMLEITDPE NGAVEHIDGF
VIPEVGDIDD WKKADEFFTI IEHEHGLEEG SLSMSVIVES GEAELAMGDL REEMGKPSNN
LERMFLLVDG EVDYTKDMRA MTPTGELPPW PELRHNTSRG ASAAGLIAVD GPYDDIRDVE
GYRERMKDNR AKGMTGIWSL TPGQVVEANT APLPPKTGSW LLEAGGQEVE LEAQDGKQVY
DGDDLSLEEV SDGGYVLQAG GDRLELDEDE LTEELLDRTA YIPSMTDIVD SMEEFEAAKE
AGKGAIAMTQ AATLVINGVE VDISKDRMWD EATYQAAQTP ITLFQDVYEH RPDQHEELAE
MYGADIVERA TAVGN
