ACEB_HALVD
ID ACEB_HALVD Reviewed; 433 AA.
AC D4GTL2; Q977U4;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Malate synthase;
DE Short=MSH;
DE EC=2.3.3.9;
GN Name=aceB; Synonyms=aceB1; OrderedLocusNames=HVO_1983; ORFNames=C498_05196;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11, FUNCTION, AND
RP SUBUNIT.
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=11513957; DOI=10.1016/s0167-4781(01)00263-9;
RA Serrano J.A., Bonete M.J.;
RT "Sequencing, phylogenetic and transcriptional analysis of the glyoxylate
RT bypass operon (ace) in the halophilic archaeon Haloferax volcanii.";
RL Biochim. Biophys. Acta 1520:154-162(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=9738442; DOI=10.1016/s0014-5793(98)00911-9;
RA Serrano J.A., Camacho M., Bonete M.J.;
RT "Operation of glyoxylate cycle in halophilic archaea: presence of malate
RT synthase and isocitrate lyase in Haloferax volcanii.";
RL FEBS Lett. 434:13-16(1998).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH GLYOXYLATE,
RP ACETYL-COA AND MAGNESIUM ION, FUNCTION, ACTIVE SITE, AND SUBUNIT.
RX PubMed=21569248; DOI=10.1186/1472-6807-11-23;
RA Bracken C.D., Neighbor A.M., Lamlenn K.K., Thomas G.C., Schubert H.L.,
RA Whitby F.G., Howard B.R.;
RT "Crystal structures of a halophilic archaeal malate synthase from Haloferax
RT volcanii and comparisons with isoforms A and G.";
RL BMC Struct. Biol. 11:23-23(2011).
CC -!- FUNCTION: Involved in the glyoxylate cycle which synthesizes precursors
CC for carbohydrates from C2 compounds such as acetate. Catalyzes the
CC Claisen condensation between acetyl-coenzyme A (acetyl-CoA) and
CC glyoxylate to form the malyl-CoA intermediate that is subsequently
CC hydrolyzed to produce malate and CoA. {ECO:0000269|PubMed:11513957,
CC ECO:0000269|PubMed:21569248, ECO:0000269|PubMed:9738442}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA + H(+);
CC Xref=Rhea:RHEA:18181, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15589, ChEBI:CHEBI:36655, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288; EC=2.3.3.9; Evidence={ECO:0000269|PubMed:9738442};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:21569248};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.11 uM for glyoxylate (with 0.2 mM acetyl-CoA at pH 8 and 40
CC degrees Celsius) {ECO:0000269|PubMed:9738442};
CC KM=0.119 uM for acetyl-CoA (with 0.5 mM glyoxylate at pH 8 and 40
CC degrees Celsius) {ECO:0000269|PubMed:9738442};
CC Note=AceB requires a high salt concentration for activity, the
CC optimum being around 3.0 M KCl. Replacement of KCl by NaCl causes a
CC decrease in activity (about 2-fold).;
CC pH dependence:
CC Optimum pH is between 8 and 9. {ECO:0000269|PubMed:9738442};
CC Temperature dependence:
CC Optimum temperature is between 45 and 65 degrees Celsius. The
CC activity of the enzyme at 80 degrees Celsius is half of the maximum.
CC {ECO:0000269|PubMed:9738442};
CC -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from
CC isocitrate: step 2/2.
CC -!- SUBUNIT: Homotrimer and homohexamer in equilibrium.
CC {ECO:0000269|PubMed:11513957, ECO:0000269|PubMed:21569248,
CC ECO:0000269|PubMed:9738442}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family. {ECO:0000305}.
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DR EMBL; AJ250923; CAC48389.1; -; Genomic_DNA.
DR EMBL; CP001956; ADE04727.1; -; Genomic_DNA.
DR EMBL; AOHU01000038; ELY34497.1; -; Genomic_DNA.
DR RefSeq; WP_004041864.1; NZ_AOHU01000038.1.
DR PDB; 3OYX; X-ray; 2.51 A; A=1-433.
DR PDB; 3OYZ; X-ray; 1.95 A; A=1-433.
DR PDB; 3PUG; X-ray; 2.70 A; A=1-433.
DR PDB; 5TAO; X-ray; 2.10 A; A=1-433.
DR PDBsum; 3OYX; -.
DR PDBsum; 3OYZ; -.
DR PDBsum; 3PUG; -.
DR PDBsum; 5TAO; -.
DR AlphaFoldDB; D4GTL2; -.
DR SMR; D4GTL2; -.
DR STRING; 309800.C498_05196; -.
DR EnsemblBacteria; ADE04727; ADE04727; HVO_1983.
DR EnsemblBacteria; ELY34497; ELY34497; C498_05196.
DR GeneID; 8925725; -.
DR KEGG; hvo:HVO_1983; -.
DR PATRIC; fig|309800.29.peg.1011; -.
DR eggNOG; arCOG00760; Archaea.
DR HOGENOM; CLU_629476_0_0_2; -.
DR OMA; DVYENRP; -.
DR OrthoDB; 44803at2157; -.
DR BRENDA; 2.3.3.9; 2561.
DR UniPathway; UPA00703; UER00720.
DR Proteomes; UP000008243; Chromosome.
DR Proteomes; UP000011532; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004474; F:malate synthase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IDA:UniProtKB.
DR GO; GO:0006097; P:glyoxylate cycle; IDA:UniProtKB.
DR GO; GO:0006099; P:tricarboxylic acid cycle; 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 3D-structure; Cytoplasm; Direct protein sequencing; Glyoxylate bypass;
KW Magnesium; Metal-binding; Reference proteome; Transferase;
KW Tricarboxylic acid cycle.
FT CHAIN 1..433
FT /note="Malate synthase"
FT /id="PRO_0000429586"
FT ACT_SITE 388
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 16..17
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:21569248"
FT BINDING 52
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:21569248"
FT BINDING 84
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:21569248"
FT BINDING 84
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000269|PubMed:21569248"
FT BINDING 158
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000269|PubMed:21569248"
FT BINDING 158
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:21569248"
FT BINDING 191..192
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000269|PubMed:21569248"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:21569248"
FT BINDING 236
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT BINDING 259
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT CONFLICT 326
FT /note="A -> V (in Ref. 1; CAC48389)"
FT /evidence="ECO:0000305"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:3OYZ"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:3OYX"
FT HELIX 29..36
FT /evidence="ECO:0007829|PDB:3OYZ"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:3OYZ"
FT STRAND 44..51
FT /evidence="ECO:0007829|PDB:3OYZ"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:3OYZ"
FT HELIX 59..73
FT /evidence="ECO:0007829|PDB:3OYZ"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:3OYZ"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:3OYZ"
FT HELIX 92..105
FT /evidence="ECO:0007829|PDB:3OYZ"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:3OYZ"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:3OYZ"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:3OYZ"
FT HELIX 127..143
FT /evidence="ECO:0007829|PDB:3OYZ"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:3OYZ"
FT HELIX 160..165
FT /evidence="ECO:0007829|PDB:3OYZ"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:3OYZ"
FT HELIX 169..174
FT /evidence="ECO:0007829|PDB:3OYZ"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:3OYZ"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:3OYZ"
FT HELIX 190..197
FT /evidence="ECO:0007829|PDB:3OYZ"
FT HELIX 210..223
FT /evidence="ECO:0007829|PDB:3OYZ"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:3OYZ"
FT HELIX 238..249
FT /evidence="ECO:0007829|PDB:3OYZ"
FT TURN 250..252
FT /evidence="ECO:0007829|PDB:3OYZ"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:3OYZ"
FT HELIX 261..269
FT /evidence="ECO:0007829|PDB:3OYZ"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:5TAO"
FT HELIX 329..334
FT /evidence="ECO:0007829|PDB:3OYZ"
FT HELIX 343..358
FT /evidence="ECO:0007829|PDB:3OYZ"
FT STRAND 364..369
FT /evidence="ECO:0007829|PDB:3OYZ"
FT STRAND 382..387
FT /evidence="ECO:0007829|PDB:3OYZ"
FT HELIX 389..395
FT /evidence="ECO:0007829|PDB:3OYZ"
FT HELIX 397..408
FT /evidence="ECO:0007829|PDB:3OYZ"
FT HELIX 410..412
FT /evidence="ECO:0007829|PDB:3OYZ"
FT HELIX 413..420
FT /evidence="ECO:0007829|PDB:3OYZ"
FT HELIX 422..428
FT /evidence="ECO:0007829|PDB:3OYZ"
SQ SEQUENCE 433 AA; 48018 MW; 67AAD93EF9E576D9 CRC64;
MTERRHDREF VRTFFTSPTA VEGEDDSAKM LRRAAGLRGM QAPDVWVPDN EDATAPSMRD
EGAENIVEVI SEQGAEFPGE IHPRMVWHRD SPETRYQGFQ HMLDITDPER GAVEHIHGFV
IPEVGGIDDW KKADEFFTIV EHEHGLDEGS LAMSVIIESG EAELAMGDLR DEMGKPTNNL
ERLFLLVDGE VDYTKDMRAM TPTGELPAWP ELRHNTSRGA SAAGCVAVDG PYDDIRDVEG
YRERMTDNQA KGMLGIWSLT PGQVVEANTS PLPPKTGSWL LDADGEEVEL ASEDGVEAYD
GDRLSLEATD GGYELRVGGD ARELTADELR EELLGLTSYV PSMDDIVDSM EEFEAAKEAG
RGAIAMTQSA TLRIGGTEID IEKDRMWDEA TYQAAMTPIS LFQDVYENRP DQHEELEERY
GAGVVERAME VGL
