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Malate synthase (MSH) (EC 2.3.3.9)

 ACEB_HALVD              Reviewed;         433 AA.
D4GTL2; Q977U4;
09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 1.
07-JUN-2017, entry version 45.
RecName: Full=Malate synthase;
Short=MSH;
EC=2.3.3.9;
Name=aceB; Synonyms=aceB1; OrderedLocusNames=HVO_1983;
ORFNames=C498_05196;
Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC
14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
Archaea; Euryarchaeota; Halobacteria; Haloferacales; Haloferacaceae;
Haloferax.
NCBI_TaxID=309800;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11, FUNCTION,
AND SUBUNIT.
STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 /
VKM B-1768 / DS2;
PubMed=11513957; DOI=10.1016/S0167-4781(01)00263-9;
Serrano J.A., Bonete M.J.;
"Sequencing, phylogenetic and transcriptional analysis of the
glyoxylate bypass operon (ace) in the halophilic archaeon Haloferax
volcanii.";
Biochim. Biophys. Acta 1520:154-162(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 /
VKM B-1768 / DS2;
PubMed=20333302; DOI=10.1371/journal.pone.0009605;
Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S.,
Madupu R., Robinson J., Khouri H., Ren Q., Lowe T.M.,
Maupin-Furlow J., Pohlschroder M., Daniels C., Pfeiffer F., Allers T.,
Eisen J.A.;
"The complete genome sequence of Haloferax volcanii DS2, a model
archaeon.";
PLoS ONE 5:E9605-E9605(2010).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 /
VKM B-1768 / DS2;
Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D.,
Darling A., Eisen J.A., Facciotti M.T.;
Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
[4]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
SUBUNIT.
STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 /
VKM B-1768 / DS2;
PubMed=9738442; DOI=10.1016/S0014-5793(98)00911-9;
Serrano J.A., Camacho M., Bonete M.J.;
"Operation of glyoxylate cycle in halophilic archaea: presence of
malate synthase and isocitrate lyase in Haloferax volcanii.";
FEBS Lett. 434:13-16(1998).
[5]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH GLYOXYLATE,
ACETYL-COA AND MAGNESIUM ION, FUNCTION, ACTIVE SITE, AND SUBUNIT.
PubMed=21569248; DOI=10.1186/1472-6807-11-23;
Bracken C.D., Neighbor A.M., Lamlenn K.K., Thomas G.C., Schubert H.L.,
Whitby F.G., Howard B.R.;
"Crystal structures of a halophilic archaeal malate synthase from
Haloferax volcanii and comparisons with isoforms A and G.";
BMC Struct. Biol. 11:23-23(2011).
-!- FUNCTION: Involved in the glyoxylate cycle which synthesizes
precursors for carbohydrates from C2 compounds such as acetate.
Catalyzes the Claisen condensation between acetyl-coenzyme A
(acetyl-CoA) and glyoxylate to form the malyl-CoA intermediate
that is subsequently hydrolyzed to produce malate and CoA.
{ECO:0000269|PubMed:11513957, ECO:0000269|PubMed:21569248,
ECO:0000269|PubMed:9738442}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + H(2)O + glyoxylate = (S)-malate +
CoA. {ECO:0000269|PubMed:9738442}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:21569248};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.11 uM for glyoxylate (with 0.2 mM acetyl-CoA at pH 8 and 40
degrees Celsius) {ECO:0000269|PubMed:9738442};
KM=0.119 uM for acetyl-CoA (with 0.5 mM glyoxylate at pH 8 and
40 degrees Celsius) {ECO:0000269|PubMed:9738442};
Note=AceB requires a high salt concentration for activity, the
optimum being around 3.0 M KCl. Replacement of KCl by NaCl
causes a decrease in activity (about 2-fold).;
pH dependence:
Optimum pH is between 8 and 9. {ECO:0000269|PubMed:9738442};
Temperature dependence:
Optimum temperature is between 45 and 65 degrees Celsius. The
activity of the enzyme at 80 degrees Celsius is half of the
maximum. {ECO:0000269|PubMed:9738442};
-!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate
from isocitrate: step 2/2.
-!- SUBUNIT: Homotrimer and homohexamer in equilibrium.
{ECO:0000269|PubMed:11513957, ECO:0000269|PubMed:21569248,
ECO:0000269|PubMed:9738442}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AJ250923; CAC48389.1; -; Genomic_DNA.
EMBL; CP001956; ADE04727.1; -; Genomic_DNA.
EMBL; AOHU01000038; ELY34497.1; -; Genomic_DNA.
RefSeq; WP_004041864.1; NZ_AOHU01000038.1.
PDB; 3OYX; X-ray; 2.51 A; A=1-433.
PDB; 3OYZ; X-ray; 1.95 A; A=1-433.
PDB; 3PUG; X-ray; 2.70 A; A=1-433.
PDB; 5TAO; X-ray; 2.10 A; A=1-433.
PDBsum; 3OYX; -.
PDBsum; 3OYZ; -.
PDBsum; 3PUG; -.
PDBsum; 5TAO; -.
ProteinModelPortal; D4GTL2; -.
SMR; D4GTL2; -.
STRING; 309800.HVO_1983; -.
EnsemblBacteria; ADE04727; ADE04727; HVO_1983.
EnsemblBacteria; ELY34497; ELY34497; C498_05196.
GeneID; 8925725; -.
KEGG; hvo:HVO_1983; -.
PATRIC; fig|309800.29.peg.1011; -.
eggNOG; arCOG00760; Archaea.
eggNOG; COG2301; LUCA.
HOGENOM; HOG000094928; -.
KO; K19282; -.
OMA; DSAKMLR; -.
OrthoDB; POG093Z038G; -.
BRENDA; 2.3.3.9; 2561.
UniPathway; UPA00703; UER00720.
Proteomes; UP000008243; Chromosome.
Proteomes; UP000011532; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004474; F:malate synthase activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IDA:UniProtKB.
GO; GO:0006097; P:glyoxylate cycle; IDA:UniProtKB.
GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
InterPro; IPR005000; Aldolase/citrate-lyase_domain.
InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
Pfam; PF03328; HpcH_HpaI; 1.
SUPFAM; SSF51621; SSF51621; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
Glyoxylate bypass; Magnesium; Metal-binding; Reference proteome;
Transferase; Tricarboxylic acid cycle.
CHAIN 1 433 Malate synthase.
/FTId=PRO_0000429586.
REGION 16 17 Acetyl-CoA binding.
{ECO:0000269|PubMed:21569248}.
REGION 191 192 Glyoxylate binding.
{ECO:0000269|PubMed:21569248}.
ACT_SITE 388 388 Proton acceptor. {ECO:0000255}.
METAL 52 52 Magnesium. {ECO:0000269|PubMed:21569248}.
METAL 158 158 Magnesium. {ECO:0000269|PubMed:21569248}.
METAL 192 192 Magnesium. {ECO:0000269|PubMed:21569248}.
BINDING 84 84 Acetyl-CoA.
{ECO:0000269|PubMed:21569248}.
BINDING 84 84 Glyoxylate.
{ECO:0000269|PubMed:21569248}.
BINDING 158 158 Glyoxylate.
{ECO:0000269|PubMed:21569248}.
BINDING 236 236 Acetyl-CoA.
BINDING 259 259 Acetyl-CoA; via carbonyl oxygen.
CONFLICT 326 326 A -> V (in Ref. 1; CAC48389).
{ECO:0000305}.
STRAND 13 19 {ECO:0000244|PDB:3OYZ}.
STRAND 23 25 {ECO:0000244|PDB:3OYX}.
HELIX 29 36 {ECO:0000244|PDB:3OYZ}.
HELIX 39 41 {ECO:0000244|PDB:3OYZ}.
STRAND 44 51 {ECO:0000244|PDB:3OYZ}.
HELIX 56 58 {ECO:0000244|PDB:3OYZ}.
HELIX 59 73 {ECO:0000244|PDB:3OYZ}.
HELIX 74 76 {ECO:0000244|PDB:3OYZ}.
STRAND 78 81 {ECO:0000244|PDB:3OYZ}.
HELIX 92 105 {ECO:0000244|PDB:3OYZ}.
HELIX 108 110 {ECO:0000244|PDB:3OYZ}.
HELIX 113 115 {ECO:0000244|PDB:3OYZ}.
STRAND 118 121 {ECO:0000244|PDB:3OYZ}.
HELIX 127 143 {ECO:0000244|PDB:3OYZ}.
STRAND 151 157 {ECO:0000244|PDB:3OYZ}.
HELIX 160 165 {ECO:0000244|PDB:3OYZ}.
HELIX 166 168 {ECO:0000244|PDB:3OYZ}.
HELIX 169 174 {ECO:0000244|PDB:3OYZ}.
HELIX 180 182 {ECO:0000244|PDB:3OYZ}.
STRAND 183 188 {ECO:0000244|PDB:3OYZ}.
HELIX 190 197 {ECO:0000244|PDB:3OYZ}.
HELIX 210 223 {ECO:0000244|PDB:3OYZ}.
STRAND 226 229 {ECO:0000244|PDB:3OYZ}.
HELIX 238 249 {ECO:0000244|PDB:3OYZ}.
TURN 250 252 {ECO:0000244|PDB:3OYZ}.
STRAND 255 258 {ECO:0000244|PDB:3OYZ}.
HELIX 261 269 {ECO:0000244|PDB:3OYZ}.
STRAND 326 328 {ECO:0000244|PDB:5TAO}.
HELIX 329 334 {ECO:0000244|PDB:3OYZ}.
HELIX 343 358 {ECO:0000244|PDB:3OYZ}.
STRAND 364 369 {ECO:0000244|PDB:3OYZ}.
STRAND 382 387 {ECO:0000244|PDB:3OYZ}.
HELIX 389 395 {ECO:0000244|PDB:3OYZ}.
HELIX 397 408 {ECO:0000244|PDB:3OYZ}.
HELIX 410 412 {ECO:0000244|PDB:3OYZ}.
HELIX 413 420 {ECO:0000244|PDB:3OYZ}.
HELIX 422 428 {ECO:0000244|PDB:3OYZ}.
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


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