MASZ_RHOPA
ID MASZ_RHOPA Reviewed; 724 AA.
AC Q6N234;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Malate synthase G {ECO:0000255|HAMAP-Rule:MF_00641};
DE EC=2.3.3.9 {ECO:0000255|HAMAP-Rule:MF_00641};
GN Name=glcB {ECO:0000255|HAMAP-Rule:MF_00641}; OrderedLocusNames=RPA4216;
OS Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=258594;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-98 / CGA009;
RX PubMed=14704707; DOI=10.1038/nbt923;
RA Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA Harrison F.H., Gibson J., Harwood C.S.;
RT "Complete genome sequence of the metabolically versatile photosynthetic
RT bacterium Rhodopseudomonas palustris.";
RL Nat. Biotechnol. 22:55-61(2004).
CC -!- FUNCTION: Involved in the glycolate utilization. Catalyzes the
CC condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-
CC CoA) and glyoxylate to form malate and CoA. {ECO:0000255|HAMAP-
CC Rule:MF_00641}.
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:0000255|HAMAP-
CC Rule:MF_00641};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00641};
CC -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from
CC isocitrate: step 2/2. {ECO:0000255|HAMAP-Rule:MF_00641}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00641}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00641}.
CC -!- SIMILARITY: Belongs to the malate synthase family. GlcB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00641}.
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DR EMBL; BX572606; CAE29657.1; -; Genomic_DNA.
DR RefSeq; WP_011159751.1; NC_005296.1.
DR AlphaFoldDB; Q6N234; -.
DR SMR; Q6N234; -.
DR STRING; 258594.RPA4216; -.
DR PRIDE; Q6N234; -.
DR EnsemblBacteria; CAE29657; CAE29657; RPA4216.
DR GeneID; 66895342; -.
DR KEGG; rpa:RPA4216; -.
DR eggNOG; COG2225; Bacteria.
DR HOGENOM; CLU_028446_1_0_5; -.
DR OMA; MAPGFDG; -.
DR PhylomeDB; Q6N234; -.
DR BioCyc; RPAL258594:TX73_RS21515-MON; -.
DR UniPathway; UPA00703; UER00720.
DR Proteomes; UP000001426; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004474; F:malate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-UniRule.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1220.12; -; 1.
DR Gene3D; 3.20.20.360; -; 2.
DR HAMAP; MF_00641; Malate_synth_G; 1.
DR InterPro; IPR044856; Malate_synth_C_sf.
DR InterPro; IPR011076; Malate_synth_sf.
DR InterPro; IPR001465; Malate_synthase.
DR InterPro; IPR006253; Malate_synthG.
DR InterPro; IPR046363; MS_N_TIM-barrel_dom.
DR PANTHER; PTHR42739; PTHR42739; 1.
DR Pfam; PF01274; Malate_synthase; 1.
DR SUPFAM; SSF51645; SSF51645; 1.
DR TIGRFAMs; TIGR01345; malate_syn_G; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Glyoxylate bypass; Magnesium; Metal-binding; Oxidation;
KW Reference proteome; Transferase; Tricarboxylic acid cycle.
FT CHAIN 1..724
FT /note="Malate synthase G"
FT /id="PRO_1000056924"
FT ACT_SITE 337
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT ACT_SITE 628
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 117
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 124..125
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 273
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 310
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 337
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 429
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 429
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 454..457
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 457
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 538
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT MOD_RES 614
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
SQ SEQUENCE 724 AA; 78627 MW; 66D835480AFC2C43 CRC64;
MNRIDAHGLK IAPVLFDFIA KEAAPKTGIA PDVFWAGLAA IVRDLAPKTR ALLKTRDDLQ
AKIDAWHLAN KGKKQDMAAY TTFLKEIGYL LPEPPTVPVE TTNIDEEIGK LCGPQLVVPL
SNARYALNAA NARWGSLYDA FYGTDAIPQE ATQAKGYDKA RGDKVIAKAK AFLDQAAPLA
TGSHSDVTGY SVIAGQLSAK LKSGNATGLK KPAQFAGFRG DAANPSAVLL VNNGLHIEIK
IDRANTIGKD DPAGVADLVI ESAVSTILDM EDSVAAVDAD DKVLIYRNTL GLMDGTLSES
FEKGGKTVTR ALNGDRTYTA PDGKEISLHG RSLLLMRNVG HHMWTDAVLD SDGQEIPEGF
LDAAVSGLIA IHDLKHLGKT RNSRTGSVYI VKPKMHGPDE VALTVELFGR VETMLGLTAN
TLKVGIMDEE RRTTVNLKAC IQNASKRIVF INTGFLDRTG DEIHTSMEAG PMIRKNEMKA
QPWIKAYEDW NVDTGLVDGL PGHAQIGKGM WAAPDKMADM LAQKIGHPQA GATTAWVPSP
TAATLHALHY HQVDVIARQQ ELAKGGPRAK LEDILTIPVS NSNWAPDDVR QEIDNNCQGI
LGYVVRWIDQ GVGCSKVPDI HDVGLMEDRA TLRISSQHLA NWLHHGVVTK EQVLDSLKRM
AVIVDKQNEG DALYRPMAPD FDGVAFEAAC DLIFKGRAQP NGYTEYILHE RRREAKAAHL
ESAR
