MASZ_AROAE
ID MASZ_AROAE Reviewed; 725 AA.
AC Q5P811;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=AZOSEA04280;
GN ORFNames=ebA819;
OS Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Aromatoleum.
OX NCBI_TaxID=76114;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EbN1;
RX PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA Reinhardt R.;
RT "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT bacterium, strain EbN1.";
RL Arch. Microbiol. 183:27-36(2005).
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; CR555306; CAI06550.1; -; Genomic_DNA.
DR RefSeq; WP_011236283.1; NC_006513.1.
DR AlphaFoldDB; Q5P811; -.
DR SMR; Q5P811; -.
DR STRING; 76114.ebA819; -.
DR PRIDE; Q5P811; -.
DR EnsemblBacteria; CAI06550; CAI06550; ebA819.
DR KEGG; eba:ebA819; -.
DR eggNOG; COG2225; Bacteria.
DR HOGENOM; CLU_028446_1_0_4; -.
DR OMA; MAPGFDG; -.
DR OrthoDB; 322024at2; -.
DR UniPathway; UPA00703; UER00720.
DR Proteomes; UP000006552; 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 CDD; cd00728; malate_synt_G; 1.
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..725
FT /note="Malate synthase G"
FT /id="PRO_1000056892"
FT ACT_SITE 340
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT ACT_SITE 633
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 118
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 125..126
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 276
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 313
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 340
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 619
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
SQ SEQUENCE 725 AA; 78732 MW; 521DE6ACFB25F40E CRC64;
MTERIQCNQL QVDAALHRFI ENEALPGTGL EAAAFWKGFS ELANELAPKN RALLAERDRL
QAEIDTWHRA HPGPIQDMPA YRAFLESIGY LQPVPAPFKI TTANVDSEIS EQAGPQLVVP
IMNARYALNA ANARWGSLYD ALYGTNAIPS DGGAEAGSSY NPVRGARVIA FARNLLDQAA
PLAQGSHDKT KAYAVAGGKL IVTLLDGSQT GLADPAKFAG FQGDAAAPSA VLLKNNGLHL
EIQFDRKHPI GKTDAAGIKD VLVEAAVTTI MDCEDSTAAV DAEDKVVVYR SWLGLITGTL
VETFDKGGKT VERKMNPDRE YTAPNGSALR LHGRSLLFIR HVGHLMTNPA ILLADGAEIP
EGIMDGVVTT LISMRDLKLK RNSRTDSMYI VKPKMHGPAE VAFASELFGR VEQLLGLPAD
TMKVGIMDEE RRTSVNLAGC IKAAESRVAF INTGFLDRTG DEMHTAMEAG PMIRKGDMKG
SAWIQAYERQ NVLVGLDCGL RGRAQIGKGM WAMPDLMAEM LEQKIGHPKA GATTAWVPSP
TGATLHALHY HQVDVQSVQQ EMEKISLAAE RDTLLDNLLT VPVAASANWS ATEIQQELDN
NAQGILGYVV RWIDQGVGCS KVPDINNIGL MEDRATLRIS SQHIANWLRH GVTNEAQVLE
TMKRMAAVVD QQNAGDPLYR PMAPDFDQSV AFQAAKDLVF KGCAQPSGYT EPLLHRWRQV
AKARG
