ID A0A291P2H7_9GAMM Unreviewed; 724 AA.
AC A0A291P2H7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Malate synthase G {ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|RuleBase:RU003572};
DE EC=2.3.3.9 {ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|RuleBase:RU003572};
GN Name=aceB {ECO:0000313|EMBL:ATJ81084.1};
GN Synonyms=glcB {ECO:0000256|HAMAP-Rule:MF_00641};
GN ORFNames=BEI_0097 {ECO:0000313|EMBL:ATJ81084.1};
OS Halomonas beimenensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=475662 {ECO:0000313|EMBL:ATJ81084.1, ECO:0000313|Proteomes:UP000219993};
RN [1] {ECO:0000313|EMBL:ATJ81084.1, ECO:0000313|Proteomes:UP000219993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NTU-111 {ECO:0000313|EMBL:ATJ81084.1,
RC ECO:0000313|Proteomes:UP000219993};
RX PubMed=29026163;
RA Chen Y.H., Lin S.S., Shyu Y.T.;
RT "Revealing the Saline Adaptation Strategies of the Halophilic Bacterium
RT Halomonas beimenensis through High-throughput Omics and Transposon
RT Mutagenesis Approaches.";
RL Sci. Rep. 7:13037-13037(2017).
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:0000256|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;
CC Evidence={ECO:0000256|ARBA:ARBA00001699, ECO:0000256|HAMAP-
CC Rule:MF_00641, ECO:0000256|RuleBase:RU003572};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_00641};
CC -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from
CC isocitrate: step 2/2. {ECO:0000256|HAMAP-Rule:MF_00641,
CC ECO:0000256|RuleBase:RU003572}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00641}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00641,
CC ECO:0000256|RuleBase:RU003572}.
CC -!- SIMILARITY: Belongs to the malate synthase family. GlcB subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|RuleBase:RU003572}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00641}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP021435; ATJ81084.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A291P2H7; -.
DR KEGG; hbe:BEI_0097; -.
DR OrthoDB; 9762054at2; -.
DR UniPathway; UPA00703; UER00720.
DR Proteomes; UP000219993; 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; 3.20.20.360; Malate synthase, domain 3; 2.
DR Gene3D; 1.20.1220.12; Malate synthase, domain III; 1.
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_TIM.
DR InterPro; IPR006253; Malate_synthG.
DR InterPro; IPR048355; MS_C.
DR InterPro; IPR048356; MS_N.
DR InterPro; IPR046363; MS_N_TIM-barrel_dom.
DR InterPro; IPR048357; MSG_insertion.
DR NCBIfam; TIGR01345; malate_syn_G; 1.
DR PANTHER; PTHR42739; MALATE SYNTHASE G; 1.
DR PANTHER; PTHR42739:SF1; MALATE SYNTHASE G; 1.
DR Pfam; PF20659; MS_C; 1.
DR Pfam; PF20656; MS_N; 1.
DR Pfam; PF01274; MS_TIM-barrel; 1.
DR Pfam; PF20658; MSG_insertion; 1.
DR SUPFAM; SSF51645; Malate synthase G; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00641};
KW Glyoxylate bypass {ECO:0000256|ARBA:ARBA00022435, ECO:0000256|HAMAP-
KW Rule:MF_00641};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00641};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00641};
KW Oxidation {ECO:0000256|ARBA:ARBA00023097, ECO:0000256|HAMAP-Rule:MF_00641};
KW Reference proteome {ECO:0000313|Proteomes:UP000219993};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00641};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, ECO:0000256|HAMAP-
KW Rule:MF_00641}.
FT DOMAIN 18..76
FT /note="Malate synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF20656"
FT DOMAIN 160..235
FT /note="Malate synthase G alpha-beta insertion"
FT /evidence="ECO:0000259|Pfam:PF20658"
FT DOMAIN 337..579
FT /note="Malate synthase TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01274"
FT DOMAIN 593..688
FT /note="Malate synthase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF20659"
FT ACT_SITE 340
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641,
FT ECO:0000256|PIRSR:PIRSR601465-50"
FT ACT_SITE 633
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641,
FT ECO:0000256|PIRSR:PIRSR601465-50"
FT BINDING 118
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT BINDING 125..126
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT BINDING 276
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT BINDING 313
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT BINDING 340
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT BINDING 433
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT BINDING 433
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT BINDING 458..461
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT BINDING 461
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT BINDING 542
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT MOD_RES 619
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
SQ SEQUENCE 724 AA; 79046 MW; 82B851465DAA5438 CRC64;
MTQRITRHRL QVAAELDRFI NEQALPGSGV DPDAFWAGVD ALFHDLTPKN RELLAERDAL
QAELDAWHRE NPGPVRDMPA YRAFLERIGY LQEAPAEVKV TTANVDREIA VQAGPQLVVP
VNNARYALNA ANARWGSLYD ALYGTDAISE EGGAEQGDSF NPKRAEKVIA YARGVLDRAA
PLATGSHAEA TRYALRDGHL VVTLAGGRET GLKEPGKLVG YQGETGAPSS VLLANNDLHL
EIQIDAGHPI GKTDAAGVKD VVVEAALTAI MDCEDSVAAV DAEDKVGVYA NWLGLMRGDL
EEQVEKGGKT FTRRLHADRT WTTPDGGELT LPGRSLLFVR NVGHLMTTPA VLDAEGNELP
EGILDGIVTS LIAIRDLQKG AGEARNSRQG SVYIVKPKMH GPKEVAFANE LFGRVEDLLG
LERDTLKMGI MDEERRTSVN LKACINEAPS RVVFINTGFL DRTGDEMHTA MQAGPMIRKG
DMKHSTWIGA YERSNVQVGL ACGLRGHAQI GKGMWAMPDL MAAMLEQKIG HPRAGANTAW
VPSPTAATLH ALHYHQVKVA EVQRELEAQG EPDFLDELLT IPVAEAPDWT DEEIQQELDN
NCQGILGYVV RWVEHGVGCS KVPDIHDVGL MEDRATLRIS SQHVANWLHH GVVEADRVRE
TLERMARVVD EQNAGDPAYR PMSADFAASH AFQAASDLIF KGIEQPSGYT EPLLHHWRAV
HKAS
//
