ID   A5FXX2_ACICJ            Unreviewed;       722 AA.
AC   A5FXX2;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   04-NOV-2026, entry version 122.
DE   RecName: Full=Malate synthase G {ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|NCBIfam:TIGR01345};
DE            EC=2.3.3.9 {ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|NCBIfam:TIGR01345};
GN   Name=glcB {ECO:0000256|HAMAP-Rule:MF_00641};
GN   OrderedLocusNames=Acry_1243 {ECO:0000313|EMBL:ABQ30454.1};
OS   Acidiphilium cryptum (strain JF-5).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Acetobacterales; Acidocellaceae; Acidiphilium.
OX   NCBI_TaxID=349163 {ECO:0000313|EMBL:ABQ30454.1, ECO:0000313|Proteomes:UP000000245};
RN   [1] {ECO:0000313|EMBL:ABQ30454.1, ECO:0000313|Proteomes:UP000000245}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JF-5 {ECO:0000313|EMBL:ABQ30454.1,
RC   ECO:0000313|Proteomes:UP000000245};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.;
RT   "Complete sequence of chromosome of Acidiphilium cryptum JF-5.";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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=glyoxylate + acetyl-CoA + 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: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, ECO:0000256|HAMAP-
CC         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}.
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DR   EMBL; CP000697; ABQ30454.1; -; Genomic_DNA.
DR   RefSeq; WP_011942095.1; NC_009484.1.
DR   AlphaFoldDB; A5FXX2; -.
DR   STRING; 349163.Acry_1243; -.
DR   KEGG; acr:Acry_1243; -.
DR   eggNOG; COG2225; Bacteria.
DR   HOGENOM; CLU_028446_1_0_5; -.
DR   OMA; AANARWM; -.
DR   UniPathway; UPA00703; UER00720.
DR   Proteomes; UP000000245; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:TreeGrafter.
DR   GO; GO:0004474; F:malate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009436; P:glyoxylate catabolic process; IEA:TreeGrafter.
DR   GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-UniRule.
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   NCBIfam; NF002825; PRK02999.1; 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   Acyltransferase {ECO:0000313|EMBL:ABQ30454.1};
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:UP000000245};
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..72
FT                   /note="Malate synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20656"
FT   DOMAIN          161..235
FT                   /note="Malate synthase G alpha-beta insertion"
FT                   /evidence="ECO:0000259|Pfam:PF20658"
FT   DOMAIN          337..570
FT                   /note="Malate synthase TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF01274"
FT   DOMAIN          591..710
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        631
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00641,
FT                   ECO:0000256|PIRSR:PIRSR601465-50"
FT   BINDING         119
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT   BINDING         126..127
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         432
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT   BINDING         432
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT   BINDING         457..460
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT   BINDING         460
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT   BINDING         541
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT   MOD_RES         617
FT                   /note="Cysteine sulfenic acid (-SOH)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
SQ   SEQUENCE   722 AA;  78017 MW;  F517E5EC117F2490 CRC64;
     MSQTYVDAAG LRVAAELHQF IETEALPGTG VESGAFWQGF AGLIARHAPR NAELLAERDR
     LQAAIDDWHR SRRGQPVDPA AYEAFLREIG YLRPEPGDVK VTSERVDPEI AAIAGPQLVV
     PVMNARYALN AANARWGSLY DALYGTDAIP ESGGLERGKA YNPQRGAAVV ARGRAFLDDH
     FPLATGSHAD VRAWRVHNGH LAAVLESGET GLKHAAQFAG YRGEPAAPTA VLLRHHNLHV
     EIAIDPTSPI GRTDKAGVAD LIVESAISTI MDAEDSVAAV DAEDKVLVYR NWLGLMAGTL
     SEQVEKGGKT FTRALNPDRA YTAPDGSTLT LPGRVLMLVR NVGHHIYTDT VLDAAGKPIP
     ETILDLVVTS LCGLHDIRRT AGLRNSRAGS VYIVKPKMHG ADEVAYANGL FAATESLLGL
     APDTLKMGIM DEERRTSANL KACIAAAASR IFFINTGFLD RTGDEIHTSI EAGPMIRKNE
     IRNTPWIKAY EDRNVDIGIV CGLPGHAQIG KGMWAAPDAM AAMLEQKVGH PRAGANTAWV
     PSPTAATLHA LHYHMVDVAA RQAELAARPM GSLADLLTIP LADRPNWRPE DIQQELDNNA
     QGILGYVVRW IDQGIGCSKV PDIHNVALME DRATLRISAQ HIANWLHHGI VSEAQVMETM
     KRMAAVVDGQ NAGDPAYRNM APGFDGVAFQ AACDLVFKGR TQPNGYTEFI LHDRRREAKA
     SA
//