ID   A0A2A4S634_9CHLR        Unreviewed;       757 AA.
AC   A0A2A4S634;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Malate synthase G {ECO:0000313|EMBL:PCI16840.1};
GN   ORFNames=COB68_10860 {ECO:0000313|EMBL:PCI16840.1};
OS   SAR202 cluster bacterium.
OC   Bacteria; Chloroflexota; SAR202 cluster.
OX   NCBI_TaxID=2030829 {ECO:0000313|EMBL:PCI16840.1, ECO:0000313|Proteomes:UP000217661};
RN   [1] {ECO:0000313|Proteomes:UP000217661}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT   "A dynamic microbial community with high functional redundancy inhabits the
RT   cold, oxic subseafloor aquifer.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PCI16840.1}.
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; NVSQ01000037; PCI16840.1; -; Genomic_DNA.
DR   Proteomes; UP000217661; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0004474; F:malate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.360; Malate synthase, domain 3; 2.
DR   Gene3D; 1.20.1220.12; Malate synthase, domain III; 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   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   SUPFAM; SSF51645; Malate synthase G; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Glyoxylate bypass {ECO:0000256|ARBA:ARBA00022435};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidation {ECO:0000256|ARBA:ARBA00023097};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          37..71
FT                   /note="Malate synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20656"
FT   DOMAIN          349..603
FT                   /note="Malate synthase TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF01274"
FT   DOMAIN          628..700
FT                   /note="Malate synthase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20659"
FT   ACT_SITE        352
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601465-50"
FT   ACT_SITE        658
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601465-50"
SQ   SEQUENCE   757 AA;  83333 MW;  A495391FAD37CDE9 CRC64;
     MLMATITLAY GARLEIADVL YEFVRDEAVN GTAWTADQLF EVLGELVQEF GPRNQELLAK
     RISRQEQIDH YYISKRNGGW EPTQASAGQD AADFEQFLVD IGYLEPESST EFSMTTPQLD
     ADMDQNGPEL VTPVNNASMA VGGANARWGS LYDAYFLSDI HPEVGREESR TARLRMVVEE
     TTEFLDAHVA QWTNGXGFKD IVSYSVXLNP QGTYEXXGHT GEGXEVGLDN TAVFVGFNKD
     GENLTDFFLE DNGLKLQFQL YGGGRVNEEN GQFRDLFVES AITNIVDFED AVAIVDADDT
     VSALRNYLGL IKGDLRAYGS RGNLKTMNSD ITSLDVNGSS QAFKGTSLMS VRNVSLHMYT
     PMVTVDGQQI PERILGVLLT TFIAASHDKG SSGEVAEADG GPIPIRGPNS KKGYIYQVTP
     KLQSSEEVAE QVRFFEAIEN KLGLANNSIL IGIMNEELGM TLQLAQALRA AQSRTFFTNT
     GFLDRTGSQI RTQTQAGPVD LRDDLTQELF NTSYELHNVD VSIHAGVHRH GKIGKGMQVR
     NRAMAEMMER KIAHPRTGGN TAWVPAPYPS DLHSMHYHMV DVDQVQRVME DSPSPGIMRR
     ELLTFPVLDS GKLAEPGVKQ SLLLGYTHSM VAYVEPWVHR GIGCSGVPNF DQIEEMKDRA
     TERIDGAIIA NWKLHGVVDQ QEIEDAVRKA AEVVDQQNAK QPGYVPMXDT XXKRDALLEE
     PAIAAVLQII DDALSSPSAY VEPALFRNRM AVKGGGG
//