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Database: UniProt
Entry: A0A1R1M3H5_9MICC
LinkDB: A0A1R1M3H5_9MICC
Original site: A0A1R1M3H5_9MICC 
ID   A0A1R1M3H5_9MICC        Unreviewed;       536 AA.
AC   A0A1R1M3H5;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=malate synthase {ECO:0000256|ARBA:ARBA00012636};
DE            EC=2.3.3.9 {ECO:0000256|ARBA:ARBA00012636};
GN   ORFNames=BGP79_04265 {ECO:0000313|EMBL:OMH34331.1};
OS   Tersicoccus sp. Bi-70.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Tersicoccus.
OX   NCBI_TaxID=1897634 {ECO:0000313|EMBL:OMH34331.1, ECO:0000313|Proteomes:UP000187343};
RN   [1] {ECO:0000313|EMBL:OMH34331.1, ECO:0000313|Proteomes:UP000187343}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bi-70 {ECO:0000313|EMBL:OMH34331.1,
RC   ECO:0000313|Proteomes:UP000187343};
RA   Nakajima Y., Yoshizawa S., Ogura Y., Hayashi T., Kogure K.;
RT   "Draft genome of Tersicoccus sp. strain Bi-70.";
RL   Submitted (AUG-2016) 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   -!- SIMILARITY: Belongs to the malate synthase family.
CC       {ECO:0000256|ARBA:ARBA00006394}.
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:OMH34331.1}.
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DR   EMBL; MIEU01000011; OMH34331.1; -; Genomic_DNA.
DR   RefSeq; WP_076694439.1; NZ_MIEU01000011.1.
DR   AlphaFoldDB; A0A1R1M3H5; -.
DR   STRING; 1897634.BGP79_04265; -.
DR   OrthoDB; 9768429at2; -.
DR   Proteomes; UP000187343; Unassembled WGS sequence.
DR   GO; GO:0004474; F:malate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   CDD; cd00727; malate_synt_A; 1.
DR   Gene3D; 3.20.20.360; Malate synthase, domain 3; 1.
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; IPR006252; Malate_synthA.
DR   InterPro; IPR001465; Malate_synthase_TIM.
DR   InterPro; IPR048355; MS_C.
DR   InterPro; IPR048356; MS_N.
DR   InterPro; IPR046363; MS_N_TIM-barrel_dom.
DR   NCBIfam; TIGR01344; malate_syn_A; 1.
DR   PANTHER; PTHR42902; MALATE SYNTHASE; 1.
DR   PANTHER; PTHR42902:SF1; MALATE SYNTHASE 1-RELATED; 1.
DR   Pfam; PF20659; MS_C; 1.
DR   Pfam; PF20656; MS_N; 1.
DR   Pfam; PF01274; MS_TIM-barrel; 1.
DR   PIRSF; PIRSF001363; Malate_synth; 1.
DR   SUPFAM; SSF51645; Malate synthase G; 1.
PE   3: Inferred from homology;
KW   Glyoxylate bypass {ECO:0000256|ARBA:ARBA00022435};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          11..63
FT                   /note="Malate synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20656"
FT   DOMAIN          158..404
FT                   /note="Malate synthase TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF01274"
FT   DOMAIN          411..530
FT                   /note="Malate synthase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20659"
FT   ACT_SITE        162
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001363-1"
FT   ACT_SITE        446
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001363-1"
SQ   SEQUENCE   536 AA;  59029 MW;  E236E35FFA82A801 CRC64;
     MSIETTDRTP VDRADEILTD EALAFVASLH TRFAARRDEL LGKRVEQQQA VAAAGTITFD
     PATRDVREGD WTVAPVPPAL QDRRVEMTGP ASPAKMAINA LNSGARVWLA DMEDASSPTW
     HNVVDSVLNL RDAARGTLAF TSPEGKTYAL RTDAPLATVV MRPRGWHLDE EHVTIDGRPA
     VGALVDFGLH VFHVAQQLIA NGEGPYYYLP KMESYLEARL WAEVFAAAEE DLGIEHGTIR
     ATMLIETIPA AFQMEEFLHE LRDYAAGLNA GRWDYLFSII KYFRDSGDRF VLADRSKVTM
     TAPLMRAYTE LLVKTCHRRG AHAMGGMAAF IPSRKDEEIN RAAFEKVRSD KTREANDGFD
     GSWVAHPDLV PVCQEVFDGV LGDRPNQVDR LREEVTVTPE QLLDVPSAGA ERTEAELNAN
     LYVAIAYTAV WLSGNGAVAI HNLMEDAATA EISRSQVWQQ IANGVVYTDT GNTATRELVT
     AALDAQKEKL RGEVGEEQYT RFYEPAAAVV ADLVLSEEYA DFLTVPAYDA VVASGR
//
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