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Database: UniProt
Entry: A0A2G0QGT1_9GAMM
LinkDB: A0A2G0QGT1_9GAMM
Original site: A0A2G0QGT1_9GAMM 
ID   A0A2G0QGT1_9GAMM        Unreviewed;       537 AA.
AC   A0A2G0QGT1;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, 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=Xhom_01395 {ECO:0000313|EMBL:PHM58369.1};
OS   Xenorhabdus hominickii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=351679 {ECO:0000313|EMBL:PHM58369.1, ECO:0000313|Proteomes:UP000225433};
RN   [1] {ECO:0000313|EMBL:PHM58369.1, ECO:0000313|Proteomes:UP000225433}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17903 {ECO:0000313|EMBL:PHM58369.1,
RC   ECO:0000313|Proteomes:UP000225433};
RX   PubMed=28993611; DOI=10.1038/s41564-017-0039-9;
RA   Tobias N.J., Wolff H., Djahanschiri B., Grundmann F., Kronenwerth M.,
RA   Shi Y.M., Simonyi S., Grun P., Shapiro-Ilan D., Pidot S.J., Stinear T.P.,
RA   Ebersberger I., Bode H.B.;
RT   "Natural product diversity associated with the nematode symbionts
RT   Photorhabdus and Xenorhabdus.";
RL   Nat. Microbiol. 2:1676-1685(2017).
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:PHM58369.1}.
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DR   EMBL; NJAI01000001; PHM58369.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G0QGT1; -.
DR   STRING; 351679.A9255_18445; -.
DR   Proteomes; UP000225433; 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          15..74
FT                   /note="Malate synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20656"
FT   DOMAIN          166..411
FT                   /note="Malate synthase TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF01274"
FT   DOMAIN          416..535
FT                   /note="Malate synthase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20659"
FT   ACT_SITE        170
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001363-1"
FT   ACT_SITE        451
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001363-1"
SQ   SEQUENCE   537 AA;  61398 MW;  CA219625A98B0395 CRC64;
     MRKGGIMQQE LTTDLTFIKP FDEADRKVLS PESIDFLKDL IVKFSDRRKK LLEERTHWQK
     KIDDGVLPDF ISETISIRGG DWKIQGIPED LRDRRVEITG PVERKMVINA LNANVKVFMA
     DFEDSLAPSW DKVINGQINL QDAVNGTISY TSEQGKRYEL KSDPAVLIAR VRGFHLSEKH
     VLYKNEPISG GLFDFALYFH LNYKKLLEQG SGPYFYLPKI QSYHEAQWWS DVFSFAESRF
     NLPKGTIKAT VLIETLPAVF QMDEILYHLR HHIVGLNCGR WDYIFSYIKT LKNHSDRVLP
     DRQSVTMTQP FLSAYSRLLI KTCHKRGAFA MGGMSAFIPS KDLEQNQQVS NKVRADKELE
     ANNGHDGTWV AHPGLADIAM AVFDKKLGER QNQLTVSREE DETITAAQLL SPCPGERTEE
     GMRANIRVAV QYIEAWISGN GCVPIYGLME DAATAEISRT SIWQWIRHEK SLSNGKKVTK
     ELFKEMLKEE LNVIKQEVGE QHFNQGRFTD ASALMERITT QDDLIDFLTL PGYQLLD
//
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