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Database: UniProt
Entry: A0A0R0CIP8_9GAMM
LinkDB: A0A0R0CIP8_9GAMM
Original site: A0A0R0CIP8_9GAMM 
ID   A0A0R0CIP8_9GAMM        Unreviewed;       546 AA.
AC   A0A0R0CIP8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=malate synthase {ECO:0000256|ARBA:ARBA00012636};
DE            EC=2.3.3.9 {ECO:0000256|ARBA:ARBA00012636};
GN   ORFNames=ABB26_02700 {ECO:0000313|EMBL:KRG65489.1};
OS   Stenotrophomonas humi.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas.
OX   NCBI_TaxID=405444 {ECO:0000313|EMBL:KRG65489.1, ECO:0000313|Proteomes:UP000050864};
RN   [1] {ECO:0000313|EMBL:KRG65489.1, ECO:0000313|Proteomes:UP000050864}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18929 {ECO:0000313|EMBL:KRG65489.1,
RC   ECO:0000313|Proteomes:UP000050864};
RA   Patil P.P., Midha S., Patil P.B.;
RT   "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL   Submitted (MAY-2015) 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:KRG65489.1}.
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DR   EMBL; LDJI01000006; KRG65489.1; -; Genomic_DNA.
DR   RefSeq; WP_057632045.1; NZ_LDJI01000006.1.
DR   AlphaFoldDB; A0A0R0CIP8; -.
DR   STRING; 405444.ABB26_02700; -.
DR   PATRIC; fig|405444.3.peg.3202; -.
DR   OrthoDB; 9768429at2; -.
DR   Proteomes; UP000050864; 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   Acyltransferase {ECO:0000313|EMBL:KRG65489.1};
KW   Glyoxylate bypass {ECO:0000256|ARBA:ARBA00022435};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KRG65489.1};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          29..78
FT                   /note="Malate synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20656"
FT   DOMAIN          177..421
FT                   /note="Malate synthase TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF01274"
FT   DOMAIN          427..545
FT                   /note="Malate synthase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20659"
FT   ACT_SITE        181
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001363-1"
FT   ACT_SITE        461
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001363-1"
SQ   SEQUENCE   546 AA;  60090 MW;  D397C512365D26B3 CRC64;
     MSAVAQAIPA HTTPRPTPGI TVTTQLAGQS GLLPAGALGL LVSLHRAVEP ERQKRLAARG
     LRQAYFDQGG APDFRTDTRD IREGDWTVAP IPAALQDRRV EITGPTDPKM VINALNSGAK
     VFMADFEDST SPTWRNVLAG QQTMRAAVRG DLDFTSPAAN GKPAKHYTLR PFDEQAVLIV
     RPRGWHLDEK HVLIDGQPIA GGLFDAAVFA FHNARTLMDN DRGPYFYLPK LQSMEEAALW
     ETALSHIEGM LCLPHGQIKV TVLIEALPAV FEMDEILHAL RDRIVGLNCG RWDYIFSYLK
     TFRRHADKVL PERSQVTMTQ PFLKAYSELL IKTCHRRGAH AMGGMAAQIP INHDAAANEQ
     AMARVRADKL REVTAGHDGT WVAHPALIPV ARAIFDEHMP TPNQHQVLRR DVQVSREELI
     APCSGTVTRA GFENNVEVCV RYLAAWLDGN GCVPIHNLME DAATAEISRS QIWQWLHAGN
     QHLDDGTAID LALLESTLRA LPARLGDTTA LPGSGRIPQA IGLLDQLSRA DELADFLTLP
     AYRQID
//
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