ID   B5F9Y7_ALIFM            Unreviewed;       534 AA.
AC   B5F9Y7;
DT   14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2008, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=Malate synthase {ECO:0000256|ARBA:ARBA00012636, ECO:0000256|RuleBase:RU000555};
DE            EC=2.3.3.9 {ECO:0000256|ARBA:ARBA00012636, ECO:0000256|RuleBase:RU000555};
GN   Name=aceB {ECO:0000313|EMBL:ACH67187.1};
GN   OrderedLocusNames=VFMJ11_2107 {ECO:0000313|EMBL:ACH67187.1};
OS   Aliivibrio fischeri (strain MJ11) (Vibrio fischeri).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=388396 {ECO:0000313|EMBL:ACH67187.1, ECO:0000313|Proteomes:UP000001857};
RN   [1] {ECO:0000313|Proteomes:UP000001857}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MJ11 {ECO:0000313|Proteomes:UP000001857};
RA   Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., Kravitz S.,
RA   Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RT   "Complete sequence of Vibrio fischeri strain MJ11.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACH67187.1, ECO:0000313|Proteomes:UP000001857}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MJ11 {ECO:0000313|EMBL:ACH67187.1,
RC   ECO:0000313|Proteomes:UP000001857};
RX   PubMed=19182778; DOI=10.1038/nature07660;
RA   Mandel M.J., Wollenberg M.S., Stabb E.V., Visick K.L., Ruby E.G.;
RT   "A single regulatory gene is sufficient to alter bacterial host range.";
RL   Nature 458:215-218(2009).
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         ECO:0000256|RuleBase:RU000555};
CC   -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from
CC       isocitrate: step 2/2. {ECO:0000256|RuleBase:RU000555}.
CC   -!- SIMILARITY: Belongs to the malate synthase family.
CC       {ECO:0000256|ARBA:ARBA00006394, ECO:0000256|RuleBase:RU000555}.
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DR   EMBL; CP001139; ACH67187.1; -; Genomic_DNA.
DR   RefSeq; WP_012534257.1; NC_011184.1.
DR   AlphaFoldDB; B5F9Y7; -.
DR   GeneID; 77253240; -.
DR   KEGG; vfm:VFMJ11_2107; -.
DR   HOGENOM; CLU_018928_3_0_6; -.
DR   UniPathway; UPA00703; UER00720.
DR   Proteomes; UP000001857; Chromosome I.
DR   GO; GO:0004474; F:malate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-UniPathway.
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; IPR019830; Malate_synthase_CS.
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.
DR   PROSITE; PS00510; MALATE_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000313|EMBL:ACH67187.1};
KW   Glyoxylate bypass {ECO:0000256|ARBA:ARBA00022435,
KW   ECO:0000256|RuleBase:RU000555};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000555};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW   ECO:0000256|RuleBase:RU000555}.
FT   DOMAIN          13..72
FT                   /note="Malate synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20656"
FT   DOMAIN          164..409
FT                   /note="Malate synthase TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF01274"
FT   DOMAIN          414..533
FT                   /note="Malate synthase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20659"
FT   ACT_SITE        168
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001363-1"
FT   ACT_SITE        449
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001363-1"
SQ   SEQUENCE   534 AA;  60671 MW;  640C2DB5A9FB5B93 CRC64;
     MTDTMTIKEQ QITITKPHLP QVEEVLTAGA VRFLTHVVEK FAHRVPELLE TRQLRQKKID
     AGQLPNFLSE TRSIRESEWS IQGIPTDLQD RRVEITGPTD RKMVINALNA NVKVFMADFE
     DSLSPSWEAV LNGQINLRDA MDGTIQYTNP QTQKVYQLKQ DPAVLICRVR GLHLPEKHVL
     FNGVAIPGAL FDFALYFYHN YQTSLKKGSG PYFYLPKLQA YQEAAWWSDV FSFAEREFGL
     KQGTIKATVL IETLPAVFEM DEILYSLKEH IVGLNCGRWD YIFSYIKTLK NHPDRVLPDR
     QVVTMEKPFL NAYSRLLIRT CHRRGAFAMG GMAAFIPSKD PEQNDWVLNK IQTDKSLEAN
     NGHDGTWVAH PGLADTARAE FDSVLGERMN QLDITRDTDA PITAEELLAP CEGERTEEGM
     RHNIRVAVQY IEAWISGNGC VPIYGLMEDA ATAEISRTSI WQWIQHGKTL DSGAVVTAEL
     FRTMLLEEMK VIEKELGTER FDSGQFTQAA KLMEQLTTSD QLTDFLTLPG YQYL
//