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Database: UniProt
Entry: A0A158ISE2_9BURK
LinkDB: A0A158ISE2_9BURK
Original site: A0A158ISE2_9BURK 
ID   A0A158ISE2_9BURK        Unreviewed;       531 AA.
AC   A0A158ISE2;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
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   ORFNames=AWB69_06588 {ECO:0000313|EMBL:SAL59564.1};
OS   Caballeronia udeis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=1232866 {ECO:0000313|EMBL:SAL59564.1, ECO:0000313|Proteomes:UP000054683};
RN   [1] {ECO:0000313|EMBL:SAL59564.1, ECO:0000313|Proteomes:UP000054683}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 27134 {ECO:0000313|EMBL:SAL59564.1};
RA   Oliw E.H.;
RL   Submitted (JAN-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         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; FCOK02000060; SAL59564.1; -; Genomic_DNA.
DR   RefSeq; WP_062090846.1; NZ_FCOK02000060.1.
DR   AlphaFoldDB; A0A158ISE2; -.
DR   OrthoDB; 9768429at2; -.
DR   UniPathway; UPA00703; UER00720.
DR   Proteomes; UP000054683; Unassembled WGS sequence.
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   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          11..72
FT                   /note="Malate synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20656"
FT   DOMAIN          162..407
FT                   /note="Malate synthase TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF01274"
FT   DOMAIN          414..531
FT                   /note="Malate synthase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20659"
FT   ACT_SITE        166
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001363-1"
FT   ACT_SITE        448
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001363-1"
SQ   SEQUENCE   531 AA;  59100 MW;  3861CFF23DF9EB19 CRC64;
     MANTLTHVPQ GMTITAEIKP GYETILTPEA LELVATLHRA FEPRRQALLK ARAERTKRLD
     AGERPDFLSE TQSIRDADWT IAPLPKALEC RRVEITGPVE RKMIINALNS GADAYMTDFE
     DSNTPNWDNQ LTGHINLKEA VRGTISLEQN GKSYKLNDKT ATLIVRPRGW HLDEKHVTVD
     GQRVSGGIFD FALFLFHNAK EQLARGAGPY FYLPKLESHL EARLWNEIFV AAQEIVGVPR
     GSIRATVLIE TILAAFEMDE ILYELREHSS GLNAGRWDYI FSAIKKFKND ANFCLADRAK
     ITMTVPFMRA YALQLLKTCH RRQAPAIGGM SALIPIKNDP QANDKAMGGV RSDKARDAGD
     GYDGGWVAHP GLVPIAMEEF VKVLGDKPNQ IAKQREDVQV TAADLLDFRP EDPITEGGVR
     GNINVGIHYL GSWLAGNGCV PIHNLMEDAA TAEISRSQVW QWIRSPKGKL DDGRKVTAEM
     VRAFTQEELV KVKEVVSGDT APYDRAATIF EAMSTSDTFA EFLTLPLYEE I
//
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