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Database: UniProt
Entry: A0A1H4PY27_9PSEU
LinkDB: A0A1H4PY27_9PSEU
Original site: A0A1H4PY27_9PSEU 
ID   A0A1H4PY27_9PSEU        Unreviewed;       525 AA.
AC   A0A1H4PY27;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
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=SAMN04489727_2649 {ECO:0000313|EMBL:SEC12303.1};
OS   Amycolatopsis tolypomycina.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis.
OX   NCBI_TaxID=208445 {ECO:0000313|EMBL:SEC12303.1, ECO:0000313|Proteomes:UP000199622};
RN   [1] {ECO:0000313|EMBL:SEC12303.1, ECO:0000313|Proteomes:UP000199622}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44544 {ECO:0000313|EMBL:SEC12303.1,
RC   ECO:0000313|Proteomes:UP000199622};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FNSO01000004; SEC12303.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H4PY27; -.
DR   STRING; 208445.SAMN04489727_2649; -.
DR   OrthoDB; 9768429at2; -.
DR   UniPathway; UPA00703; UER00720.
DR   Proteomes; UP000199622; 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          4..66
FT                   /note="Malate synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20656"
FT   DOMAIN          157..402
FT                   /note="Malate synthase TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF01274"
FT   DOMAIN          410..524
FT                   /note="Malate synthase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20659"
FT   ACT_SITE        161
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001363-1"
FT   ACT_SITE        444
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001363-1"
SQ   SEQUENCE   525 AA;  57742 MW;  CF057301552AE813 CRC64;
     MSSEVQVLGD PVERGDEILT PEALAFLAGL HDAFAGRRDE LLQARSKRRE EARTTGRLDF
     LPETKEIREG DWQVAGAPAA LRDRRVEITG PTDRKMTINA LNSGAKVWLA DLEDANTPHW
     HNVVSGQVNL YDAIRETITL ESGGKSYALS GDVEHATIVV RPRGWHLPEA HLSFGGREGV
     GALVDFGLHF FHNAAELLKR GKGPYYYLPK MESHLEARLW DDVFTHAEKT LGIEHGTVRA
     TVLIETIPAA FEMEEILYEL REHASGLNAG RWDYLFSVIK YFRDAGEKFV LPDRNSVTMT
     APFMRAYTEL LVRTCHKRGA FAIGGMAAFI PSKDPETNKG AFEKVHADKS REAGDGFDGS
     WVAHPGMVEL CKEEFDKVLG EQPNQLGRTR DEVSVTADQL LDVASTPGSA TAAGLRAAVD
     VGVRYIASWL GGNGAAAIHN LMEDAATAEI SRSQIWQWVK NGTTLDSGDT VTAELVRGVL
     ADVRGELAGE LKPELLEPAV ELFEQVALAE EFPDFLTLPA YEKIK
//
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