ID A0A0Q8C606_9MICO Unreviewed; 536 AA.
AC A0A0Q8C606;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=ASD61_15050 {ECO:0000313|EMBL:KRA09479.1};
OS Leifsonia sp. Root60.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leifsonia.
OX NCBI_TaxID=1736567 {ECO:0000313|EMBL:KRA09479.1, ECO:0000313|Proteomes:UP000051073};
RN [1] {ECO:0000313|EMBL:KRA09479.1, ECO:0000313|Proteomes:UP000051073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root60 {ECO:0000313|EMBL:KRA09479.1,
RC ECO:0000313|Proteomes:UP000051073};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRA09479.1, ECO:0000313|Proteomes:UP000051073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root60 {ECO:0000313|EMBL:KRA09479.1,
RC ECO:0000313|Proteomes:UP000051073};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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 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}.
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:KRA09479.1}.
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DR EMBL; LMGR01000002; KRA09479.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q8C606; -.
DR STRING; 1736567.ASD61_15050; -.
DR UniPathway; UPA00703; UER00720.
DR Proteomes; UP000051073; 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 Reference proteome {ECO:0000313|Proteomes:UP000051073};
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 2..61
FT /note="Malate synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF20656"
FT DOMAIN 163..415
FT /note="Malate synthase TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01274"
FT DOMAIN 423..534
FT /note="Malate synthase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF20659"
FT ACT_SITE 167
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001363-1"
FT ACT_SITE 456
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001363-1"
SQ SEQUENCE 536 AA; 60164 MW; C3ABEBC344615D70 CRC64;
MEVTAPLGDR YSEILTPEAL AFLAELHDRF AGIRHDLLAA RLQTRVASAN GRDPRFLPET
APVRADATWR VAGAGPGLED RRVEITGPTD RKMAINALNS GAKVWLADLE DATSPTWTNV
IEGQLSLLDA LRGTLAYTSD DGREYTVAGR IGLTHGGEAE TPTIVMRPRG WHLVEKHLRF
HDRSGRAMNA SGSLVDFGLY FFHNAHRLIE LGLGPYFYLP KLESHREARL WNDVFTFSQD
HLGIPRGTVR ATVLIETIQA AFEMEEILYE LRDHCAGLNA GRWDYIFSII KTFRSRGRRW
VFPDRSEITM TVPFMRAYTE LLVATCHRRG AYAIGGMSAF IPNRRDPEVT ARALEKVSTD
KRREAADGFD GTWVAHPDLI PTARAEFDAV FGDRSNQLHR LRDDVDVTAA ELLDIPSIGG
TVSEEGVRDN VRIAVRYIES WLRGTGAAAI DNLMEDAATA EISRSQIWQW VNENTVTREG
RRIDAAWLET VVAAVAEELP RSRDDRFDDA FAVFRQVALE PEFPTFLTIP AYTRFL
//