ID A0A1C7NRE4_9FUNG Unreviewed; 553 AA.
AC A0A1C7NRE4;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-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 Name=acu-9 {ECO:0000313|EMBL:OBZ91530.1};
GN ORFNames=A0J61_00421 {ECO:0000313|EMBL:OBZ91530.1};
OS Choanephora cucurbitarum.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Choanephoraceae; Choanephoroideae;
OC Choanephora.
OX NCBI_TaxID=101091 {ECO:0000313|EMBL:OBZ91530.1, ECO:0000313|Proteomes:UP000093000};
RN [1] {ECO:0000313|EMBL:OBZ91530.1, ECO:0000313|Proteomes:UP000093000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KUS-F28377 {ECO:0000313|EMBL:OBZ91530.1,
RC ECO:0000313|Proteomes:UP000093000};
RA Min B., Park H., Park J.-H., Shin H.-D., Choi I.-G.;
RT "Choanephora cucurbitarum.";
RL Submitted (MAR-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}.
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:OBZ91530.1}.
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DR EMBL; LUGH01000009; OBZ91530.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C7NRE4; -.
DR STRING; 101091.A0A1C7NRE4; -.
DR InParanoid; A0A1C7NRE4; -.
DR OrthoDB; 177378at2759; -.
DR UniPathway; UPA00703; UER00720.
DR Proteomes; UP000093000; 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:UP000093000};
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 19..81
FT /note="Malate synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF20656"
FT DOMAIN 174..419
FT /note="Malate synthase TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01274"
FT DOMAIN 425..544
FT /note="Malate synthase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF20659"
FT ACT_SITE 178
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001363-1"
FT ACT_SITE 459
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001363-1"
SQ SEQUENCE 553 AA; 62588 MW; F77E99F71D9A7B81 CRC64;
MSAVTSRSSA KLIKTSVPGV AVLAPVTASE ADILSPQALQ FVATLQRIFN PTRKTLMQKR
ALRQQELDRG VLPNFLPETA YIRDDPNWRA APPAPGLQDR RVEITGPVDR KMVINALNSG
AFTFMADFED STSPTWENII SGQVNLRDAV RESIEFTNPN GKKYALRKDG KIATLLVRPR
GWHMVEKHVL VDGEPCSASI FDFALYFFHN AKELVKRGKG PYFYLPKMES HLEARLWNDI
FNVAQDMINI PRGTIRGTVL IETLLAAYEM DEIIYELRDH SSGLNCGRWD YIFSFIKKLR
NHPQFVLPQR SQVTMTVPFM DAYVRLLIQT CHKRGVHAMG GMAAQIPIKN NPEANEAAMA
KVRSDKLREV TAGHDGTWVA HPDLVKIALD IFNEHMPQPN QLHIRRDDVK VTATDLIDIN
FKGTITEDSI RENIQIGLAY MEAWLRGVGC VPIFNLMEDL ATYEISRSQL YQWVHHQVRT
NEGKTVTSEY VGNILNEEVE KIRKNLGNDK FSQSKYEAAK KAFATNVTGE RYDDFLPDLL
YDDIVSASAH SKL
//
