ID A0A0Q9N4H6_9MICC Unreviewed; 550 AA.
AC A0A0Q9N4H6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=ASG77_17295 {ECO:0000313|EMBL:KRE69138.1};
OS Arthrobacter sp. Soil762.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1736401 {ECO:0000313|EMBL:KRE69138.1, ECO:0000313|Proteomes:UP000051715};
RN [1] {ECO:0000313|Proteomes:UP000051715}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil762 {ECO:0000313|Proteomes:UP000051715};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE69138.1, ECO:0000313|Proteomes:UP000051715}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil762 {ECO:0000313|EMBL:KRE69138.1,
RC ECO:0000313|Proteomes:UP000051715};
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:KRE69138.1}.
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DR EMBL; LMSG01000023; KRE69138.1; -; Genomic_DNA.
DR RefSeq; WP_056349597.1; NZ_LMSG01000023.1.
DR AlphaFoldDB; A0A0Q9N4H6; -.
DR OrthoDB; 9768429at2; -.
DR UniPathway; UPA00703; UER00720.
DR Proteomes; UP000051715; 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 19..73
FT /note="Malate synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF20656"
FT DOMAIN 167..408
FT /note="Malate synthase TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01274"
FT DOMAIN 421..532
FT /note="Malate synthase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF20659"
FT ACT_SITE 171
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001363-1"
FT ACT_SITE 455
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001363-1"
SQ SEQUENCE 550 AA; 62277 MW; C20A686E01ABA7FB CRC64;
MNTFTDSFTI NGITLTAQPV CRQDEVLTPD ALEFVAKLHR ATAERRQELL QARRTRRAEI
AAGQDPSFLR ETEDIRNDPS WRVAPPAPGL EDRRVEITGP VDKKMTINAL NSGAKVWLAD
MEDSSTPTWR NVIKGQLNLT DALERRIDYT SPEGKEYKLR PAGELPTIVV RPRGWHLPEK
HMIIDGAPVA GGIVDFGLFF FHNARRLLAQ GKGPYFYLPK IENHLEARLW NDIFILAQDL
LGIPQGTIRA TVLIETITAA FEMEEILYEL RDHASGLNAG RWDYIFSLIK NFRTRGPRFV
LPDRAQVTMT QPFMRAYTEQ LVRACHKRGA MAIGGMAAAV PNRKDEAANT NAFEKVRADK
TREANDGFDG SWVAHPDLVP VCREVFDATL GERPNQLDRT REDVIPDDRA LINVAATTGT
ITEQGIRNNI EVGIRYIESW LRGNGAVAIH NLMEDAATAE ISRSQIWQWM FASAITDRGE
IITHQWIEEL LDEEFARLER FDGDRFEDSR DIFEEVTLSQ DFPSFLTLPA YARYLTEARE
KATKEELSAA
//
