ID A0A1Q9UTJ8_9MICO Unreviewed; 539 AA.
AC A0A1Q9UTJ8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=BJF86_03880 {ECO:0000313|EMBL:OLT40969.1};
OS Serinicoccus sp. CNJ-927.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Ornithinimicrobiaceae; Serinicoccus.
OX NCBI_TaxID=1904970 {ECO:0000313|EMBL:OLT40969.1, ECO:0000313|Proteomes:UP000186856};
RN [1] {ECO:0000313|EMBL:OLT40969.1, ECO:0000313|Proteomes:UP000186856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNJ-927 {ECO:0000313|EMBL:OLT40969.1,
RC ECO:0000313|Proteomes:UP000186856};
RX PubMed=27902408; DOI=10.1099/mic.0.000386;
RA Schorn M.A., Alanjary M.M., Aguinaldo K., Korobeynikov A., Podell S.,
RA Patin N., Lincecum T., Jensen P.R., Ziemert N., Moore B.S.;
RT "Sequencing rare marine actinomycete genomes reveals high density of unique
RT natural product biosynthetic gene clusters.";
RL Microbiology 162:2075-2086(2016).
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:OLT40969.1}.
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DR EMBL; MKKF01000033; OLT40969.1; -; Genomic_DNA.
DR RefSeq; WP_075818690.1; NZ_MKKF01000033.1.
DR AlphaFoldDB; A0A1Q9UTJ8; -.
DR OrthoDB; 9768429at2; -.
DR UniPathway; UPA00703; UER00720.
DR Proteomes; UP000186856; 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 15..76
FT /note="Malate synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF20656"
FT DOMAIN 172..417
FT /note="Malate synthase TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01274"
FT DOMAIN 425..537
FT /note="Malate synthase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF20659"
FT ACT_SITE 176
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 539 AA; 59743 MW; 50ED3BBF5D7DAC07 CRC64;
MASTDAPITL DLPEGVLVTG ELRPGYDEIL TRPALELVAQ LHRSLETRRQ ECLAARADVV
RRVADGEDLD FLPETAQVRA DDTWRVADPA PGLVDRRVEM TGPTDRKMTI NAMNSGARVW
LADQEDANTP LWENVVEGQI NLRDAISGTI SFTSPEGKEY ALTTTDQQQL PTIVMRPRGW
HLDEKHITVD GQRVAGGLVD VALYLCASAQ LQLDAGKGPY FYLPKMEHHL EARLWNDAFV
LAQDALGIPQ GTIRATCLIE TYPAAFQMEE ILHELREHSA GLNAGRWDYL FSVIKTYRTR
GADFVLPDRA AVTMTAPFMR AYTELLVRTC HRRGAHAIGG MSAFVPAKDE EVNAAAYEKV
RTDKEREARD GFDGSWVAHP AMVPTCREVF DAVFGDRPNQ LDRTREDVQV RAADLLDVAS
TPGEVTEQGL KANIEVAIAY LSVWLTGRGA VAIHHLMEDA ATAEISRSQV WQWLHQGITL
ADTGERVTPE LVRQLTDQVL EELPGGADEH RAATELFLQV AVAEEFADFL TVPAYETMP
//
