ID D5WWP2_KYRT2 Unreviewed; 531 AA.
AC D5WWP2;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 24-JAN-2024, entry version 66.
DE RecName: Full=malate synthase {ECO:0000256|ARBA:ARBA00012636};
DE EC=2.3.3.9 {ECO:0000256|ARBA:ARBA00012636};
GN OrderedLocusNames=Btus_1005 {ECO:0000313|EMBL:ADG05743.1};
OS Kyrpidia tusciae (strain DSM 2912 / NBRC 15312 / T2) (Bacillus tusciae).
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae; Kyrpidia.
OX NCBI_TaxID=562970 {ECO:0000313|EMBL:ADG05743.1, ECO:0000313|Proteomes:UP000002368};
RN [1] {ECO:0000313|Proteomes:UP000002368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2912 / NBRC 15312 / T2 {ECO:0000313|Proteomes:UP000002368};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Ovchinnikova G., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F.,
RA Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T.,
RA Wu D., Pukall R., Schneider S., Wahrenburg C., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Bacillus tusciae DSM 2912.";
RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADG05743.1, ECO:0000313|Proteomes:UP000002368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2912 / NBRC 15312 / T2 {ECO:0000313|Proteomes:UP000002368};
RX PubMed=22180816; DOI=10.4056/sigs.2144922;
RA Klenk H.P., Lapidus A., Chertkov O., Copeland A., Del Rio T.G., Nolan M.,
RA Lucas S., Chen F., Tice H., Cheng J.F., Han C., Bruce D., Goodwin L.,
RA Pitluck S., Pati A., Ivanova N., Mavromatis K., Daum C., Chen A.,
RA Palaniappan K., Chang Y.J., Land M., Hauser L., Jeffries C.D., Detter J.C.,
RA Rohde M., Abt B., Pukall R., Goker M., Bristow J., Markowitz V.,
RA Hugenholtz P., Eisen J.A.;
RT "Complete genome sequence of the thermophilic, hydrogen-oxidizing Bacillus
RT tusciae type strain (T2) and reclassification in the new genus, Kyrpidia
RT gen. nov. as Kyrpidia tusciae comb. nov. and emendation of the family
RT Alicyclobacillaceae da Costa and Rainey, 2010.";
RL Stand. Genomic Sci. 5:121-134(2011).
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 -!- SIMILARITY: Belongs to the malate synthase family.
CC {ECO:0000256|ARBA:ARBA00006394}.
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DR EMBL; CP002017; ADG05743.1; -; Genomic_DNA.
DR RefSeq; WP_013075034.1; NC_014098.1.
DR AlphaFoldDB; D5WWP2; -.
DR STRING; 562970.Btus_1005; -.
DR KEGG; bts:Btus_1005; -.
DR eggNOG; COG2225; Bacteria.
DR HOGENOM; CLU_018928_3_0_9; -.
DR OrthoDB; 9768429at2; -.
DR Proteomes; UP000002368; Chromosome.
DR GO; GO:0004474; F:malate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
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; 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.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:ADG05743.1};
KW Glyoxylate bypass {ECO:0000256|ARBA:ARBA00022435};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADG05743.1};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 7..68
FT /note="Malate synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF20656"
FT DOMAIN 160..405
FT /note="Malate synthase TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01274"
FT DOMAIN 410..528
FT /note="Malate synthase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF20659"
FT ACT_SITE 164
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 531 AA; 60025 MW; 003BAA138F549879 CRC64;
MAEWPQGVEV IGEVTPEYGE ILTPEALAFV ADLHRRFDER RRALLADRAE RQKRLDAGWR
PDFPAETAEI RAGDWTVGPI PADLQDRRVE ITGPAGDRKM VINALNSGAK VFMADFEDAN
SPTWANTVGG QVNLRDAVNR TITYTSPEGK QYALKDQVAV LMVRPRGWHL GEKHVRVDGR
PVSGALFDFA LYLFHNAKNL IARGTGPYYY LPKMESRHEA RLWNDVFTFA EDRMHLPVGT
IKATVLLETI MATFEMDEML YELRDHIVGM NCGRWDYIFS YIKRFRNQPD VIFPDRNLVT
MTVPFMRAYT LYTIKTCHRR GAFAIGGMAA QIPVKNDPAA NEEAFAKVRA DKEREARDGH
DGTWVAHPGL VPVAMEVFDR LMPGPNQLSR KREDVQVTAD DLLAIPEGPI TEQGLRNNVS
VGIQYIEAWL RGNGAVPIFH LMEDAATAEI ARAQVWQWIH HPKGILADGR KVDAALFRQI
LAEELQKIKE NLGEARFAQG KFDQAAALFT DMSLRDDFEE FLTLPGYAYL D
//
