ID F8KYZ3_PARAV Unreviewed; 533 AA.
AC F8KYZ3;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
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=mls {ECO:0000313|EMBL:CCB86116.1};
GN OrderedLocusNames=PUV_11660 {ECO:0000313|EMBL:CCB86116.1};
OS Parachlamydia acanthamoebae (strain UV7).
OC Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Parachlamydiaceae;
OC Parachlamydia.
OX NCBI_TaxID=765952 {ECO:0000313|EMBL:CCB86116.1, ECO:0000313|Proteomes:UP000000495};
RN [1] {ECO:0000313|EMBL:CCB86116.1, ECO:0000313|Proteomes:UP000000495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UV7 {ECO:0000313|Proteomes:UP000000495};
RX PubMed=21690563; DOI=10.1093/molbev/msr161;
RA Collingro A., Tischler P., Weinmaier T., Penz T., Heinz E., Brunham R.C.,
RA Read T.D., Bavoil P.M., Sachse K., Kahane S., Friedman M.G., Rattei T.,
RA Myers G.S., Horn M.;
RT "Unity in variety--the pan-genome of the Chlamydiae.";
RL Mol. Biol. Evol. 28:3253-3270(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 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}.
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DR EMBL; FR872580; CCB86116.1; -; Genomic_DNA.
DR RefSeq; WP_013924800.1; NC_015702.1.
DR STRING; 765952.PUV_11660; -.
DR KEGG; puv:PUV_11660; -.
DR eggNOG; COG2225; Bacteria.
DR HOGENOM; CLU_018928_3_0_0; -.
DR OrthoDB; 9768429at2; -.
DR UniPathway; UPA00703; UER00720.
DR Proteomes; UP000000495; Chromosome.
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 Acyltransferase {ECO:0000313|EMBL:CCB86116.1};
KW Glyoxylate bypass {ECO:0000256|ARBA:ARBA00022435,
KW ECO:0000256|RuleBase:RU000555};
KW Reference proteome {ECO:0000313|Proteomes:UP000000495};
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 16..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 412..532
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 447
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001363-1"
SQ SEQUENCE 533 AA; 61058 MW; 2D383D539F880447 CRC64;
MKLEKPSVVT TLQIGKIQDR ILIPEAIQFL TELHKEFNGR RKQLLQKRVE RQKQLNQGIL
PTFLPETAAI RDDLTWNIPP PPSDLQKRAV EITGPVERKM MINALNSGAN XFMADFEDAL
SPTWKNVIEG QSNLIDAVNR TISFISPENK SYALKDEIAT LMVRPRGWHL NEKHFQIDGE
EISGSLFDFG LYFFHNARRL IRQGSGPYFY LPKLENHEEA RLWNDVFLFA QDFLSIPQGT
IRATVLIESI LAIFEAEEIL YELREHSAGL NAGRWDYIFS IIKKFQKKED PLLPDRSQIT
MEVPFMQAYT KRIVQICHKR DAHAIGGMAA FIPSRDNPEV THQALEKIKE DKLRECHGGF
DGTWVAHPAL VAIAKGIFEE ILKDQPHQIQ KKFQSSEVSA HDLLDFKVPN GKITEKGVRQ
NVRISLLYME SWLNGVGAAA LDHLMEDAAT AEISRAQLWQ WIHHHPAAQL PDGRTVSAEL
LKQFFEEEQQ KIIAEAKDKN RPHLTEAKKI LESIVMKKAF VEFLTLISYE HLT
//
