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Database: UniProt
Entry: P53594
LinkDB: P53594
Original site: P53594 
ID   MTKA_METEA              Reviewed;         390 AA.
AC   P53594; C5B110;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   13-FEB-2019, entry version 111.
DE   RecName: Full=Malate--CoA ligase subunit beta;
DE            EC=6.2.1.9;
DE   AltName: Full=MTK-beta;
DE   AltName: Full=Malate thiokinase;
DE   AltName: Full=Malyl-CoA synthetase;
GN   Name=mtkA; OrderedLocusNames=MexAM1_META1p1730;
OS   Methylobacterium extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 /
OS   NCIMB 9133 / AM1) (Methylorubrum extorquens).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylorubrum.
OX   NCBI_TaxID=272630;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7961516; DOI=10.1128/jb.176.23.7398-7404.1994;
RA   Chistoserdova L.V., Lidstrom M.E.;
RT   "Genetics of the serine cycle in Methylobacterium extorquens AM1:
RT   identification, sequence, and mutation of three new genes involved in
RT   C1 assimilation, orf4, mtkA, and mtkB.";
RL   J. Bacteriol. 176:7398-7404(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1;
RX   PubMed=19440302; DOI=10.1371/journal.pone.0005584;
RA   Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A.,
RA   Zhou Y., Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C.,
RA   Gillett W., Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S.,
RA   Muller E., Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G.,
RA   Roche D., Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z.,
RA   Marx C.J., Vorholt J.A., Olson M.V., Kaul R., Weissenbach J.,
RA   Medigue C., Lidstrom M.E.;
RT   "Methylobacterium genome sequences: a reference blueprint to
RT   investigate microbial metabolism of C1 compounds from natural and
RT   industrial sources.";
RL   PLoS ONE 4:E5584-E5584(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-malate + ATP + CoA = (S)-malyl-CoA + ADP + phosphate;
CC         Xref=Rhea:RHEA:26193, ChEBI:CHEBI:15589, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57317,
CC         ChEBI:CHEBI:456216; EC=6.2.1.9;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00558};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00558};
CC   -!- PATHWAY: One-carbon metabolism; formaldehyde assimilation via
CC       serine pathway.
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00558}.
CC   -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta
CC       subunit family. {ECO:0000255|HAMAP-Rule:MF_00558}.
DR   EMBL; L33465; AAA62654.1; -; Genomic_DNA.
DR   EMBL; CP001510; ACS39574.1; -; Genomic_DNA.
DR   PIR; B55230; B55230.
DR   RefSeq; WP_003597633.1; NC_012808.1.
DR   ProteinModelPortal; P53594; -.
DR   SMR; P53594; -.
DR   STRING; 272630.MexAM1_META1p1730; -.
DR   EnsemblBacteria; ACS39574; ACS39574; MexAM1_META1p1730.
DR   KEGG; mea:Mex_1p1730; -.
DR   eggNOG; ENOG4105CMV; Bacteria.
DR   eggNOG; COG0045; LUCA.
DR   HOGENOM; HOG000007059; -.
DR   KO; K14067; -.
DR   OMA; VQIEINP; -.
DR   OrthoDB; 316012at2; -.
DR   BioCyc; MetaCyc:MONOMER-4228; -.
DR   UniPathway; UPA00927; -.
DR   Proteomes; UP000009081; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0050074; F:malate-CoA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.40.50.261; -; 1.
DR   HAMAP; MF_00558; Succ_CoA_beta; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR005811; CoA_ligase.
DR   InterPro; IPR017866; Succ-CoA_synthase_bsu_CS.
DR   InterPro; IPR005809; Succ_CoA_synthase_bsu.
DR   InterPro; IPR016102; Succinyl-CoA_synth-like.
DR   PANTHER; PTHR11815; PTHR11815; 1.
DR   Pfam; PF08442; ATP-grasp_2; 1.
DR   Pfam; PF00549; Ligase_CoA; 1.
DR   PIRSF; PIRSF001554; SucCS_beta; 1.
DR   SUPFAM; SSF52210; SSF52210; 1.
DR   TIGRFAMs; TIGR01016; sucCoAbeta; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Ligase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Tricarboxylic acid cycle.
FT   CHAIN         1    390       Malate--CoA ligase subunit beta.
FT                                /FTId=PRO_0000102888.
FT   DOMAIN        9    244       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00558}.
FT   METAL       199    199       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00558}.
FT   METAL       213    213       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00558}.
FT   BINDING      46     46       ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   BINDING      99     99       ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   BINDING     102    102       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   BINDING     107    107       ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   CONFLICT     60     60       I -> L (in Ref. 1; AAA62654).
FT                                {ECO:0000305}.
SQ   SEQUENCE   390 AA;  42074 MW;  F25CB69F899760C9 CRC64;
     MDVHEYQAKE LLASFGVAVP KGAVAFSPDQ AVYAATELGG SFWAVKAQIH AGARGKAGGI
     KLCRTYNEVR DAARDLLGKR LVTLQTGPEG KPVQRVYVET ADPFERELYL GYVLDRKAER
     VRVIASQRGG MDIEEIAAKE PEALIQVVVE PAVGLQQFQA REIAFQLGLN IKQVSAAVKT
     IMNAYRAFRD CDGTMLEINP LVVTKDDRVL ALDAKMSFDD NALFRRRNIA DMHDPSQGDP
     REAQAAEHNL SYIGLEGEIG CIVNGAGLAM ATMDMIKHAG GEPANFLDVG GGASPDRVAT
     AFRLVLSDRN VKAILVNIFA GINRCDWVAE GVVKAAREVK IDVPLIVRLA GTNVDEGKKI
     LAESGLDLIT ADTLTEAARK AVEACHGAKH
//
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