ID   MTKB_METEA              Reviewed;         296 AA.
AC   P53595; C5B111;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Malate--CoA ligase subunit alpha;
DE            EC=6.2.1.9;
DE   AltName: Full=MTK-alpha;
DE   AltName: Full=Malate thiokinase;
DE   AltName: Full=Malyl-CoA synthetase;
GN   Name=mtkB; OrderedLocusNames=MexAM1_META1p1731;
OS   Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB
OS   9133 / AM1) (Methylobacterium extorquens).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
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 C1
RT   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., Zhou Y.,
RA   Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W.,
RA   Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E.,
RA   Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D.,
RA   Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J.,
RA   Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C.,
RA   Lidstrom M.E.;
RT   "Methylobacterium genome sequences: a reference blueprint to investigate
RT   microbial metabolism of C1 compounds from natural and 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   -!- PATHWAY: One-carbon metabolism; formaldehyde assimilation via serine
CC       pathway.
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_01988}.
CC   -!- SIMILARITY: Belongs to the succinate/malate CoA ligase alpha subunit
CC       family. {ECO:0000255|HAMAP-Rule:MF_01988}.
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DR   EMBL; L33465; AAA62655.1; -; Genomic_DNA.
DR   EMBL; CP001510; ACS39575.1; -; Genomic_DNA.
DR   PIR; C55230; C55230.
DR   RefSeq; WP_003597632.1; NC_012988.1.
DR   AlphaFoldDB; P53595; -.
DR   SMR; P53595; -.
DR   STRING; 272630.MexAM1_META1p1731; -.
DR   EnsemblBacteria; ACS39575; ACS39575; MexAM1_META1p1731.
DR   KEGG; mea:Mex_1p1731; -.
DR   eggNOG; COG0074; Bacteria.
DR   HOGENOM; CLU_052104_0_0_5; -.
DR   OMA; TFHAQEM; -.
DR   OrthoDB; 1081709at2; -.
DR   BioCyc; MetaCyc:MON-4227; -.
DR   UniPathway; UPA00927; -.
DR   Proteomes; UP000009081; Chromosome.
DR   GO; GO:0050074; F:malate-CoA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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; 3.40.50.261; -; 1.
DR   HAMAP; MF_01988; Succ_CoA_alpha; 1.
DR   InterPro; IPR017440; Cit_synth/succinyl-CoA_lig_AS.
DR   InterPro; IPR033847; Citrt_syn/SCS-alpha_CS.
DR   InterPro; IPR003781; CoA-bd.
DR   InterPro; IPR005810; CoA_lig_alpha.
DR   InterPro; IPR005811; CoA_ligase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR016102; Succinyl-CoA_synth-like.
DR   Pfam; PF02629; CoA_binding; 1.
DR   Pfam; PF00549; Ligase_CoA; 1.
DR   PIRSF; PIRSF001553; SucCS_alpha; 1.
DR   SMART; SM00881; CoA_binding; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF52210; SSF52210; 1.
DR   TIGRFAMs; TIGR01019; sucCoAalpha; 1.
DR   PROSITE; PS01216; SUCCINYL_COA_LIG_1; 1.
DR   PROSITE; PS00399; SUCCINYL_COA_LIG_2; 1.
PE   3: Inferred from homology;
KW   Ligase; Nucleotide-binding; Tricarboxylic acid cycle.
FT   CHAIN           1..296
FT                   /note="Malate--CoA ligase subunit alpha"
FT                   /id="PRO_0000102812"
FT   ACT_SITE        251
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01988"
FT   BINDING         17..20
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01988"
FT   BINDING         43
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01988"
FT   BINDING         96..98
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01988"
FT   CONFLICT        253..296
FT                   /note="GAIISATGDSAAEKAEIMRSYGLTVAPDPGSFGSTVADVLARAA -> HHGF
FT                   GSG (in Ref. 1; AAA62655)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   296 AA;  30519 MW;  8B53FB1C2BDF6297 CRC64;
     MSILIDEKTP ILVQGITGDK GTFHAKEMIA YGSNVVGGVT PGKGGKTHCG VPVFNTVKEA
     VEATGATTSI TFVAPPFAAD AIMEAADAGL KLVCSITDGI PAQDMMRVKR YLRRYPKEKR
     TMVVGPNCAG IISPGKSMLG IMPGHIYLPG KVGVISRSGT LGYEAAAQMK ELGIGISTSV
     GIGGDPINGS SFLDHLALFE QDPETEAVLM IGEIGGPQEA EASAWIKENF SKPVIGFVAG
     LTAPKGRRMG HAGAIISATG DSAAEKAEIM RSYGLTVAPD PGSFGSTVAD VLARAA