ID   MTKA_RHILO              Reviewed;         394 AA.
AC   Q98KT9;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Probable 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=mlr1324;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
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-Rule:MF_00558};
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_00558}.
CC   -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta subunit
CC       family. {ECO:0000255|HAMAP-Rule:MF_00558}.
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DR   EMBL; BA000012; BAB48725.1; -; Genomic_DNA.
DR   RefSeq; WP_010910078.1; NC_002678.2.
DR   AlphaFoldDB; Q98KT9; -.
DR   SMR; Q98KT9; -.
DR   STRING; 266835.14022115; -.
DR   EnsemblBacteria; BAB48725; BAB48725; BAB48725.
DR   GeneID; 66683515; -.
DR   KEGG; mlo:mlr1324; -.
DR   eggNOG; COG0045; Bacteria.
DR   HOGENOM; CLU_037430_0_2_5; -.
DR   OMA; AIQQFKV; -.
DR   OrthoDB; 316012at2; -.
DR   UniPathway; UPA00927; -.
DR   Proteomes; UP000000552; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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; 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; PS01217; SUCCINYL_COA_LIG_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Tricarboxylic acid cycle.
FT   CHAIN           1..394
FT                   /note="Probable malate--CoA ligase subunit beta"
FT                   /id="PRO_0000102889"
FT   DOMAIN          9..244
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT   BINDING         46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT   BINDING         99
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT   BINDING         102
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT   BINDING         107
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT   BINDING         199
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT   BINDING         213
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
SQ   SEQUENCE   394 AA;  42482 MW;  A1D573E98E5CB24C CRC64;
     MDIHEYQAKE LLARHGVHVP RGGLAYSPEQ ATYRAREIGG GKWVLKAQVH SGARGKAGGI
     KLCANDEEIS SAAEAMLGRK LVTQQTGPRG KLISRLYLEE AVDIAQELYV GFVLDRKEER
     VMIVASAAGG MEIEDIVEKE PNSILRTSVD PGVGMQRFQA REIAFGLGLD HNLIGKATET
     IFSCYQVFRD YDASMLEINP LVVTRDGNLI ALDAKMSFDE NALFRRPEIS ELRDKSQEDP
     RETFASDRGL SYVGLDGNIG CIINGAGLAM ATMDMIKIAG GEPANFLDIG GGASPERVAK
     SFRAVLGDKN VETILVNIFA GINRCDWVAE GVIKAIREVG VNVPLVVRLS GTKAEEGRRI
     LADSGEAVIV ADTLAEAAEK AVAAWRAAAK KKAA