MTKA_METEA
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 03-AUG-2022, entry version 133.
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 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 -!- 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 AlphaFoldDB; P53594; -.
DR SMR; P53594; -.
DR STRING; 272630.MexAM1_META1p1730; -.
DR PRIDE; P53594; -.
DR EnsemblBacteria; ACS39574; ACS39574; MexAM1_META1p1730.
DR KEGG; mea:Mex_1p1730; -.
DR eggNOG; COG0045; Bacteria.
DR HOGENOM; CLU_037430_0_2_5; -.
DR OMA; AIQQFKV; -.
DR OrthoDB; 316012at2; -.
DR BioCyc; MetaCyc:MON-4228; -.
DR UniPathway; UPA00927; -.
DR Proteomes; UP000009081; 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; 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; Ligase; Magnesium; Metal-binding; Nucleotide-binding;
KW Tricarboxylic acid cycle.
FT CHAIN 1..390
FT /note="Malate--CoA ligase subunit beta"
FT /id="PRO_0000102888"
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"
FT CONFLICT 60
FT /note="I -> L (in Ref. 1; AAA62654)"
FT /evidence="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
