SUCC_MAGSA
ID SUCC_MAGSA Reviewed; 398 AA.
AC Q2W063;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Succinate--CoA ligase [ADP-forming] subunit beta {ECO:0000255|HAMAP-Rule:MF_00558};
DE EC=6.2.1.5 {ECO:0000255|HAMAP-Rule:MF_00558};
DE AltName: Full=Succinyl-CoA synthetase subunit beta {ECO:0000255|HAMAP-Rule:MF_00558};
DE Short=SCS-beta {ECO:0000255|HAMAP-Rule:MF_00558};
GN Name=sucC {ECO:0000255|HAMAP-Rule:MF_00558}; OrderedLocusNames=amb3958;
OS Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=342108;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT "Complete genome sequence of the facultative anaerobic magnetotactic
RT bacterium Magnetospirillum sp. strain AMB-1.";
RL DNA Res. 12:157-166(2005).
CC -!- FUNCTION: Succinyl-CoA synthetase functions in the citric acid cycle
CC (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of
CC either ATP or GTP and thus represents the only step of substrate-level
CC phosphorylation in the TCA. The beta subunit provides nucleotide
CC specificity of the enzyme and binds the substrate succinate, while the
CC binding sites for coenzyme A and phosphate are found in the alpha
CC subunit. {ECO:0000255|HAMAP-Rule:MF_00558}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + succinate = ADP + phosphate + succinyl-CoA;
CC Xref=Rhea:RHEA:17661, ChEBI:CHEBI:30031, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292,
CC ChEBI:CHEBI:456216; EC=6.2.1.5; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00558};
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: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC from succinyl-CoA (ligase route): step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_00558}.
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; AP007255; BAE52762.1; -; Genomic_DNA.
DR RefSeq; WP_011386312.1; NC_007626.1.
DR AlphaFoldDB; Q2W063; -.
DR SMR; Q2W063; -.
DR STRING; 342108.amb3958; -.
DR EnsemblBacteria; BAE52762; BAE52762; amb3958.
DR KEGG; mag:amb3958; -.
DR HOGENOM; CLU_037430_0_2_5; -.
DR OMA; ITACDEV; -.
DR OrthoDB; 316012at2; -.
DR UniPathway; UPA00223; UER00999.
DR Proteomes; UP000007058; 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: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 Reference proteome; Tricarboxylic acid cycle.
FT CHAIN 1..398
FT /note="Succinate--CoA ligase [ADP-forming] subunit beta"
FT /id="PRO_1000082118"
FT DOMAIN 9..253
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 53..55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT BINDING 108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT BINDING 111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT BINDING 116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT BINDING 208
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT BINDING 222
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT BINDING 273
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT BINDING 330..332
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
SQ SEQUENCE 398 AA; 42633 MW; 002BCC4080FCB69A CRC64;
MNIHEYQGKQ VLAKYGVAVL KGGVAYTPDE AVQVAKDLGG PVWVVKSQIH AGGRGAGRFK
NDPNGKGGVR VAKSVEEVKT NVDQMLGQVL ITKQTGPAGK EVKRVYIEQG CDIKRELYLS
MLVDRATCRV TIVASTEGGM EIEEVAHNHP EKILKVAIDP VEGFQQYHGR QIAFGLGLEG
KQVNTCVKFV GALYKAFMDL DCSIVEINPL VVTGAGELIA LDAKVNFDDN ALFRHKDIEE
LRDESEEDPA ELEAARHSLN YIKLDGQIGC MVNGAGLAMA TMDIIKLYGA EPANFLDVGG
GATKERVTTA FKLILSDPNV EGILVNIFGG IMRCDVIAEG VVAAAREVSL NVPLVVRLEG
TNVELGKKIM AQSGLPIIAA DNLADAAEKV VKAVKEAA
