SUCC_HISS2
ID SUCC_HISS2 Reviewed; 389 AA.
AC B0UUF3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=HSM_1432;
OS Histophilus somni (strain 2336) (Haemophilus somnus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Histophilus.
OX NCBI_TaxID=228400;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2336;
RG US DOE Joint Genome Institute;
RA Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D., Gillaspy A.F.,
RA Carson M., Gipson J., Gipson M., Bruce D., Detter J.C., Han C.S., Land M.,
RA Tapia R., Thompson L.S., Orvis J., Zaitshik J., Barnes G., Brettin T.S.,
RA Dyer D.W., Inzana T.J.;
RT "Complete sequence of Haemophilus somnus 2336.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000947; ACA31177.1; -; Genomic_DNA.
DR RefSeq; WP_012340577.1; NC_010519.1.
DR AlphaFoldDB; B0UUF3; -.
DR SMR; B0UUF3; -.
DR STRING; 228400.HSM_1432; -.
DR EnsemblBacteria; ACA31177; ACA31177; HSM_1432.
DR KEGG; hsm:HSM_1432; -.
DR HOGENOM; CLU_037430_0_2_6; -.
DR OMA; ITACDEV; -.
DR OrthoDB; 316012at2; -.
DR UniPathway; UPA00223; UER00999.
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 Tricarboxylic acid cycle.
FT CHAIN 1..389
FT /note="Succinate--CoA ligase [ADP-forming] subunit beta"
FT /id="PRO_1000082101"
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 53..55
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 BINDING 264
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT BINDING 321..323
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
SQ SEQUENCE 389 AA; 42528 MW; 2EC955495B8D251E CRC64;
MNLHEYQSKK LFADYGLPVT KGYVCENVEQ ALSAIEKLSG SQWIAKCQIH AGGRGKAGGV
KVVKSAQEVR SFFTKFLGQR LVTVQTNEQG QPIHQIYLEP CAEIQKELYL SAIIDRSSQR
IVFMASSEGG MDIEEVAEKT PHLLHRVTID PLVGAMPYQG RELAFKLGLS GKQIQQFSQI
FCQLAKLFVE KDLSLLEINP LVILKNDELF CLDAKVVVDD NALYRHPDLF SMRDLTQEDP
REAEAEKWNL NYVALDGNIG CMVNGAGLAM GTMDIIKLHG GRPANFLDVG GGATKERVME
AFKIILTDSA VKAVLVNIFG GIVRCDLIAK GIVSAINEIG VSVPVIVRLE GTNADLGREI
LAQSNLNLIA VNSLTEAAEQ AVNAAKESE
