SUCC_FRATT
ID SUCC_FRATT Reviewed; 387 AA.
AC Q5NHF3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=FTT_0504c;
OS Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=177416;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCHU S4 / Schu 4;
RX PubMed=15640799; DOI=10.1038/ng1499;
RA Larsson P., Oyston P.C.F., Chain P., Chu M.C., Duffield M., Fuxelius H.-H.,
RA Garcia E., Haelltorp G., Johansson D., Isherwood K.E., Karp P.D.,
RA Larsson E., Liu Y., Michell S., Prior J., Prior R., Malfatti S.,
RA Sjoestedt A., Svensson K., Thompson N., Vergez L., Wagg J.K., Wren B.W.,
RA Lindler L.E., Andersson S.G.E., Forsman M., Titball R.W.;
RT "The complete genome sequence of Francisella tularensis, the causative
RT agent of tularemia.";
RL Nat. Genet. 37:153-159(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; AJ749949; CAG45137.1; -; Genomic_DNA.
DR RefSeq; WP_003020338.1; NZ_CP010290.1.
DR RefSeq; YP_169539.1; NC_006570.2.
DR PDB; 6MGG; X-ray; 1.78 A; B/D=1-387.
DR PDB; 6PFN; X-ray; 1.76 A; B/D=1-387.
DR PDBsum; 6MGG; -.
DR PDBsum; 6PFN; -.
DR AlphaFoldDB; Q5NHF3; -.
DR SMR; Q5NHF3; -.
DR STRING; 177416.FTT_0504c; -.
DR EnsemblBacteria; CAG45137; CAG45137; FTT_0504c.
DR KEGG; ftu:FTT_0504c; -.
DR eggNOG; COG0045; Bacteria.
DR OMA; ITACDEV; -.
DR UniPathway; UPA00223; UER00999.
DR Proteomes; UP000001174; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Tricarboxylic acid cycle.
FT CHAIN 1..387
FT /note="Succinate--CoA ligase [ADP-forming] subunit beta"
FT /id="PRO_1000082093"
FT DOMAIN 9..245
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 100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT BINDING 103
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 200
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT BINDING 214
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT BINDING 265
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT BINDING 322..324
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT HELIX 5..14
FT /evidence="ECO:0007829|PDB:6PFN"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:6PFN"
FT HELIX 28..38
FT /evidence="ECO:0007829|PDB:6PFN"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:6PFN"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:6PFN"
FT TURN 54..58
FT /evidence="ECO:0007829|PDB:6PFN"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:6PFN"
FT HELIX 66..76
FT /evidence="ECO:0007829|PDB:6PFN"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:6MGG"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:6PFN"
FT STRAND 105..116
FT /evidence="ECO:0007829|PDB:6PFN"
FT TURN 117..120
FT /evidence="ECO:0007829|PDB:6PFN"
FT STRAND 121..128
FT /evidence="ECO:0007829|PDB:6PFN"
FT HELIX 134..140
FT /evidence="ECO:0007829|PDB:6PFN"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:6PFN"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:6PFN"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:6PFN"
FT HELIX 158..167
FT /evidence="ECO:0007829|PDB:6PFN"
FT HELIX 173..191
FT /evidence="ECO:0007829|PDB:6PFN"
FT STRAND 194..205
FT /evidence="ECO:0007829|PDB:6PFN"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:6PFN"
FT STRAND 214..219
FT /evidence="ECO:0007829|PDB:6PFN"
FT HELIX 221..226
FT /evidence="ECO:0007829|PDB:6PFN"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:6PFN"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:6PFN"
FT HELIX 241..248
FT /evidence="ECO:0007829|PDB:6PFN"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:6PFN"
FT STRAND 257..266
FT /evidence="ECO:0007829|PDB:6PFN"
FT HELIX 267..278
FT /evidence="ECO:0007829|PDB:6PFN"
FT TURN 279..281
FT /evidence="ECO:0007829|PDB:6PFN"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:6PFN"
FT HELIX 298..308
FT /evidence="ECO:0007829|PDB:6PFN"
FT STRAND 315..318
FT /evidence="ECO:0007829|PDB:6PFN"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:6PFN"
FT HELIX 326..337
FT /evidence="ECO:0007829|PDB:6MGG"
FT STRAND 346..349
FT /evidence="ECO:0007829|PDB:6PFN"
FT HELIX 355..363
FT /evidence="ECO:0007829|PDB:6MGG"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:6MGG"
FT STRAND 370..374
FT /evidence="ECO:0007829|PDB:6PFN"
FT HELIX 375..384
FT /evidence="ECO:0007829|PDB:6PFN"
SQ SEQUENCE 387 AA; 41542 MW; 919784198896DE32 CRC64;
MNLHEYQAKD LLESYGLKVQ KGIVAHNPNE AAQAFDQLGG KFAVVKAQVH AGGRGKAGGV
KVVKSSQEAR EVAESLIGKN LVTFQTDAEG QPVNSVGVFE DVYPVTRELY LGAVVDRSSR
KVTFMASTEG GVDIEEVAHN SPEKILKVEV DPLVGLQPFQ AREVAFKLGL EGKQINDFVK
TMLGAYKAFI ECDFALFEIN PLAVRENGEI VCVDGKINLD SNALYRHPKL LALRDKSQEN
AKELKASEHE LNYVALEGNI GCMVNGAGLA MATMDIIQLY GGKPANFLDV GGGATKERVI
EAFKLILDDE NVKAILINIF GGIVRCDMIA EAIIEAVKEV NVTVPVVVRL EGNNAEKGAK
ILADSGLKLI PADGLADAAD KVVKSLG
