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Database: UniProt
Entry: SUCC_FRATT
LinkDB: SUCC_FRATT
Original site: 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   27-MAR-2024, entry version 105.
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; Pseudomonadota; 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       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17663;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00558};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CoA + GTP + succinate = GDP + phosphate + succinyl-CoA;
CC         Xref=Rhea:RHEA:22120, ChEBI:CHEBI:30031, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292,
CC         ChEBI:CHEBI:58189; Evidence={ECO:0000255|HAMAP-Rule:MF_00558};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22122;
CC         Evidence={ECO:0000255|HAMAP-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   OrthoDB; 9802602at2; -.
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:0004776; F:succinate-CoA ligase (GDP-forming) activity; IEA:RHEA.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 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; IPR017866; Succ-CoA_synthase_bsu_CS.
DR   InterPro; IPR005811; SUCC_ACL_C.
DR   InterPro; IPR005809; Succ_CoA_ligase-like_bsu.
DR   InterPro; IPR016102; Succinyl-CoA_synth-like.
DR   NCBIfam; TIGR01016; sucCoAbeta; 1.
DR   PANTHER; PTHR11815:SF10; SUCCINATE--COA LIGASE [ADP-FORMING] SUBUNIT BETA, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11815; SUCCINYL-COA SYNTHETASE BETA CHAIN; 1.
DR   Pfam; PF08442; ATP-grasp_2; 1.
DR   Pfam; PF00549; Ligase_CoA; 1.
DR   PIRSF; PIRSF001554; SucCS_beta; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 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
//
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