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Database: UniProt
Entry: Q7UKI3
LinkDB: Q7UKI3
Original site: Q7UKI3 
ID   SUCC_RHOBA              Reviewed;         394 AA.
AC   Q7UKI3;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 2.
DT   16-JAN-2019, entry version 88.
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};
GN   OrderedLocusNames=RB10617;
OS   Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC   Bacteria; Planctomycetes; Planctomycetia; Planctomycetales;
OC   Planctomycetaceae; Rhodopirellula.
OX   NCBI_TaxID=243090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX   PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA   Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T.,
RA   Ludwig W., Gade D., Beck A., Borzym K., Heitmann K., Rabus R.,
RA   Schlesner H., Amann R., Reinhardt R.;
RT   "Complete genome sequence of the marine planctomycete Pirellula sp.
RT   strain 1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
CC   -!- FUNCTION: Succinyl-CoA synthetase functions in the citric acid
CC       cycle (TCA), coupling the hydrolysis of succinyl-CoA to the
CC       synthesis of either ATP or GTP and thus represents the only step
CC       of substrate-level phosphorylation in the TCA. The beta subunit
CC       provides nucleotide specificity of the enzyme and binds the
CC       substrate succinate, while the binding sites for coenzyme A and
CC       phosphate are found in the alpha subunit. {ECO:0000255|HAMAP-
CC       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-
CC       Rule:MF_00558};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       succinate from succinyl-CoA (ligase route): step 1/1.
CC       {ECO:0000255|HAMAP-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
CC       subunit family. {ECO:0000255|HAMAP-Rule:MF_00558}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAD76879.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; BX294152; CAD76879.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_869518.1; NC_005027.1.
DR   ProteinModelPortal; Q7UKI3; -.
DR   SMR; Q7UKI3; -.
DR   STRING; 243090.RB10617; -.
DR   EnsemblBacteria; CAD76879; CAD76879; RB10617.
DR   GeneID; 1795467; -.
DR   KEGG; rba:RB10617; -.
DR   PATRIC; fig|243090.15.peg.5131; -.
DR   eggNOG; ENOG4105CMV; Bacteria.
DR   eggNOG; COG0045; LUCA.
DR   HOGENOM; HOG000007059; -.
DR   InParanoid; Q7UKI3; -.
DR   KO; K01903; -.
DR   OrthoDB; 316012at2; -.
DR   UniPathway; UPA00223; UER00999.
DR   Proteomes; UP000001025; Chromosome.
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; Complete proteome; Ligase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Tricarboxylic acid cycle.
FT   CHAIN         1    394       Succinate--CoA ligase [ADP-forming]
FT                                subunit beta.
FT                                /FTId=PRO_0000102848.
FT   DOMAIN        9    252       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00558}.
FT   NP_BIND      53     55       ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   REGION      329    331       Substrate binding; shared with subunit
FT                                alpha. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   METAL       207    207       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00558}.
FT   METAL       221    221       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00558}.
FT   BINDING      46     46       ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   BINDING     107    107       ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   BINDING     110    110       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   BINDING     115    115       ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   BINDING     272    272       Substrate; shared with subunit alpha.
FT                                {ECO:0000255|HAMAP-Rule:MF_00558}.
SQ   SEQUENCE   394 AA;  41891 MW;  C693CBC8EF600148 CRC64;
     MKIHEYQGKQ LFRTAGVPVL DGHMVTTPDE AAAAYDKLGG KIAVVKAQIH AGGRGKGNVI
     DNPDQKGVVL VKSAEEAKAA AEGLLGKKLV TIQTGPEGQT VSKVFVEAGC DIARELYLGI
     VVDRAGSKPV LMVSTEGGVE IETVAEETPE LIFKEHFDPA VGLDGFQVRK LCKKLGIEGA
     AAKSAYKFMT AMCRFFVDFD CEMAEINPLV ITGDGEMVAL DAKIIFDENA MFRHKDLEEL
     RDLSEEEESE LRAKKAGLSY VKLDGNIACL VNGAGLAMST MDIIKYHGGE PANFLDVGGG
     ANAAQVTEAF RILLSDPNCK GVLVNIFGGI ARCTTIAGAL ITASKEVGFN VPLVVRLEGT
     EVEEGRKMLA ESDVDIINAM DLTDAAKKIV AATA
//
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