ID   SUCC1_STRCO             Reviewed;         394 AA.
AC   Q9KY56;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   16-JUN-2009, entry version 57.
DE   RecName: Full=Succinyl-CoA ligase [ADP-forming] subunit beta-1;
DE            EC=6.2.1.5;
DE   AltName: Full=Succinyl-CoA synthetase subunit beta-1;
DE            Short=SCS-beta-1;
GN   Name=sucC1; OrderedLocusNames=SCO4808; ORFNames=SCD63A.19;
OS   Streptomyces coelicolor.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Streptomycineae; Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1902;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   MEDLINE=21996410; PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H.,
RA   Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M.,
RA   Cronin A., Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S.,
RA   Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S.,
RA   Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S.,
RA   Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K.,
RA   Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J.,
RA   Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces
RT   coelicolor A3(2).";
RL   Nature 417:141-147(2002).
CC   -!- CATALYTIC ACTIVITY: ATP + succinate + CoA = ADP + phosphate +
CC       succinyl-CoA.
CC   -!- COFACTOR: Binds 1 magnesium or manganese ion per subunit (By
CC       similarity).
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta
CC       subunit family.
CC   -!- SIMILARITY: Contains 1 ATP-grasp domain.
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DR   EMBL; AL939121; CAB92671.1; -; Genomic_DNA.
DR   RefSeq; NP_628965.1; -.
DR   HSSP; P07460; 1JKJ.
DR   GeneID; 1100249; -.
DR   GenomeReviews; AL645882_GR; SCO4808.
DR   KEGG; sco:SCO4808; -.
DR   NMPDR; fig|100226.1.peg.4763; -.
DR   HOGENOM; Q9KY56; -.
DR   OMA; Q9KY56; NLHCLDA.
DR   BioCyc; SCOE100226:SCO4808-MON; -.
DR   BRENDA; 6.2.1.5; 1084.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IEA:HAMAP.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:HAMAP.
DR   HAMAP; MF_00558; -; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type.
DR   InterPro; IPR013816; ATP_grasp_subdomain_2.
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   Gene3D; G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 1.
DR   Gene3D; G3DSA:3.40.50.261; Succinyl-CoA_synth-like; 1.
DR   PANTHER; PTHR11815; CoA_lig_beta; 1.
DR   Pfam; PF08442; ATP-grasp_2; 1.
DR   Pfam; PF00549; Ligase_CoA; 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; Manganese;
KW   Metal-binding; Nucleotide-binding; Tricarboxylic acid cycle.
FT   CHAIN         1    394       Succinyl-CoA ligase [ADP-forming] subunit
FT                                beta-1.
FT                                /FTId=PRO_0000102869.
FT   DOMAIN        9    237       ATP-grasp.
FT   NP_BIND      35    101       ATP (By similarity).
FT   METAL       190    190       Magnesium or manganese (By similarity).
FT   METAL       192    192       Magnesium or manganese (By similarity).
SQ   SEQUENCE   394 AA;  41602 MW;  14839C3E479D2783 CRC64;
     MDLFEYQARD LFAKHDVPVL AGEVIDTPEA AREITERLGG KSVVKAQVKV GGRGKAGGVK
     LAASADEAVA RATDILGMDI KGHTVHKVMI AETAPEIVEE YYVSFLLDRA NRTFLSIASV
     EGGVEIEEVA ATRPEAVAKT PIDAIDGVTP EKAREIVEAA KFPAEVADKV ADILVKLWDT
     FIKEDALLVE VNPLAKVVSG DVIALDGKVS LDDNAEFRHP DFEALHDKAA ANPLEAAAKE
     KNLNYVKLDG EVGIIGNGAG LVMSTLDVVA YAGEAHGNVK PANFLDIGGG ASAQVMANGL
     EIILGDPDVR SVFVNVFGGI TACDEVANGI VQALKLLEDR GEKVEKPLVV RLDGNNAELG
     RKILTDANHP LVQRVDTMDG AADKAAELAH AAAK
//