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Database: UniProt
Entry: P9WGC5
LinkDB: P9WGC5
Original site: P9WGC5 
ID   SUCC_MYCTU              Reviewed;         387 AA.
AC   P9WGC5; L0T6W4; P71559;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   13-FEB-2019, entry version 28.
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=Rv0951;
GN   ORFNames=MTCY10D7.23c;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
RA   Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
RA   Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
RA   Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
RA   Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
RA   Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
RA   Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the
RT   complete genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.M111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
RA   Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
RA   Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
RA   Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
RA   Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high
RT   resolution mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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}.
DR   EMBL; AL123456; CCP43699.1; -; Genomic_DNA.
DR   PIR; E70716; E70716.
DR   RefSeq; NP_215466.1; NC_000962.3.
DR   RefSeq; WP_003898659.1; NZ_NVQJ01000001.1.
DR   ProteinModelPortal; P9WGC5; -.
DR   SMR; P9WGC5; -.
DR   STRING; 83332.Rv0951; -.
DR   PaxDb; P9WGC5; -.
DR   PRIDE; P9WGC5; -.
DR   EnsemblBacteria; CCP43699; CCP43699; Rv0951.
DR   GeneID; 885434; -.
DR   KEGG; mtu:Rv0951; -.
DR   TubercuList; Rv0951; -.
DR   eggNOG; ENOG4105CMV; Bacteria.
DR   eggNOG; COG0045; LUCA.
DR   KO; K01903; -.
DR   OMA; LCMDAKF; -.
DR   PhylomeDB; P9WGC5; -.
DR   BioCyc; MetaCyc:G185E-5106-MONOMER; -.
DR   BioCyc; MTBH37RV:G185E-5106-MONOMER; -.
DR   UniPathway; UPA00223; UER00999.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005618; C:cell wall; HDA:MTBBASE.
DR   GO; GO:0005829; C:cytosol; HDA:MTBBASE.
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   ATP-binding; Complete proteome; Ligase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Tricarboxylic acid cycle.
FT   CHAIN         1    387       Succinate--CoA ligase [ADP-forming]
FT                                subunit beta.
FT                                /FTId=PRO_0000102840.
FT   DOMAIN        9    236       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00558}.
FT   NP_BIND      52     54       ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   REGION      318    320       Substrate binding; shared with subunit
FT                                alpha. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   METAL       191    191       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00558}.
FT   METAL       205    205       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00558}.
FT   BINDING      45     45       ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   BINDING      94     94       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   BINDING      99     99       ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   BINDING     256    256       Substrate; shared with subunit alpha.
FT                                {ECO:0000255|HAMAP-Rule:MF_00558}.
SQ   SEQUENCE   387 AA;  40926 MW;  C3155A7CCAF98FDC CRC64;
     MDLFEYQAKE LFAKHNVPST PGRVTDTAEG AKAIATEIGR PVMVKAQVKI GGRGKAGGVK
     YAATPQDAYE HAKNILGLDI KGHIVKKLLV AEASDIAEEY YLSFLLDRAN RTYLAMCSVE
     GGMEIEEVAA TKPERLAKVP VNAVKGVDLD FARSIAEQGH LPAEVLDTAA VTIAKLWELF
     VAEDATLVEV NPLVRTPDHK ILALDAKITL DGNADFRQPG HAEFEDRAAT DPLELKAKEH
     DLNYVKLDGQ VGIIGNGAGL VMSTLDVVAY AGEKHGGVKP ANFLDIGGGA SAEVMAAGLD
     VVLGDQQVKS VFVNVFGGIT SCDAVATGIV KALGMLGDEA NKPLVVRLDG NNVEEGRRIL
     TEANHPLVTL VATMDEAADK AAELASA
//
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