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Database: UniProt
Entry: A1RTB8
LinkDB: A1RTB8
Original site: A1RTB8 
ID   SUCC_PYRIL              Reviewed;         382 AA.
AC   A1RTB8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   15-FEB-2017, entry version 67.
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=Pisl_1026;
OS   Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales;
OC   Thermoproteaceae; Pyrobaculum.
OX   NCBI_TaxID=384616;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4184 / JCM 9189 / GEO3;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L.,
RA   Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Lowe T.,
RA   Richardson P.;
RT   "Complete sequence of Pyrobaculum islandicum DSM 4184.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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: ATP + succinate + CoA = ADP + phosphate +
CC       succinyl-CoA. {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-
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; CP000504; ABL88200.1; -; Genomic_DNA.
DR   RefSeq; WP_011762775.1; NC_008701.1.
DR   ProteinModelPortal; A1RTB8; -.
DR   STRING; 384616.Pisl_1026; -.
DR   EnsemblBacteria; ABL88200; ABL88200; Pisl_1026.
DR   GeneID; 4616320; -.
DR   KEGG; pis:Pisl_1026; -.
DR   eggNOG; arCOG01337; Archaea.
DR   eggNOG; COG0045; LUCA.
DR   HOGENOM; HOG000007059; -.
DR   KO; K01903; -.
DR   OMA; ERDCTQV; -.
DR   OrthoDB; POG094900JC; -.
DR   UniPathway; UPA00223; UER00999.
DR   Proteomes; UP000002595; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.30.470.20; -; 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; 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   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; Tricarboxylic acid cycle.
FT   CHAIN         1    382       Succinate--CoA ligase [ADP-forming]
FT                                subunit beta.
FT                                /FTId=PRO_1000082182.
FT   DOMAIN        9    240       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00558}.
FT   NP_BIND      52     54       ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   REGION      317    319       Substrate binding; shared with subunit
FT                                alpha. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   METAL       193    193       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00558}.
FT   METAL       207    207       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     260    260       Substrate; shared with subunit alpha.
FT                                {ECO:0000255|HAMAP-Rule:MF_00558}.
SQ   SEQUENCE   382 AA;  42355 MW;  06E2854D9DBA68B9 CRC64;
     MKLHEYEAKE LFLRYGVKIP PGKLALTPDE VRKIAEEIGT PVVLKAQVVV AGRGKAGGIK
     IAQTPEEAYE LSKKMFGMNI KGLVVRKLYV TKYVEVEREM YLSLIIDRAS RRYLFLASPI
     GGVDIEEIAK TSPEKIKKVY VDPSIGLRDY HIRSIISWLG FKPGSQQWQQ TASVIQAMYR
     IMVDYDAELV ETNPLALSKE GEVIPLDARV IVDDNALFKH PDLEKALEED PRDITEFEAY
     AKKIGFHYVE LDGDIGIIGN GAGLTMATMD LVYHFGGRPA NFLDIGGGAS REVVKEAVKV
     LLNHPRVKVI FVNIFGGITR ADEVALGIKD ALAEVKEHTK KIVVRIKGTN EEQGKAILSE
     IGIPLFENAE EAAKKAVELA KI
//
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