(data stored in ACNUC7421 zone)

SWISSPROT: D1CE55_THET1

ID   D1CE55_THET1            Unreviewed;       382 AA.
AC   D1CE55;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   08-MAY-2019, entry version 67.
DE   RecName: Full=Succinate--CoA ligase [ADP-forming] subunit beta {ECO:0000256|HAMAP-Rule:MF_00558};
DE            EC=6.2.1.5 {ECO:0000256|HAMAP-Rule:MF_00558};
DE   AltName: Full=Succinyl-CoA synthetase subunit beta {ECO:0000256|HAMAP-Rule:MF_00558};
DE            Short=SCS-beta {ECO:0000256|HAMAP-Rule:MF_00558};
GN   Name=sucC {ECO:0000256|HAMAP-Rule:MF_00558};
GN   OrderedLocusNames=Tter_0289 {ECO:0000313|EMBL:ACZ41211.1};
OS   Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC   Bacteria; Thermobaculum.
OX   NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ41211.1, ECO:0000313|Proteomes:UP000000323};
RN   [1] {ECO:0000313|EMBL:ACZ41211.1, ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   PubMed=21304745;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Del Rio T.G., Nolan M.,
RA   Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Lu M., Brettin T.,
RA   Detter J.C., Goker M., Tindall B.J., Beck B., McDermott T.R.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Cheng J.F.;
RT   "Complete genome sequence of 'Thermobaculum terrenum' type strain
RT   (YNP1).";
RL   Stand. Genomic Sci. 3:153-162(2010).
RN   [2] {ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   DOI=10.4056/sigs.1153107;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T.,
RA   Nolan M., Tice H., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Lu M.,
RA   Brettin T., Detter J., Goker M., Tindall B., Beck B., McDermott T.,
RA   Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA   Kyrpides N., Klenk H., Cheng J.;
RT   "Complete genome sequence of Thermobaculum terrenum type strain
RT   (YNP1T).";
RL   Stand. Genomic Sci. 3:153-162(2010).
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:0000256|HAMAP-
CC       Rule:MF_00558, ECO:0000256|SAAS:SAAS01084253}.
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:0000256|HAMAP-
CC         Rule:MF_00558};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00558};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00558};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       succinate from succinyl-CoA (ligase route): step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_00558, ECO:0000256|SAAS:SAAS01084252}.
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits.
CC       {ECO:0000256|HAMAP-Rule:MF_00558, ECO:0000256|SAAS:SAAS01084240}.
CC   -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta
CC       subunit family. {ECO:0000256|HAMAP-Rule:MF_00558,
CC       ECO:0000256|SAAS:SAAS00551500}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00558}.
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DR   EMBL; CP001825; ACZ41211.1; -; Genomic_DNA.
DR   RefSeq; WP_012874246.1; NC_013525.1.
DR   STRING; 525904.Tter_0289; -.
DR   EnsemblBacteria; ACZ41211; ACZ41211; Tter_0289.
DR   KEGG; ttr:Tter_0289; -.
DR   eggNOG; ENOG4105CMV; Bacteria.
DR   eggNOG; COG0045; LUCA.
DR   HOGENOM; HOG000007059; -.
DR   KO; K01903; -.
DR   OMA; LGGITRC; -.
DR   OrthoDB; 316012at2; -.
DR   BioCyc; TTER525904:G1GGS-292-MONOMER; -.
DR   UniPathway; UPA00223; UER00999.
DR   Proteomes; UP000000323; Chromosome 1.
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;
DR   PRODOM; D1CE55.
DR   SWISS-2DPAGE; D1CE55.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00558, ECO:0000256|PROSITE-
KW   ProRule:PRU00409};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000323};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00558,
KW   ECO:0000256|SAAS:SAAS00043448, ECO:0000313|EMBL:ACZ41211.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00558,
KW   ECO:0000256|SAAS:SAAS01086150};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00558,
KW   ECO:0000256|SAAS:SAAS01086152};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00558,
KW   ECO:0000256|PROSITE-ProRule:PRU00409, ECO:0000256|SAAS:SAAS00436163};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000323};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00558,
KW   ECO:0000256|SAAS:SAAS01085245}.
FT   DOMAIN        9    223       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   NP_BIND      52     54       ATP. {ECO:0000256|HAMAP-Rule:MF_00558}.
FT   REGION      313    315       Substrate binding; shared with subunit
FT                                alpha. {ECO:0000256|HAMAP-Rule:MF_00558}.
FT   METAL       191    191       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00558}.
FT   METAL       205    205       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00558}.
FT   BINDING      45     45       ATP. {ECO:0000256|HAMAP-Rule:MF_00558}.
FT   BINDING      94     94       ATP; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00558}.
FT   BINDING      99     99       ATP. {ECO:0000256|HAMAP-Rule:MF_00558}.
FT   BINDING     256    256       Substrate; shared with subunit alpha.
FT                                {ECO:0000256|HAMAP-Rule:MF_00558}.
SQ   SEQUENCE   382 AA;  40939 MW;  AE96B4E3EF808FC7 CRC64;
     MNLHEYQSRE ILAKHGIPIP PGILARSVEE AVEAASSLGY PVVIKAQVHS GGRGKAGGIK
     LVNSQRELEY VAPTILSMNI GGRPVSALLV VPAADIQKEY YLSVVLDREL KTFTLIASAE
     GGVDIEEVAR EHPDSILRVP AHPWLGLQPY QARELAYKVG FEGSLVRTFV EIAMSLYRCA
     LDVEASLVEI NPLAKVSSGD LIALDSKIVV DDNSLFRHPD IAEMRDLSQE ETAEVEASRV
     GISYIKLDGN IGCMVNGAGL AMATMDLVKL YGGSPANFLD IGGGAHADQV EAAMNIILSD
     EKVSAVLINI FGGITRCDDV ARGIVEGLRN IKRGVPIVVR LVGTNEEEGH RILEDAGLRS
     LSSLEEAAKL AVELASKSTV SR
//

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