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Database: UniProt
Entry: P0A836
LinkDB: P0A836
Original site: P0A836 
ID   SUCC_ECOLI              Reviewed;         388 AA.
AC   P0A836; P07460;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   13-FEB-2019, entry version 121.
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, ECO:0000269|PubMed:10353839, ECO:0000269|PubMed:7040388};
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=b0728, JW0717;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3002435; DOI=10.1021/bi00343a031;
RA   Buck D., Spencer M.E., Guest J.R.;
RT   "Primary structure of the succinyl-CoA synthetase of Escherichia
RT   coli.";
RL   Biochemistry 24:6245-6252(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
RA   Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
RA   Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
RA   Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
RA   Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
RA   Yano M., Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome
RT   corresponding to the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   PROTEIN SEQUENCE OF 1-12.
RC   STRAIN=K12 / EMG2;
RX   PubMed=9298646; DOI=10.1002/elps.1150180807;
RA   Link A.J., Robison K., Church G.M.;
RT   "Comparing the predicted and observed properties of proteins encoded
RT   in the genome of Escherichia coli K-12.";
RL   Electrophoresis 18:1259-1313(1997).
RN   [6]
RP   CATALYTIC ACTIVITY, AND COFACTOR.
RX   PubMed=7040388;
RA   Vogel H.J., Bridger W.A.;
RT   "A phosphorus 31 nuclear magnetic resonance study of the intermediates
RT   of the Escherichia coli succinyl coenzyme A synthetase reaction.
RT   Evidence for substrate synergism and catalytic cooperativity.";
RL   J. Biol. Chem. 257:4834-4842(1982).
RN   [7]
RP   IDENTIFICATION BY 2D-GEL.
RX   PubMed=9298644; DOI=10.1002/elps.1150180805;
RA   VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R.,
RA   Neidhardt F.C.;
RT   "Escherichia coli proteome analysis using the gene-protein database.";
RL   Electrophoresis 18:1243-1251(1997).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=10353839; DOI=10.1021/bi990527s;
RA   Joyce M.A., Fraser M.E., Brownie E.R., James M.N., Bridger W.A.,
RA   Wolodko W.T.;
RT   "Probing the nucleotide-binding site of Escherichia coli succinyl-CoA
RT   synthetase.";
RL   Biochemistry 38:7273-7283(1999).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH SUCD, CATALYTIC
RP   ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=8144675;
RA   Wolodko W.T., Fraser M.E., James M.N.G., Bridger W.A.;
RT   "The crystal structure of succinyl-CoA synthetase from Escherichia
RT   coli at 2.5-A resolution.";
RL   J. Biol. Chem. 269:10883-10890(1994).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH SUCD.
RX   PubMed=9917402; DOI=10.1006/jmbi.1998.2324;
RA   Fraser M.E., James M.N., Bridger W.A., Wolodko W.T.;
RT   "A detailed structural description of Escherichia coli succinyl-CoA
RT   synthetase.";
RL   J. Mol. Biol. 285:1633-1653(1999).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) IN COMPLEX WITH SUCD; ADP AND
RP   MAGNESIUM.
RX   PubMed=10625475; DOI=10.1021/bi991696f;
RA   Joyce M.A., Fraser M.E., James M.N., Bridger W.A., Wolodko W.T.;
RT   "ADP-binding site of Escherichia coli succinyl-CoA synthetase revealed
RT   by X-ray crystallography.";
RL   Biochemistry 39:17-25(2000).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF MUTANT ALA-197 IN COMPLEX
RP   WITH SUCD.
RX   PubMed=11781092; DOI=10.1021/bi011518y;
RA   Fraser M.E., Joyce M.A., Ryan D.G., Wolodko W.T.;
RT   "Two glutamate residues, Glu 208 alpha and Glu 197 beta, are crucial
RT   for phosphorylation and dephosphorylation of the active-site histidine
RT   residue in succinyl-CoA synthetase.";
RL   Biochemistry 41:537-546(2002).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH SUCD.
RX   PubMed=17642514; DOI=10.1107/S0907444907029319;
RA   Hidber E., Brownie E.R., Hayakawa K., Fraser M.E.;
RT   "Participation of Cys123alpha of Escherichia coli succinyl-CoA
RT   synthetase in catalysis.";
RL   Acta Crystallogr. D 63:876-884(2007).
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. Can use either ATP or
CC       GTP, but prefers ATP. It can also function in the other direction
CC       for anabolic purposes, and this may be particularly important for
CC       providing succinyl-CoA during anaerobic growth when the oxidative
CC       route from 2-oxoglutarate is severely repressed.
CC       {ECO:0000255|HAMAP-Rule:MF_00558, ECO:0000269|PubMed:10353839}.
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, ECO:0000269|PubMed:10353839,
CC         ECO:0000269|PubMed:7040388};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00558,
CC         ECO:0000269|PubMed:10625475, ECO:0000269|PubMed:7040388};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00558, ECO:0000269|PubMed:10625475};
CC   -!- ACTIVITY REGULATION: Exhibits two interesting properties:
CC       "substrate synergism", in which the enzyme is most active for the
CC       catalysis of its partial reactions only when all the substrate-
CC       binding sites are occupied, and "catalytic cooperativity" between
CC       alternating active sites in the tetramer, whereby the interaction
CC       of substrates (particularly ATP) at one site is needed to promote
CC       catalysis at the other.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=70 uM for ATP {ECO:0000269|PubMed:10353839};
CC         KM=394 uM for GTP {ECO:0000269|PubMed:10353839};
CC         Note=kcat is 2684 min(-1) with ATP as substrate and 1471 min(-1)
CC         with GTP as substrate. {ECO:0000269|PubMed:10353839};
CC       pH dependence:
CC         Optimum pH is 7.4. {ECO:0000269|PubMed:8144675};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       succinate from succinyl-CoA (ligase route): step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_00558, ECO:0000305|PubMed:10353839}.
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00558, ECO:0000269|PubMed:8144675,
CC       ECO:0000269|PubMed:9917402}.
CC   -!- INTERACTION:
CC       P0AGE9:sucD; NbExp=4; IntAct=EBI-369117, EBI-369078;
CC   -!- MISCELLANEOUS: Succinyl-CoA synthetase (SCS) of E.coli catalyzes
CC       its reaction via three steps that involve phosphoryl enzyme and
CC       enzyme-bound succinyl phosphate as intermediates.
CC   -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta
CC       subunit family. {ECO:0000255|HAMAP-Rule:MF_00558}.
DR   EMBL; J01619; AAA23899.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73822.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35394.1; -; Genomic_DNA.
DR   PIR; A24090; SYECSB.
DR   RefSeq; NP_415256.1; NC_000913.3.
DR   RefSeq; WP_001048602.1; NZ_LN832404.1.
DR   PDB; 1CQI; X-ray; 3.30 A; B/E=1-385.
DR   PDB; 1CQJ; X-ray; 2.90 A; B/E=1-385.
DR   PDB; 1JKJ; X-ray; 2.35 A; B/E=1-388.
DR   PDB; 1JLL; X-ray; 2.69 A; B/E=1-388.
DR   PDB; 1SCU; X-ray; 2.50 A; B/E=1-388.
DR   PDB; 2NU6; X-ray; 2.55 A; B/E=1-388.
DR   PDB; 2NU7; X-ray; 2.20 A; B/E=1-388.
DR   PDB; 2NU8; X-ray; 2.15 A; B/E=1-388.
DR   PDB; 2NU9; X-ray; 2.90 A; B/E/G/I=1-388.
DR   PDB; 2NUA; X-ray; 2.95 A; B/E=1-388.
DR   PDB; 2SCU; X-ray; 2.30 A; B/E=1-388.
DR   PDBsum; 1CQI; -.
DR   PDBsum; 1CQJ; -.
DR   PDBsum; 1JKJ; -.
DR   PDBsum; 1JLL; -.
DR   PDBsum; 1SCU; -.
DR   PDBsum; 2NU6; -.
DR   PDBsum; 2NU7; -.
DR   PDBsum; 2NU8; -.
DR   PDBsum; 2NU9; -.
DR   PDBsum; 2NUA; -.
DR   PDBsum; 2SCU; -.
DR   ProteinModelPortal; P0A836; -.
DR   SMR; P0A836; -.
DR   BioGrid; 4259946; 19.
DR   ComplexPortal; CPX-1092; Succinyl-CoA synthetase.
DR   DIP; DIP-31852N; -.
DR   IntAct; P0A836; 30.
DR   STRING; 316385.ECDH10B_0794; -.
DR   CarbonylDB; P0A836; -.
DR   SWISS-2DPAGE; P0A836; -.
DR   EPD; P0A836; -.
DR   jPOST; P0A836; -.
DR   PaxDb; P0A836; -.
DR   PRIDE; P0A836; -.
DR   EnsemblBacteria; AAC73822; AAC73822; b0728.
DR   EnsemblBacteria; BAA35394; BAA35394; BAA35394.
DR   GeneID; 945312; -.
DR   KEGG; ecj:JW0717; -.
DR   KEGG; eco:b0728; -.
DR   PATRIC; fig|1411691.4.peg.1545; -.
DR   EchoBASE; EB0974; -.
DR   EcoGene; EG10981; sucC.
DR   eggNOG; ENOG4105CMV; Bacteria.
DR   eggNOG; COG0045; LUCA.
DR   HOGENOM; HOG000007059; -.
DR   InParanoid; P0A836; -.
DR   KO; K01903; -.
DR   PhylomeDB; P0A836; -.
DR   BioCyc; EcoCyc:SUCCCOASYN-BETA; -.
DR   BioCyc; ECOL316407:JW0717-MONOMER; -.
DR   BioCyc; MetaCyc:SUCCCOASYN-BETA; -.
DR   BRENDA; 6.2.1.5; 2165.
DR   UniPathway; UPA00223; UER00999.
DR   EvolutionaryTrace; P0A836; -.
DR   PRO; PR:P0A836; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; HDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0009361; C:succinate-CoA ligase complex (ADP-forming); IDA:EcoCyc.
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; IMP:EcoliWiki.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IMP:EcoliWiki.
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   3D-structure; ATP-binding; Complete proteome;
KW   Direct protein sequencing; Ligase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Tricarboxylic acid cycle.
FT   CHAIN         1    388       Succinate--CoA ligase [ADP-forming]
FT                                subunit beta.
FT                                /FTId=PRO_0000102832.
FT   DOMAIN        9    244       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00558}.
FT   NP_BIND      53     55       ATP. {ECO:0000255|HAMAP-Rule:MF_00558,
FT                                ECO:0000269|PubMed:10625475}.
FT   REGION      321    323       Substrate binding; shared with subunit
FT                                alpha. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   METAL       199    199       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00558,
FT                                ECO:0000269|PubMed:10625475}.
FT   METAL       213    213       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00558,
FT                                ECO:0000269|PubMed:10625475}.
FT   BINDING      46     46       ATP. {ECO:0000255|HAMAP-Rule:MF_00558,
FT                                ECO:0000269|PubMed:10625475}.
FT   BINDING      99     99       ATP. {ECO:0000255|HAMAP-Rule:MF_00558,
FT                                ECO:0000269|PubMed:10625475}.
FT   BINDING     102    102       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00558,
FT                                ECO:0000269|PubMed:10625475}.
FT   BINDING     107    107       ATP. {ECO:0000255|HAMAP-Rule:MF_00558,
FT                                ECO:0000269|PubMed:10625475}.
FT   BINDING     264    264       Substrate; shared with subunit alpha.
FT                                {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   MUTAGEN     197    197       E->A: Prevents phosphorylation of the
FT                                enzyme intermediate in both reaction
FT                                directions.
FT                                {ECO:0000269|PubMed:11781092}.
FT   MUTAGEN     197    197       E->Q: Prevents phosphorylation of the
FT                                enzyme intermediate by ATP.
FT                                {ECO:0000269|PubMed:11781092}.
FT   HELIX         5     14       {ECO:0000244|PDB:2NU8}.
FT   STRAND       22     27       {ECO:0000244|PDB:2NU8}.
FT   HELIX        28     38       {ECO:0000244|PDB:2NU8}.
FT   STRAND       43     47       {ECO:0000244|PDB:2NU8}.
FT   STRAND       50     52       {ECO:0000244|PDB:2NU8}.
FT   TURN         54     58       {ECO:0000244|PDB:2NU8}.
FT   STRAND       60     63       {ECO:0000244|PDB:2NU8}.
FT   HELIX        66     76       {ECO:0000244|PDB:2NU8}.
FT   STRAND       79     81       {ECO:0000244|PDB:2NU8}.
FT   STRAND       96    100       {ECO:0000244|PDB:2NU8}.
FT   STRAND      104    115       {ECO:0000244|PDB:2NU8}.
FT   TURN        116    119       {ECO:0000244|PDB:2NU8}.
FT   STRAND      120    127       {ECO:0000244|PDB:2NU8}.
FT   HELIX       133    139       {ECO:0000244|PDB:2NU8}.
FT   HELIX       141    143       {ECO:0000244|PDB:2NU8}.
FT   STRAND      144    148       {ECO:0000244|PDB:2NU8}.
FT   TURN        151    153       {ECO:0000244|PDB:2NU8}.
FT   HELIX       157    166       {ECO:0000244|PDB:2NU8}.
FT   HELIX       172    190       {ECO:0000244|PDB:2NU8}.
FT   STRAND      193    204       {ECO:0000244|PDB:2NU8}.
FT   STRAND      209    212       {ECO:0000244|PDB:2NU8}.
FT   STRAND      215    218       {ECO:0000244|PDB:2NU8}.
FT   HELIX       220    225       {ECO:0000244|PDB:2NU8}.
FT   HELIX       227    232       {ECO:0000244|PDB:2NU8}.
FT   HELIX       235    237       {ECO:0000244|PDB:2NU8}.
FT   HELIX       240    247       {ECO:0000244|PDB:2NU8}.
FT   STRAND      251    254       {ECO:0000244|PDB:2NU8}.
FT   STRAND      256    265       {ECO:0000244|PDB:2NU8}.
FT   HELIX       266    278       {ECO:0000244|PDB:2NU8}.
FT   STRAND      285    288       {ECO:0000244|PDB:2NU8}.
FT   HELIX       295    306       {ECO:0000244|PDB:2NU8}.
FT   STRAND      308    310       {ECO:0000244|PDB:2SCU}.
FT   STRAND      313    320       {ECO:0000244|PDB:2NU8}.
FT   STRAND      321    323       {ECO:0000244|PDB:1JLL}.
FT   HELIX       325    339       {ECO:0000244|PDB:2NU8}.
FT   STRAND      345    351       {ECO:0000244|PDB:2NU8}.
FT   HELIX       354    362       {ECO:0000244|PDB:2NU8}.
FT   STRAND      366    370       {ECO:0000244|PDB:2NU8}.
FT   HELIX       374    384       {ECO:0000244|PDB:2NU8}.
FT   TURN        385    387       {ECO:0000244|PDB:2NU8}.
SQ   SEQUENCE   388 AA;  41393 MW;  09C429EC97A823CF CRC64;
     MNLHEYQAKQ LFARYGLPAP VGYACTTPRE AEEAASKIGA GPWVVKCQVH AGGRGKAGGV
     KVVNSKEDIR AFAENWLGKR LVTYQTDANG QPVNQILVEA ATDIAKELYL GAVVDRSSRR
     VVFMASTEGG VEIEKVAEET PHLIHKVALD PLTGPMPYQG RELAFKLGLE GKLVQQFTKI
     FMGLATIFLE RDLALIEINP LVITKQGDLI CLDGKLGADG NALFRQPDLR EMRDQSQEDP
     REAQAAQWEL NYVALDGNIG CMVNGAGLAM GTMDIVKLHG GEPANFLDVG GGATKERVTE
     AFKIILSDDK VKAVLVNIFG GIVRCDLIAD GIIGAVAEVG VNVPVVVRLE GNNAELGAKK
     LADSGLNIIA AKGLTDAAQQ VVAAVEGK
//
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