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Database: UniProt
Entry: P53590
LinkDB: P53590
Original site: P53590 
ID   SUCB2_PIG               Reviewed;         433 AA.
AC   P53590; Q95279;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2002, sequence version 2.
DT   16-JAN-2019, entry version 146.
DE   RecName: Full=Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03221};
DE            EC=6.2.1.4 {ECO:0000255|HAMAP-Rule:MF_03221, ECO:0000269|PubMed:27487822, ECO:0000269|PubMed:8401211};
DE   AltName: Full=GTP-specific succinyl-CoA synthetase subunit beta {ECO:0000255|HAMAP-Rule:MF_03221};
DE            Short=G-SCS {ECO:0000255|HAMAP-Rule:MF_03221};
DE            Short=GTPSCS {ECO:0000255|HAMAP-Rule:MF_03221};
DE   AltName: Full=Succinyl-CoA synthetase beta-G chain {ECO:0000255|HAMAP-Rule:MF_03221};
DE            Short=SCS-betaG {ECO:0000255|HAMAP-Rule:MF_03221};
DE   Flags: Precursor; Fragment;
GN   Name=SUCLG2 {ECO:0000255|HAMAP-Rule:MF_03221};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC   Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-41, FUNCTION, AND
RP   CATALYTIC ACTIVITY.
RC   TISSUE=Heart;
RX   PubMed=8401211; DOI=10.1002/pro.5560020808;
RA   Bailey D.L., Wolodko W.T., Bridger W.A.;
RT   "Cloning, characterization, and expression of the beta subunit of pig
RT   heart succinyl-CoA synthetase.";
RL   Protein Sci. 2:1255-1262(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-82.
RC   TISSUE=Small intestine;
RX   PubMed=8672129; DOI=10.1007/s003359900153;
RA   Winteroe A.K., Fredholm M., Davies W.;
RT   "Evaluation and characterization of a porcine small intestine cDNA
RT   library: analysis of 839 clones.";
RL   Mamm. Genome 7:509-517(1996).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 39-433 IN COMPLEX WITH
RP   SUCLG1.
RX   PubMed=10873456; DOI=10.1006/jmbi.2000.3807;
RA   Fraser M.E., James M.N., Bridger W.A., Wolodko W.T.;
RT   "Phosphorylated and dephosphorylated structures of pig heart, GTP-
RT   specific succinyl-CoA synthetase.";
RL   J. Mol. Biol. 299:1325-1339(2000).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 40-433 IN COMPLEX WITH
RP   SUCLG1; GTP AND POTASSIUM.
RX   PubMed=16481318; DOI=10.1074/jbc.M511785200;
RA   Fraser M.E., Hayakawa K., Hume M.S., Ryan D.G., Brownie E.R.;
RT   "Interactions of GTP with the ATP-grasp domain of GTP-specific
RT   succinyl-CoA synthetase.";
RL   J. Biol. Chem. 281:11058-11065(2006).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 40-433 IN COMPLEX WITH
RP   SUCLG1.
RX   PubMed=26249701; DOI=10.1107/S2053230X15011188;
RA   Huang J., Malhi M., Deneke J., Fraser M.E.;
RT   "Structure of GTP-specific succinyl-CoA synthetase in complex with
RT   CoA.";
RL   Acta Crystallogr. F Struct. Biol. Commun. 71:1067-1071(2015).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 40-433 IN COMPLEX WITH
RP   SUCLG1 AND SUCCINATE, FUNCTION, CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=27487822; DOI=10.1107/S2059798316010044;
RA   Huang J., Fraser M.E.;
RT   "Structural basis for the binding of succinate to succinyl-CoA
RT   synthetase.";
RL   Acta Crystallogr. D 72:912-921(2016).
CC   -!- FUNCTION: GTP-specific succinyl-CoA synthetase functions in the
CC       citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA
CC       to the synthesis of GTP and thus represents the only step of
CC       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_03221, ECO:0000269|PubMed:27487822,
CC       ECO:0000269|PubMed:8401211}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CoA + GTP + succinate = GDP + phosphate + succinyl-CoA;
CC         Xref=Rhea:RHEA:22120, ChEBI:CHEBI:30031, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292,
CC         ChEBI:CHEBI:58189; EC=6.2.1.4; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03221, ECO:0000269|PubMed:27487822,
CC         ECO:0000269|PubMed:8401211};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03221};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_03221};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.76 mM for succinate {ECO:0000269|PubMed:27487822};
CC         Vmax=5.99 umol/min/mg enzyme {ECO:0000269|PubMed:27487822};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       succinate from succinyl-CoA (ligase route): step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_03221, ECO:0000305|PubMed:8401211}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The beta
CC       subunit determines specificity for GTP. {ECO:0000255|HAMAP-
CC       Rule:MF_03221, ECO:0000269|PubMed:10873456,
CC       ECO:0000269|PubMed:16481318, ECO:0000269|PubMed:26249701,
CC       ECO:0000269|PubMed:27487822}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-
CC       Rule:MF_03221}.
CC   -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta
CC       subunit family. GTP-specific subunit beta subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_03221}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA31120.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; L06944; AAA31120.1; ALT_INIT; mRNA.
DR   EMBL; Z81187; CAB03559.1; -; mRNA.
DR   PIR; A44529; A44529.
DR   UniGene; Ssc.12108; -.
DR   PDB; 1EUC; X-ray; 2.10 A; B=39-433.
DR   PDB; 1EUD; X-ray; 2.10 A; B=39-433.
DR   PDB; 2FP4; X-ray; 2.08 A; B=40-433.
DR   PDB; 2FPG; X-ray; 2.96 A; B=40-433.
DR   PDB; 2FPI; X-ray; 2.70 A; B=40-433.
DR   PDB; 2FPP; X-ray; 2.35 A; B=40-433.
DR   PDB; 4XX0; X-ray; 2.10 A; B=40-433.
DR   PDB; 5CAE; X-ray; 2.20 A; B=40-433.
DR   PDBsum; 1EUC; -.
DR   PDBsum; 1EUD; -.
DR   PDBsum; 2FP4; -.
DR   PDBsum; 2FPG; -.
DR   PDBsum; 2FPI; -.
DR   PDBsum; 2FPP; -.
DR   PDBsum; 4XX0; -.
DR   PDBsum; 5CAE; -.
DR   ProteinModelPortal; P53590; -.
DR   SMR; P53590; -.
DR   CORUM; P53590; -.
DR   MINT; P53590; -.
DR   STRING; 9823.ENSSSCP00000012257; -.
DR   PaxDb; P53590; -.
DR   PeptideAtlas; P53590; -.
DR   PRIDE; P53590; -.
DR   eggNOG; KOG2799; Eukaryota.
DR   eggNOG; COG0045; LUCA.
DR   HOGENOM; HOG000007059; -.
DR   HOVERGEN; HBG055555; -.
DR   InParanoid; P53590; -.
DR   SABIO-RK; P53590; -.
DR   UniPathway; UPA00223; UER00999.
DR   EvolutionaryTrace; P53590; -.
DR   Proteomes; UP000008227; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004776; F:succinate-CoA ligase (GDP-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006104; P:succinyl-CoA metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.40.50.261; -; 1.
DR   HAMAP; MF_00558; Succ_CoA_beta; 1.
DR   HAMAP; MF_03221; Succ_CoA_betaG_euk; 1.
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; IPR034722; Succ_CoA_betaG_euk.
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; PS01217; SUCCINYL_COA_LIG_3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Complete proteome;
KW   Direct protein sequencing; GTP-binding; Ligase; Magnesium;
KW   Metal-binding; Mitochondrion; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT      <1     38       Mitochondrion.
FT   CHAIN        39    433       Succinate--CoA ligase [GDP-forming]
FT                                subunit beta, mitochondrial.
FT                                {ECO:0000255|HAMAP-Rule:MF_03221}.
FT                                /FTId=PRO_0000033358.
FT   DOMAIN       47    275       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_03221}.
FT   NP_BIND      91     93       GTP. {ECO:0000255|HAMAP-Rule:MF_03221,
FT                                ECO:0000269|PubMed:16481318}.
FT   REGION      366    368       Substrate binding; shared with subunit
FT                                alpha. {ECO:0000255|HAMAP-Rule:MF_03221,
FT                                ECO:0000269|PubMed:27487822}.
FT   METAL       244    244       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_03221,
FT                                ECO:0000305|PubMed:16481318}.
FT   METAL       258    258       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_03221,
FT                                ECO:0000305|PubMed:16481318}.
FT   BINDING      58     58       GTP. {ECO:0000255|HAMAP-Rule:MF_03221,
FT                                ECO:0000269|PubMed:16481318}.
FT   BINDING     147    147       GTP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-Rule:MF_03221,
FT                                ECO:0000269|PubMed:16481318}.
FT   BINDING     309    309       Substrate; shared with subunit alpha.
FT                                {ECO:0000255|HAMAP-Rule:MF_03221,
FT                                ECO:0000269|PubMed:27487822}.
FT   SITE         80     80       Important for substrate specificity.
FT                                {ECO:0000255|HAMAP-Rule:MF_03221}.
FT   SITE        148    148       Important for substrate specificity.
FT                                {ECO:0000255|HAMAP-Rule:MF_03221}.
FT   MOD_RES      74     74       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q9Z2I8}.
FT   MOD_RES      79     79       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:Q9Z2I8}.
FT   MOD_RES     133    133       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q9Z2I8}.
FT   MOD_RES     140    140       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q9Z2I8}.
FT   MOD_RES     162    162       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9Z2I8}.
FT   MOD_RES     201    201       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q9Z2I8}.
FT   MOD_RES     228    228       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q96I99}.
FT   MOD_RES     272    272       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q9Z2I8}.
FT   MOD_RES     292    292       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q96I99}.
FT   MOD_RES     339    339       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:Q9Z2I8}.
FT   MOD_RES     348    348       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q9Z2I8}.
FT   MOD_RES     387    387       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q9Z2I8}.
FT   MOD_RES     424    424       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q9Z2I8}.
FT   NON_TER       1      1
FT   HELIX        43     52       {ECO:0000244|PDB:2FP4}.
FT   STRAND       60     65       {ECO:0000244|PDB:2FP4}.
FT   HELIX        66     76       {ECO:0000244|PDB:2FP4}.
FT   STRAND       79     85       {ECO:0000244|PDB:2FP4}.
FT   STRAND       88     90       {ECO:0000244|PDB:2FP4}.
FT   HELIX        92     94       {ECO:0000244|PDB:2FP4}.
FT   STRAND      104    109       {ECO:0000244|PDB:2FP4}.
FT   HELIX       111    119       {ECO:0000244|PDB:2FP4}.
FT   TURN        120    123       {ECO:0000244|PDB:2FP4}.
FT   STRAND      124    127       {ECO:0000244|PDB:2FP4}.
FT   STRAND      141    145       {ECO:0000244|PDB:2FP4}.
FT   STRAND      150    160       {ECO:0000244|PDB:2FP4}.
FT   TURN        161    164       {ECO:0000244|PDB:2FP4}.
FT   STRAND      165    173       {ECO:0000244|PDB:2FP4}.
FT   HELIX       178    184       {ECO:0000244|PDB:2FP4}.
FT   HELIX       186    188       {ECO:0000244|PDB:2FP4}.
FT   STRAND      190    193       {ECO:0000244|PDB:2FP4}.
FT   TURN        196    198       {ECO:0000244|PDB:2FP4}.
FT   HELIX       202    211       {ECO:0000244|PDB:2FP4}.
FT   HELIX       216    235       {ECO:0000244|PDB:2FP4}.
FT   STRAND      238    248       {ECO:0000244|PDB:2FP4}.
FT   TURN        250    252       {ECO:0000244|PDB:1EUC}.
FT   STRAND      254    256       {ECO:0000244|PDB:2FP4}.
FT   STRAND      258    263       {ECO:0000244|PDB:2FP4}.
FT   HELIX       265    270       {ECO:0000244|PDB:2FP4}.
FT   HELIX       272    275       {ECO:0000244|PDB:2FP4}.
FT   STRAND      281    283       {ECO:0000244|PDB:2FPI}.
FT   HELIX       285    292       {ECO:0000244|PDB:2FP4}.
FT   STRAND      296    299       {ECO:0000244|PDB:2FP4}.
FT   STRAND      301    310       {ECO:0000244|PDB:2FP4}.
FT   HELIX       311    323       {ECO:0000244|PDB:2FP4}.
FT   STRAND      330    333       {ECO:0000244|PDB:2FP4}.
FT   HELIX       340    352       {ECO:0000244|PDB:2FP4}.
FT   STRAND      358    368       {ECO:0000244|PDB:2FP4}.
FT   HELIX       370    384       {ECO:0000244|PDB:2FP4}.
FT   STRAND      390    396       {ECO:0000244|PDB:2FP4}.
FT   HELIX       399    408       {ECO:0000244|PDB:2FP4}.
FT   STRAND      411    415       {ECO:0000244|PDB:1EUC}.
FT   HELIX       419    428       {ECO:0000244|PDB:2FP4}.
SQ   SEQUENCE   433 AA;  46803 MW;  AA04B72BC1B80E24 CRC64;
     IPAAPVAAQA RKLLRDLAFR PPLLAARSQV VQLTPRRWLN LQEYQSKKLM SDNGVKVQRF
     FVADTANEAL EAAKRLNAKE IVLKAQILAG GRGKGVFSSG LKGGVHLTKD PEVVGQLAKQ
     MIGYNLATKQ TPKEGVKVNK VMVAEALDIS RETYLAILMD RSCNGPVLVG SPQGGVDIEE
     VAASNPELIF KEQIDIIEGI KDSQAQRMAE NLGFLGPLQN QAADQIKKLY NLFLKIDATQ
     VEVNPFGETP EGQVVCFDAK INFDDNAEFR QKDIFAMDDK SENEPIENEA AKYDLKYIGL
     DGNIACFVNG AGLAMATCDI IFLNGGKPAN FLDLGGGVKE SQVYQAFKLL TADPKVEAIL
     VNIFGGIVNC AIIANGITKA CRELELKVPL VVRLEGTNVH EAQNILTNSG LPITSAVDLE
     DAAKKAVASV TKK
//
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