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SUCD_THETH
ID   SUCD_THETH              Reviewed;         288 AA.
AC   P09143;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Succinate--CoA ligase [GDP-forming] subunit alpha {ECO:0000305|PubMed:22751660};
DE            EC=6.2.1.4 {ECO:0000269|PubMed:22751660};
DE   AltName: Full=Succinyl-CoA synthetase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01988};
DE            Short=SCS-alpha {ECO:0000255|HAMAP-Rule:MF_01988};
GN   Name=sucD {ECO:0000255|HAMAP-Rule:MF_01988}; Synonyms=scsA;
OS   Thermus thermophilus.
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=B / NCIMB 11247;
RX   PubMed=3186449; DOI=10.1093/nar/16.20.9858;
RA   Nicholls D.J., Sundaram T.K., Atkinson T., Minton N.P.;
RT   "Nucleotide sequence of the succinyl-CoA synthetase alpha-subunit from
RT   Thermus aquaticus B.";
RL   Nucleic Acids Res. 16:9858-9858(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=B / NCIMB 11247;
RX   PubMed=2204576; DOI=10.1016/0378-1097(90)90093-6;
RA   Nicholls D.J., Sundaram T.K., Atkinson T., Minton N.P.;
RT   "Cloning and nucleotide sequences of the mdh and sucD genes from Thermus
RT   aquaticus B.";
RL   FEMS Microbiol. Lett. 58:7-14(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33923 / DSM 674 / AT-62;
RX   PubMed=2034208; DOI=10.1007/bf00273580;
RA   Nishiyama M., Horinouchi S., Beppu T.;
RT   "Characterization of an operon encoding succinyl-CoA synthetase and malate
RT   dehydrogenase from Thermus flavus AT-62 and its expression in Escherichia
RT   coli.";
RL   Mol. Gen. Genet. 226:1-9(1991).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.23 ANGSTROMS).
RG   RIKEN structural genomics initiative (RSGI);
RT   "The crystal structure of succinyl-CoA synthetase from Thermus
RT   thermophilus.";
RL   Submitted (JUL-2003) to the PDB data bank.
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS), ACTIVE SITE, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX   PubMed=22751660; DOI=10.1107/s0907444912010852;
RA   Joyce M.A., Hayakawa K., Wolodko W.T., Fraser M.E.;
RT   "Biochemical and structural characterization of the GTP-preferring
RT   succinyl-CoA synthetase from Thermus aquaticus.";
RL   Acta Crystallogr. D 68:751-762(2012).
CC   -!- FUNCTION: Succinyl-CoA synthetase functions in the citric acid cycle
CC       (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of
CC       either ATP or GTP and thus represents the only step of substrate-level
CC       phosphorylation in the TCA. The alpha subunit of the enzyme binds the
CC       substrates coenzyme A and phosphate, while succinate binding and
CC       nucleotide specificity is provided by the beta subunit (By similarity).
CC       Can use either ATP or GTP, but prefers GTP (PubMed:22751660).
CC       {ECO:0000255|HAMAP-Rule:MF_01988, ECO:0000269|PubMed:22751660}.
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;
CC         Evidence={ECO:0000269|PubMed:22751660};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=121 uM for ATP {ECO:0000269|PubMed:22751660};
CC         KM=24 uM for GTP {ECO:0000269|PubMed:22751660};
CC         KM=1.4 mM for succinate {ECO:0000269|PubMed:22751660};
CC         KM=5.5 uM for CoA {ECO:0000269|PubMed:22751660};
CC       pH dependence:
CC         Optimum pH is 8.0-8.4. {ECO:0000269|PubMed:22751660};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC       from succinyl-CoA (ligase route): step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01988, ECO:0000305|PubMed:22751660}.
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_01988, ECO:0000269|PubMed:22751660}.
CC   -!- SIMILARITY: Belongs to the succinate/malate CoA ligase alpha subunit
CC       family. {ECO:0000255|HAMAP-Rule:MF_01988}.
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DR   EMBL; M35832; AAA27504.2; -; Genomic_DNA.
DR   EMBL; X56033; CAA39507.1; -; Genomic_DNA.
DR   EMBL; X54073; CAA38007.1; -; Genomic_DNA.
DR   RefSeq; WP_014509987.1; NZ_LR027517.1.
DR   PDB; 1OI7; X-ray; 1.23 A; A=1-288.
DR   PDB; 3UFX; X-ray; 2.35 A; A/D/F/H=1-288.
DR   PDBsum; 1OI7; -.
DR   PDBsum; 3UFX; -.
DR   AlphaFoldDB; P09143; -.
DR   SMR; P09143; -.
DR   UniPathway; UPA00223; UER00999.
DR   EvolutionaryTrace; P09143; -.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004776; F:succinate-CoA ligase (GDP-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.261; -; 1.
DR   HAMAP; MF_01988; Succ_CoA_alpha; 1.
DR   InterPro; IPR017440; Cit_synth/succinyl-CoA_lig_AS.
DR   InterPro; IPR033847; Citrt_syn/SCS-alpha_CS.
DR   InterPro; IPR003781; CoA-bd.
DR   InterPro; IPR005810; CoA_lig_alpha.
DR   InterPro; IPR005811; CoA_ligase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR016102; Succinyl-CoA_synth-like.
DR   Pfam; PF02629; CoA_binding; 1.
DR   Pfam; PF00549; Ligase_CoA; 1.
DR   PIRSF; PIRSF001553; SucCS_alpha; 1.
DR   SMART; SM00881; CoA_binding; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF52210; SSF52210; 1.
DR   TIGRFAMs; TIGR01019; sucCoAalpha; 1.
DR   PROSITE; PS01216; SUCCINYL_COA_LIG_1; 1.
DR   PROSITE; PS00399; SUCCINYL_COA_LIG_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Ligase; Nucleotide-binding; Tricarboxylic acid cycle.
FT   CHAIN           1..288
FT                   /note="Succinate--CoA ligase [GDP-forming] subunit alpha"
FT                   /id="PRO_0000102807"
FT   ACT_SITE        246
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01988,
FT                   ECO:0000269|PubMed:22751660"
FT   BINDING         16..19
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01988"
FT   BINDING         42
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01988"
FT   BINDING         95..97
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01988"
FT   BINDING         158
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared with subunit beta"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01988"
FT   CONFLICT        130..132
FT                   /note="EET -> HLP (in Ref. 1; AAA27504)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        157..158
FT                   /note="TY -> RH (in Ref. 1; AAA27504)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        183..185
FT                   /note="IGT -> RRL (in Ref. 1; AAA27504)"
FT                   /evidence="ECO:0000305"
FT   STRAND          9..13
FT                   /evidence="ECO:0007829|PDB:1OI7"
FT   TURN            14..16
FT                   /evidence="ECO:0007829|PDB:1OI7"
FT   HELIX           18..30
FT                   /evidence="ECO:0007829|PDB:1OI7"
FT   STRAND          33..38
FT                   /evidence="ECO:0007829|PDB:1OI7"
FT   STRAND          50..55
FT                   /evidence="ECO:0007829|PDB:1OI7"
FT   HELIX           56..62
FT                   /evidence="ECO:0007829|PDB:1OI7"
FT   STRAND          66..70
FT                   /evidence="ECO:0007829|PDB:1OI7"
FT   HELIX           74..86
FT                   /evidence="ECO:0007829|PDB:1OI7"
FT   STRAND          90..94
FT                   /evidence="ECO:0007829|PDB:1OI7"
FT   HELIX           101..114
FT                   /evidence="ECO:0007829|PDB:1OI7"
FT   STRAND          117..123
FT                   /evidence="ECO:0007829|PDB:1OI7"
FT   STRAND          125..128
FT                   /evidence="ECO:0007829|PDB:1OI7"
FT   TURN            129..131
FT                   /evidence="ECO:0007829|PDB:1OI7"
FT   STRAND          132..137
FT                   /evidence="ECO:0007829|PDB:1OI7"
FT   HELIX           139..141
FT                   /evidence="ECO:0007829|PDB:1OI7"
FT   STRAND          144..152
FT                   /evidence="ECO:0007829|PDB:1OI7"
FT   HELIX           154..166
FT                   /evidence="ECO:0007829|PDB:1OI7"
FT   STRAND          171..176
FT                   /evidence="ECO:0007829|PDB:1OI7"
FT   STRAND          179..181
FT                   /evidence="ECO:0007829|PDB:1OI7"
FT   HELIX           187..195
FT                   /evidence="ECO:0007829|PDB:1OI7"
FT   STRAND          202..207
FT                   /evidence="ECO:0007829|PDB:1OI7"
FT   STRAND          209..212
FT                   /evidence="ECO:0007829|PDB:1OI7"
FT   HELIX           213..224
FT                   /evidence="ECO:0007829|PDB:1OI7"
FT   STRAND          229..234
FT                   /evidence="ECO:0007829|PDB:1OI7"
FT   TURN            235..237
FT                   /evidence="ECO:0007829|PDB:3UFX"
FT   HELIX           258..268
FT                   /evidence="ECO:0007829|PDB:1OI7"
FT   HELIX           276..287
FT                   /evidence="ECO:0007829|PDB:1OI7"
SQ   SEQUENCE   288 AA;  29822 MW;  243A68469E78AF68 CRC64;
     MILVNRETRV LVQGITGREG QFHTKQMLDY GTKIVAGVTP GKGGTEVLGV PVYDTVKEAV
     AHHEVDASII FVPAPAAADA ALEAAHAGIP LIVLITEGIP TLDMVRAVEE IKALGSRLIG
     GNCPGIISAE ETKIGIMPGH VFKRGRVGII SRSGTLTYEA AAALSQAGLG TTTTVGIGGD
     PVIGTTFKDL LPLFNEDPET EAVVLIGEIG GSDEEEAAAW VKDHMKKPVV GFIGGRSAPK
     GKRMGHAGAI IMGNVGTPES KLRAFAEAGI PVADTIDEIV ELVKKALG
 
 
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