(data stored in SCRATCH zone)

SWISSPROT: Q13DR2_RHOPS

ID   Q13DR2_RHOPS            Unreviewed;       294 AA.
AC   Q13DR2;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   08-MAY-2019, entry version 94.
DE   RecName: Full=Succinate--CoA ligase [ADP-forming] subunit alpha {ECO:0000256|HAMAP-Rule:MF_01988};
DE            EC=6.2.1.5 {ECO:0000256|HAMAP-Rule:MF_01988};
DE   AltName: Full=Succinyl-CoA synthetase subunit alpha {ECO:0000256|HAMAP-Rule:MF_01988};
DE            Short=SCS-alpha {ECO:0000256|HAMAP-Rule:MF_01988};
GN   Name=sucD {ECO:0000256|HAMAP-Rule:MF_01988};
GN   OrderedLocusNames=RPD_0539 {ECO:0000313|EMBL:ABE37777.1};
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE37777.1, ECO:0000313|Proteomes:UP000001818};
RN   [1] {ECO:0000313|EMBL:ABE37777.1, ECO:0000313|Proteomes:UP000001818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5 {ECO:0000313|EMBL:ABE37777.1,
RC   ECO:0000313|Proteomes:UP000001818};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-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 alpha subunit
CC       of the enzyme binds the substrates coenzyme A and phosphate, while
CC       succinate binding and nucleotide specificity is provided by the
CC       beta subunit. {ECO:0000256|HAMAP-Rule:MF_01988,
CC       ECO:0000256|RuleBase:RU000699}.
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_01988, ECO:0000256|RuleBase:RU000699};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       succinate from succinyl-CoA (ligase route): step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_01988, ECO:0000256|RuleBase:RU000699}.
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits.
CC       {ECO:0000256|HAMAP-Rule:MF_01988, ECO:0000256|RuleBase:RU000699}.
CC   -!- SIMILARITY: Belongs to the succinate/malate CoA ligase alpha
CC       subunit family. {ECO:0000256|HAMAP-Rule:MF_01988,
CC       ECO:0000256|RuleBase:RU000677}.
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DR   EMBL; CP000283; ABE37777.1; -; Genomic_DNA.
DR   RefSeq; WP_011500964.1; NC_007958.1.
DR   STRING; 316057.RPD_0539; -.
DR   EnsemblBacteria; ABE37777; ABE37777; RPD_0539.
DR   KEGG; rpd:RPD_0539; -.
DR   eggNOG; ENOG4105CH8; Bacteria.
DR   eggNOG; COG0074; LUCA.
DR   HOGENOM; HOG000239685; -.
DR   KO; K01902; -.
DR   OMA; IIFVPPA; -.
DR   OrthoDB; 1081709at2; -.
DR   BioCyc; RPAL316057:RPD_RS02760-MONOMER; -.
DR   UniPathway; UPA00223; UER00999.
DR   Proteomes; UP000001818; Chromosome.
DR   GO; GO:0048037; F:cofactor binding; IEA:InterPro.
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: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   3: Inferred from homology;
DR   PRODOM; Q13DR2.
DR   SWISS-2DPAGE; Q13DR2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001818};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01988,
KW   ECO:0000256|RuleBase:RU000677, ECO:0000313|EMBL:ABE37777.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01988,
KW   ECO:0000256|RuleBase:RU000699};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_01988,
KW   ECO:0000256|RuleBase:RU000699}.
FT   DOMAIN        4    100       CoA_binding. {ECO:0000259|SMART:SM00881}.
FT   REGION       17     20       Coenzyme A binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01988}.
FT   REGION       96     98       Coenzyme A binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01988}.
FT   ACT_SITE    251    251       Tele-phosphohistidine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01988,
FT                                ECO:0000256|PIRSR:PIRSR001553-1}.
FT   BINDING      43     43       Coenzyme A. {ECO:0000256|HAMAP-Rule:
FT                                MF_01988}.
FT   BINDING     159    159       Substrate; shared with subunit beta.
FT                                {ECO:0000256|HAMAP-Rule:MF_01988}.
SQ   SEQUENCE   294 AA;  30051 MW;  27369B19FF1475D5 CRC64;
     MSILIDANTK VICQGFTGKN GTFHSEAAVA YGTKMVGGTS PGKGGTTHLG LPVFDTVREA
     RDKTGADASV IYVPPPGAAD AICEAIDAEI PLIVCITEGI PVLDMVRVKR SLVGSKSRLI
     GPNCPGVMTA GECKIGIMPA NIFKQGSVGI VSRSGTLTYE AVFQTTSEGL GQTTAVGIGG
     DPVKGTEFID VLEMFLADDK TTSIIMIGEI GGSAEEEAAQ FLIDEAKRGR KKPMVGFIAG
     VTAPPGRRMG HAGAIISGGK GDAASKTSAM EAAGITVSPS PARLGKTLVE VLKG
//

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