(data stored in ACNUC7421 zone)

SWISSPROT: A1AZH6_PARDP

ID   A1AZH6_PARDP            Unreviewed;       294 AA.
AC   A1AZH6;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, 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=Pden_0558 {ECO:0000313|EMBL:ABL68670.1};
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL68670.1, ECO:0000313|Proteomes:UP000000361};
RN   [1] {ECO:0000313|Proteomes:UP000000361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
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., Munk A.C., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J.,
RA   van Spanning R.J.M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans
RT   PD1222.";
RL   Submitted (DEC-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; CP000489; ABL68670.1; -; Genomic_DNA.
DR   RefSeq; WP_011746903.1; NC_008686.1.
DR   STRING; 318586.Pden_0558; -.
DR   PRIDE; A1AZH6; -.
DR   EnsemblBacteria; ABL68670; ABL68670; Pden_0558.
DR   KEGG; pde:Pden_0558; -.
DR   eggNOG; ENOG4105CH8; Bacteria.
DR   eggNOG; COG0074; LUCA.
DR   HOGENOM; HOG000239685; -.
DR   KO; K01902; -.
DR   OMA; IIFVPPA; -.
DR   BioCyc; PDEN318586:G1GW1-560-MONOMER; -.
DR   UniPathway; UPA00223; UER00999.
DR   Proteomes; UP000000361; Chromosome 1.
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; A1AZH6.
DR   SWISS-2DPAGE; A1AZH6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000361};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01988,
KW   ECO:0000256|RuleBase:RU000677, ECO:0000313|EMBL:ABL68670.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01988,
KW   ECO:0000256|RuleBase:RU000699};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000361};
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;  30234 MW;  0F6AD3E310118EAE CRC64;
     MAVLVNKDTK VICQGITGSQ GTFHTEQAIA YGTQMVGGVT PGKGGTEHLG LPVFNSVHEA
     VAKTGANATA IYVPPPFAAD SILEAIDAEI PLIVAITEGI PVLDMMKVKR ALEGSKSLLI
     GPNCPGIMTP DECKIGIMPG SIFKRGSVGV VSRSGTLTYE AVKQTSDVGL GQSSAVGIGG
     DPIKGMEHID VLRMFLDDPE TESIIMIGEI GGSAEEEAAE FLAEQKRKGK WKPTAGFIAG
     RTAPKGRRMG HAGAIVSGGK GDAESKIEAM KSAGIVVADS PAGLGEAVLK ALGR
//

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