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Database: UniProt
Entry: A0A0G1WJN3_9BACT
LinkDB: A0A0G1WJN3_9BACT
Original site: A0A0G1WJN3_9BACT 
ID   A0A0G1WJN3_9BACT        Unreviewed;       300 AA.
AC   A0A0G1WJN3;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   25-OCT-2017, entry version 15.
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   ORFNames=UY61_C0074G0003 {ECO:0000313|EMBL:KKW18810.1};
OS   Candidatus Adlerbacteria bacterium GW2011_GWC1_50_9.
OC   Bacteria; Candidatus Adlerbacteria.
OX   NCBI_TaxID=1618608 {ECO:0000313|EMBL:KKW18810.1, ECO:0000313|Proteomes:UP000034201};
RN   [1] {ECO:0000313|EMBL:KKW18810.1, ECO:0000313|Proteomes:UP000034201}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a
RT   large radiation of phyla.";
RL   Nature 0:0-0(2015).
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   -!- CATALYTIC ACTIVITY: ATP + succinate + CoA = ADP + phosphate +
CC       succinyl-CoA. {ECO:0000256|HAMAP-Rule:MF_01988}.
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       succinate from succinyl-CoA (ligase route): step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_01988}.
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits.
CC       {ECO:0000256|HAMAP-Rule:MF_01988}.
CC   -!- SIMILARITY: Belongs to the succinate/malate CoA ligase alpha
CC       subunit family. {ECO:0000256|HAMAP-Rule:MF_01988}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01988}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KKW18810.1}.
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DR   EMBL; LCQQ01000074; KKW18810.1; -; Genomic_DNA.
DR   EnsemblBacteria; KKW18810; KKW18810; UY61_C0074G0003.
DR   PATRIC; fig|1618608.3.peg.869; -.
DR   UniPathway; UPA00223; UER00999.
DR   Proteomes; UP000034201; Unassembled WGS sequence.
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; IPR033847; Citrt_syn/SCS-alpha_CS.
DR   InterPro; IPR003781; CoA-bd.
DR   InterPro; IPR005810; CoA_lig_alpha.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032875; Succ_CoA_lig_flav_dom.
DR   InterPro; IPR016102; Succinyl-CoA_synth-like.
DR   Pfam; PF02629; CoA_binding; 1.
DR   Pfam; PF13607; Succ_CoA_lig; 1.
DR   PIRSF; PIRSF001553; SucCS_alpha; 1.
DR   SMART; SM00881; CoA_binding; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF52210; SSF52210; 1.
DR   PROSITE; PS01216; SUCCINYL_COA_LIG_1; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000034201};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01988};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01988};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034201};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_01988}.
FT   DOMAIN        4    101       CoA_binding. {ECO:0000259|SMART:SM00881}.
FT   REGION       17     20       Coenzyme A binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01988}.
FT   REGION       97     99       Coenzyme A binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01988}.
FT   ACT_SITE    257    257       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}.
SQ   SEQUENCE   300 AA;  31294 MW;  29F31D754B2213E5 CRC64;
     MSILVDKKTR VLIQGITGHE GARACREMLS YGTRVLAGVT PGKGGRKIEG VPVYDGIREA
     ILRHPGINTS LIAVPALFVR DAAAEAIKNK ISLINILTEH VTVRDSAWIV ARSRSRGVRV
     VGPSSVGIIS PGKGKVGSIG SSAVEKKIFS PGPVGIISKS GGMTAEIGVL LTRAGIGQST
     AVGIGGDPII GSDFADLLTL FERDPATQAV VLFGEVGGSY EEEAARLISQ RKFTKPVVAI
     IAGYFTKDIA PATVLGHAGA IVSRGRGGYY SKVLALKKAG VHVASTLEDI PKIIKSILRL
//
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