SUCD_HAEIN
ID SUCD_HAEIN Reviewed; 293 AA.
AC P45102;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Succinate--CoA ligase [ADP-forming] subunit alpha {ECO:0000255|HAMAP-Rule:MF_01988};
DE EC=6.2.1.5 {ECO:0000255|HAMAP-Rule:MF_01988};
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}; OrderedLocusNames=HI_1197;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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.
CC {ECO:0000255|HAMAP-Rule:MF_01988}.
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:0000255|HAMAP-
CC Rule:MF_01988};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC from succinyl-CoA (ligase route): step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_01988}.
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits.
CC {ECO:0000255|HAMAP-Rule:MF_01988}.
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; L42023; AAC22851.1; -; Genomic_DNA.
DR PIR; D64189; D64189.
DR RefSeq; NP_439353.1; NC_000907.1.
DR RefSeq; WP_005694247.1; NC_000907.1.
DR AlphaFoldDB; P45102; -.
DR SMR; P45102; -.
DR STRING; 71421.HI_1197; -.
DR PRIDE; P45102; -.
DR EnsemblBacteria; AAC22851; AAC22851; HI_1197.
DR KEGG; hin:HI_1197; -.
DR PATRIC; fig|71421.8.peg.1249; -.
DR eggNOG; COG0074; Bacteria.
DR HOGENOM; CLU_052104_0_0_6; -.
DR OMA; VIICITE; -.
DR PhylomeDB; P45102; -.
DR BioCyc; HINF71421:G1GJ1-1228-MON; -.
DR UniPathway; UPA00223; UER00999.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0009361; C:succinate-CoA ligase complex (ADP-forming); IBA:GO_Central.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IBA:GO_Central.
DR GO; GO:0004776; F:succinate-CoA ligase (GDP-forming) activity; IBA:GO_Central.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
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;
KW Ligase; Nucleotide-binding; Reference proteome; Tricarboxylic acid cycle.
FT CHAIN 1..293
FT /note="Succinate--CoA ligase [ADP-forming] subunit alpha"
FT /id="PRO_0000102794"
FT ACT_SITE 247
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01988"
FT BINDING 17..20
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01988"
FT BINDING 43
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01988"
FT BINDING 96..98
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01988"
FT BINDING 159
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit beta"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01988"
SQ SEQUENCE 293 AA; 30389 MW; E9C4AF5D3F3D9FE1 CRC64;
MAILIDKNTK VICQGFTGGQ GTFHSEQALA YGTQLVGGVS PNKGGTTHLG LPVFNTVREA
VENTGVTATV IYVPASFCKD AIIEAIDAGI QLIVCITEGI PTLDMLKVKQ KLNETGVVMI
GPNCPGVITP DECKIGIMPA HIHKKGKVGI VSRSGTLTYE AVKQTTDEGF GQSTCVGIGG
DPIPGSSFID ILERFQQDPE TEAIVMIGEI GGSAEEEAAI FIKDNVTKPV VAYIAGITAP
KGKRMGHAGA IISGGKGTAV EKIAALEAAG VTCVKSLAEI GEALRKLLKS SKN
