SUCA_YEAST
ID SUCA_YEAST Reviewed; 329 AA.
AC P53598; D6W2J8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Succinate--CoA ligase [ADP-forming] subunit alpha, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03222, ECO:0000305|PubMed:9874242};
DE EC=6.2.1.5 {ECO:0000255|HAMAP-Rule:MF_03222, ECO:0000269|PubMed:9874242};
DE AltName: Full=Succinyl-CoA synthetase subunit alpha {ECO:0000255|HAMAP-Rule:MF_03222};
DE Short=SCS-alpha {ECO:0000255|HAMAP-Rule:MF_03222};
DE Flags: Precursor;
GN Name=LSC1 {ECO:0000303|PubMed:9874242};
GN OrderedLocusNames=YOR142W {ECO:0000312|SGD:S000005668}; ORFNames=YOR3352W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9200815;
RX DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i;
RA Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
RA Schwager C., Paces V., Sander C., Ansorge W.;
RT "DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
RL Yeast 13:655-672(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RX PubMed=9874242; DOI=10.1046/j.1432-1327.1998.2580736.x;
RA Przybyla-Zawislak B., Dennis R.A., Zakharkin S.O., McCammon M.T.;
RT "Genes of succinyl-CoA ligase from Saccharomyces cerevisiae.";
RL Eur. J. Biochem. 258:736-743(1998).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=17761666; DOI=10.1074/mcp.m700098-mcp200;
RA Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,
RA van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.;
RT "Profiling phosphoproteins of yeast mitochondria reveals a role of
RT phosphorylation in assembly of the ATP synthase.";
RL Mol. Cell. Proteomics 6:1896-1906(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: Succinyl-CoA synthetase functions in the citric acid cycle
CC (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP
CC and thus represents the only step of substrate-level phosphorylation in
CC the TCA (PubMed:9874242). 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 {ECO:0000255|HAMAP-Rule:MF_03222, ECO:0000269|PubMed:9874242}.
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_03222, ECO:0000269|PubMed:9874242};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC from succinyl-CoA (ligase route): step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_03222, ECO:0000305|PubMed:9874242}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC {ECO:0000255|HAMAP-Rule:MF_03222}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03222,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}.
CC -!- INDUCTION: Induced during growth on nonfermentable carbon sources and
CC repressed during growth on glucose. {ECO:0000269|PubMed:9874242}.
CC -!- MISCELLANEOUS: Present with 18400 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase alpha subunit
CC family. {ECO:0000255|HAMAP-Rule:MF_03222}.
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DR EMBL; X94335; CAA64059.1; -; Genomic_DNA.
DR EMBL; Z75050; CAA99342.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10914.1; -; Genomic_DNA.
DR PIR; S61696; S61696.
DR RefSeq; NP_014785.3; NM_001183561.3.
DR AlphaFoldDB; P53598; -.
DR SMR; P53598; -.
DR BioGRID; 34536; 169.
DR ComplexPortal; CPX-1379; Mitochondrial succinyl-CoA synthetase complex.
DR DIP; DIP-6542N; -.
DR IntAct; P53598; 8.
DR MINT; P53598; -.
DR STRING; 4932.YOR142W; -.
DR iPTMnet; P53598; -.
DR UCD-2DPAGE; P53598; -.
DR MaxQB; P53598; -.
DR PaxDb; P53598; -.
DR PRIDE; P53598; -.
DR EnsemblFungi; YOR142W_mRNA; YOR142W; YOR142W.
DR GeneID; 854310; -.
DR KEGG; sce:YOR142W; -.
DR SGD; S000005668; LSC1.
DR VEuPathDB; FungiDB:YOR142W; -.
DR eggNOG; KOG1255; Eukaryota.
DR GeneTree; ENSGT00940000156351; -.
DR HOGENOM; CLU_052104_0_0_1; -.
DR InParanoid; P53598; -.
DR OMA; VIICITE; -.
DR BioCyc; YEAST:YOR142W-MON; -.
DR Reactome; R-SCE-71403; Citric acid cycle (TCA cycle).
DR UniPathway; UPA00223; UER00999.
DR PRO; PR:P53598; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P53598; protein.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
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; IDA:SGD.
DR GO; GO:0004776; F:succinate-CoA ligase (GDP-forming) activity; IBA:GO_Central.
DR GO; GO:1901289; P:succinyl-CoA catabolic process; IC:ComplexPortal.
DR GO; GO:0006104; P:succinyl-CoA metabolic process; IDA:SGD.
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 PROSITE; PS01216; SUCCINYL_COA_LIG_1; 1.
DR PROSITE; PS00399; SUCCINYL_COA_LIG_2; 1.
PE 1: Evidence at protein level;
KW Ligase; Mitochondrion; Nucleotide-binding; Reference proteome;
KW Transit peptide; Tricarboxylic acid cycle.
FT TRANSIT 1..24
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT CHAIN 25..329
FT /note="Succinate--CoA ligase [ADP-forming] subunit alpha,
FT mitochondrial"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT /id="PRO_0000033351"
FT ACT_SITE 284
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT BINDING 45..48
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT BINDING 71
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT BINDING 124..126
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT BINDING 189
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit beta"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
SQ SEQUENCE 329 AA; 35032 MW; 17DD3AFC47E92644 CRC64;
MLRSTVSKAS LKICRHFHRE SIPYDKTIKN LLLPKDTKVI FQGFTGKQGT FHASISQEYG
TNVVGGTNPK KAGQTHLGQP VFASVKDAIK ETGATASAIF VPPPIAAAAI KESIEAEIPL
AVCITEGIPQ HDMLYIAEML QTQDKTRLVG PNCPGIINPA TKVRIGIQPP KIFQAGKIGI
ISRSGTLTYE AVQQTTKTDL GQSLVIGMGG DAFPGTDFID ALKLFLEDET TEGIIMLGEI
GGKAEIEAAQ FLKEYNFSRS KPMPVASFIA GTVAGQMKGV RMGHSGAIVE GSGTDAESKK
QALRDVGVAV VESPGYLGQA LLDQFAKFK
