(data stored in SCRATCH zone)

SWISSPROT: Q758H3_ASHGO

ID   Q758H3_ASHGO            Unreviewed;       417 AA.
AC   Q758H3;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 111.
DE   RecName: Full=Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03219};
DE            EC=6.2.1.5 {ECO:0000256|HAMAP-Rule:MF_03219};
DE   AltName: Full=Succinyl-CoA synthetase beta chain {ECO:0000256|HAMAP-Rule:MF_03219};
DE            Short=SCS-beta {ECO:0000256|HAMAP-Rule:MF_03219};
GN   ORFNames=AGOS_AEL211W {ECO:0000313|EMBL:AAS52474.1};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS52474.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS52474.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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. The beta subunit provides nucleotide specificity of the enzyme
CC       and binds the substrate succinate, while the binding sites for coenzyme
CC       A and phosphate are found in the alpha subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_03219}.
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_03219};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03219};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_03219};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC       from succinyl-CoA (ligase route): step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_03219}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC       {ECO:0000256|HAMAP-Rule:MF_03219, ECO:0000256|RuleBase:RU361258}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03219}.
CC   -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta subunit
CC       family. {ECO:0000256|HAMAP-Rule:MF_03219,
CC       ECO:0000256|RuleBase:RU361258}.
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DR   EMBL; AE016818; AAS52474.1; -; Genomic_DNA.
DR   RefSeq; NP_984650.1; NM_210003.1.
DR   STRING; 33169.AAS52474; -.
DR   EnsemblFungi; AAS52474; AAS52474; AGOS_AEL211W.
DR   GeneID; 4620832; -.
DR   KEGG; ago:AGOS_AEL211W; -.
DR   HOGENOM; HOG000007059; -.
DR   InParanoid; Q758H3; -.
DR   KO; K01900; -.
DR   OMA; ITACDEV; -.
DR   UniPathway; UPA00223; UER00999.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0042709; C:succinate-CoA ligase complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IBA:GO_Central.
DR   GO; GO:0006104; P:succinyl-CoA metabolic process; IBA:GO_Central.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.40.50.261; -; 1.
DR   HAMAP; MF_00558; Succ_CoA_beta; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR005811; CoA_ligase.
DR   InterPro; IPR017866; Succ-CoA_synthase_bsu_CS.
DR   InterPro; IPR005809; Succ_CoA_synthase_bsu.
DR   InterPro; IPR016102; Succinyl-CoA_synth-like.
DR   PANTHER; PTHR11815; PTHR11815; 1.
DR   Pfam; PF08442; ATP-grasp_2; 1.
DR   Pfam; PF00549; Ligase_CoA; 1.
DR   PIRSF; PIRSF001554; SucCS_beta; 1.
DR   SUPFAM; SSF52210; SSF52210; 1.
DR   TIGRFAMs; TIGR01016; sucCoAbeta; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q758H3.
DR   SWISS-2DPAGE; Q758H3.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_03219, ECO:0000256|PROSITE-
KW   ProRule:PRU00409};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_03219, ECO:0000256|RuleBase:RU361258};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_03219};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_03219};
KW   Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03219};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03219, ECO:0000256|PROSITE-
KW   ProRule:PRU00409, ECO:0000256|RuleBase:RU361258};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_03219}.
FT   DOMAIN          30..273
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   NP_BIND         73..75
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03219"
FT   REGION          350..352
FT                   /note="Substrate binding; shared with subunit alpha"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03219"
FT   METAL           226
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03219"
FT   METAL           242
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03219"
FT   BINDING         66
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03219"
FT   BINDING         134
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03219"
FT   BINDING         293
FT                   /note="Substrate; shared with subunit alpha"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03219"
SQ   SEQUENCE   417 AA;  45001 MW;  BA51439BD8EC08F3 CRC64;
     MMLSRRLAHG AHKAVRVQTR ALSIHEYQSS ELLRQYGIGT PRGQAASTAQ QAYDAAAGLG
     HELVVKAQAL TGGRGKGHFN TGLQSGVHMI SSAEEARELA EQMLGNRLIT KQSGAKGKPV
     SAVYVVERVK ARHEAYLSIL MDRQTKKPLI ICSSQGGMNI EEVAHSNPDA IKKFYVDVKK
     GLDAETAAAV ARSLGFSQEA EADAADAVQK LYKIFREKDA TQIEINPLSE VEGQHTKVMC
     MDAKFGFDDN ASFRQQEVYS WRDLTQEDPD EVVAKNSDLN FVKLQGNIGC LVNGAGLAMA
     TMDVIKLYGG DPANFLDCGG GATPETIETA FKLILSNTKV KAIFVNIFGG IVRCDYVAQG
     LVAATKNLDV KVPIVARLQG TNLEEGRRII KESGLKIYGF DELDPAAEKV VGLAASS
//

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