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SUCB_NEUCR
ID   SUCB_NEUCR              Reviewed;         447 AA.
AC   Q9P567; Q7SC52;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03219};
DE            EC=6.2.1.5 {ECO:0000255|HAMAP-Rule:MF_03219};
DE   AltName: Full=Succinyl-CoA synthetase beta chain {ECO:0000255|HAMAP-Rule:MF_03219};
DE            Short=SCS-beta {ECO:0000255|HAMAP-Rule:MF_03219};
DE   Flags: Precursor;
GN   Name=tca-9 {ECO:0000303|PubMed:15522735}; ORFNames=B9J10.140, NCU08471;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
RN   [3]
RP   PATHWAY.
RX   PubMed=15522735; DOI=10.1016/s0065-2660(04)52005-9;
RA   Radford A.;
RT   "Metabolic highways of Neurospora crassa revisited.";
RL   Adv. Genet. 52:165-207(2004).
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:0000255|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:0000255|HAMAP-
CC         Rule:MF_03219};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03219};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03219};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC       from succinyl-CoA (ligase route): step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_03219, ECO:0000305|PubMed:15522735}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_03219}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03219}.
CC   -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta subunit
CC       family. {ECO:0000255|HAMAP-Rule:MF_03219}.
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DR   EMBL; AL356324; CAB92021.1; -; Genomic_DNA.
DR   EMBL; CM002237; EAA34077.1; -; Genomic_DNA.
DR   PIR; T49777; T49777.
DR   RefSeq; XP_963313.1; XM_958220.3.
DR   AlphaFoldDB; Q9P567; -.
DR   SMR; Q9P567; -.
DR   STRING; 5141.EFNCRP00000008443; -.
DR   PRIDE; Q9P567; -.
DR   EnsemblFungi; EAA34077; EAA34077; NCU08471.
DR   GeneID; 3879462; -.
DR   KEGG; ncr:NCU08471; -.
DR   VEuPathDB; FungiDB:NCU08471; -.
DR   HOGENOM; CLU_037430_0_2_1; -.
DR   InParanoid; Q9P567; -.
DR   OMA; ITACDEV; -.
DR   UniPathway; UPA00223; UER00999.
DR   Proteomes; UP000001805; Chromosome 6, Linkage Group II.
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; 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; PS01217; SUCCINYL_COA_LIG_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Magnesium; Metal-binding; Mitochondrion;
KW   Nucleotide-binding; Reference proteome; Transit peptide;
KW   Tricarboxylic acid cycle.
FT   TRANSIT         1..34
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03219"
FT   CHAIN           35..447
FT                   /note="Succinate--CoA ligase [ADP-forming] subunit beta,
FT                   mitochondrial"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03219"
FT                   /id="PRO_0000033363"
FT   DOMAIN          45..287
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03219"
FT   BINDING         82
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03219"
FT   BINDING         89..91
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03219"
FT   BINDING         150
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03219"
FT   BINDING         242
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03219"
FT   BINDING         256
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03219"
FT   BINDING         307
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared with subunit alpha"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03219"
FT   BINDING         364..366
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared with subunit alpha"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03219"
SQ   SEQUENCE   447 AA;  48210 MW;  FFF59594016F9A4D CRC64;
     MFKLGRNRAL ASAFAATSRA PLASRLPSVS QQQRRALSIH EYLSADLLRQ YGIGVPKGDV
     ARTGAEAEAI AKQIGGEDMV IKAQVLAGGR GKGTFDNGLK GGVRVIYSPT EAKMFAEQMI
     GHKLITKQTG AQGRLCSAVY ICERKFARRE FYLAVLMDRA SQGPVIVSSS QGGMDIEGVA
     KENPEAIHTT YIDINVGVTD EMARDIATKL GFSEQCVEEA KDTIQKLYKI FCEKDATQIE
     INPLSETSDH KVMAMDAKFG FDDNADFRQP DIFKLRDTTQ EDPDEVRAAQ AGLNFIKLDG
     DIGCLVNGAG LAMATMDIIK LNGGQPANFL DVGGGATPAA IREAFELITS DPKVTAIFVN
     IFGGIVRCDA IAHGLINTVK SLDLKIPIIA RLQGTNMEAA RQLINDSGMK IFSIDDLQSA
     AEKSVQLSKV VKMARDIDVG VEFTLGI
 
 
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