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Database: UniProt
Entry: Q9P567
LinkDB: Q9P567
Original site: Q9P567 
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   16-JAN-2019, entry version 137.
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};
GN   ORFNames=B9J10.140, NCU08471;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM
OS   1257 / FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae;
OC   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.,
RA   Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J.,
RA   Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the
RT   Neurospora 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.,
RA   Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L.,
RA   Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C.,
RA   Marcotte E., Greenberg D., Roy A., Foley K., Naylor J.,
RA   Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M.,
RA   Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S.,
RA   Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C.,
RA   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.,
RA   Paulsen I., 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
CC       cycle (TCA), coupling the hydrolysis of succinyl-CoA to the
CC       synthesis of ATP and thus represents the only step of substrate-
CC       level phosphorylation in the TCA. The beta subunit provides
CC       nucleotide specificity of the enzyme and binds the substrate
CC       succinate, while the binding sites for coenzyme A and phosphate
CC       are found in the alpha subunit. {ECO:0000255|HAMAP-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-
CC       Rule:MF_03219};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       succinate from succinyl-CoA (ligase route): step 1/1.
CC       {ECO:0000255|HAMAP-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-
CC       Rule:MF_03219}.
CC   -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta
CC       subunit family. {ECO:0000255|HAMAP-Rule:MF_03219}.
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   ProteinModelPortal; Q9P567; -.
DR   SMR; Q9P567; -.
DR   PRIDE; Q9P567; -.
DR   EnsemblFungi; EAA34077; EAA34077; NCU08471.
DR   GeneID; 3879462; -.
DR   KEGG; ncr:NCU08471; -.
DR   EuPathDB; FungiDB:NCU08471; -.
DR   HOGENOM; HOG000007059; -.
DR   InParanoid; Q9P567; -.
DR   KO; K01900; -.
DR   OMA; LCMDAKF; -.
DR   UniPathway; UPA00223; UER00999.
DR   Proteomes; UP000001805; Chromosome 6, Linkage Group II.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-UniRule.
DR   GO; GO:0006104; P:succinyl-CoA metabolic process; IEA:EnsemblFungi.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
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; Complete proteome; Ligase; Magnesium; Metal-binding;
KW   Mitochondrion; Nucleotide-binding; Reference proteome;
KW   Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT       1     34       Mitochondrion. {ECO:0000255|HAMAP-
FT                                Rule:MF_03219}.
FT   CHAIN        35    447       Succinate--CoA ligase [ADP-forming]
FT                                subunit beta, mitochondrial.
FT                                {ECO:0000255|HAMAP-Rule:MF_03219}.
FT                                /FTId=PRO_0000033363.
FT   DOMAIN       45    287       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_03219}.
FT   NP_BIND      89     91       ATP. {ECO:0000255|HAMAP-Rule:MF_03219}.
FT   REGION      364    366       Substrate binding; shared with subunit
FT                                alpha. {ECO:0000255|HAMAP-Rule:MF_03219}.
FT   METAL       242    242       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_03219}.
FT   METAL       256    256       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_03219}.
FT   BINDING      82     82       ATP. {ECO:0000255|HAMAP-Rule:MF_03219}.
FT   BINDING     150    150       ATP. {ECO:0000255|HAMAP-Rule:MF_03219}.
FT   BINDING     307    307       Substrate; shared with subunit alpha.
FT                                {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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