(data stored in ACNUC7421 zone)

SWISSPROT: Q4W9L3_ASPFU

ID   Q4W9L3_ASPFU            Unreviewed;       444 AA.
AC   Q4W9L3;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 98.
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=AFUA_4G04520 {ECO:0000313|EMBL:EAL84600.1};
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL84600.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL84600.1, ECO:0000313|Proteomes:UP000002530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC   {ECO:0000313|Proteomes:UP000002530};
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA   Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA   Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA   Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA   Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA   Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA   Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA   Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA   Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA   Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA   Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA   Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA   Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA   Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAL84600.1}.
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DR   EMBL; AAHF01000016; EAL84600.1; -; Genomic_DNA.
DR   RefSeq; XP_746638.1; XM_741545.1.
DR   STRING; 746128.CADAFUBP00009570; -.
DR   SwissPalm; Q4W9L3; -.
DR   PRIDE; Q4W9L3; -.
DR   EnsemblFungi; EAL84600; EAL84600; AFUA_4G04520.
DR   GeneID; 3503973; -.
DR   KEGG; afm:AFUA_4G04520; -.
DR   EuPathDB; FungiDB:Afu4g04520; -.
DR   HOGENOM; HOG000007059; -.
DR   InParanoid; Q4W9L3; -.
DR   KO; K01900; -.
DR   OMA; ITACDEV; -.
DR   OrthoDB; 973871at2759; -.
DR   UniPathway; UPA00223; UER00999.
DR   Proteomes; UP000002530; Chromosome 4.
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;
DR   PRODOM; Q4W9L3.
DR   SWISS-2DPAGE; Q4W9L3.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_03219};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_03219, ECO:0000256|RuleBase:RU361258,
KW   ECO:0000313|EMBL:EAL84600.1}; 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,
KW   ECO:0000256|RuleBase:RU361258};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_03219}.
FT   DOMAIN          36..242
FT                   /note="ATP-grasp_2"
FT                   /evidence="ECO:0000259|Pfam:PF08442"
FT   DOMAIN          302..421
FT                   /note="Ligase_CoA"
FT                   /evidence="ECO:0000259|Pfam:PF00549"
FT   NP_BIND         86..88
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03219"
FT   REGION          361..363
FT                   /note="Substrate binding; shared with subunit alpha"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03219"
FT   METAL           239
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03219"
FT   METAL           253
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03219"
FT   BINDING         79
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03219"
FT   BINDING         147
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03219"
FT   BINDING         304
FT                   /note="Substrate; shared with subunit alpha"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03219"
SQ   SEQUENCE   444 AA;  48017 MW;  6A28C85B841D52AF CRC64;
     MFKLARSSRP VAAAIRAATE SSVQFRLAQQ QRNLSIHEYL SARLLKSYGV GVPKGEVAHS
     AEEAEAVAKS IGNDDMVIKA QVLAGGRGKG SFDNGLKGGV RVIYSPTEAK MFASQMIGHK
     LITKQTGAAG RLCNAVYICE RKFARREFYL AVLMDRATQT PVIVASSQGG MDIEAVAKEH
     PEAIMTTPID IKVGVTDDIA RKIATDLGFS EQCIEDAKTT IQNLYKVFME KDATQIEINP
     LSETSDHQVL AMDAKLNFDD NAEFRQKEVF SWRDTTQEDA DEVKAAEYGL NFIKLDGDIG
     CLVNGAGLAM ATMDIIKLNG GNPANFLDVG GGATPAAIKS AFELITSDPK VTAIFVNIFG
     GIVRCDAIAR GLINVVEDMG LRIPIVARLQ GTNMEQAQKL INESGLKIFS IEDLQSAAEK
     SVQFSKVVKM AREIDVGVEF TLGI
//

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