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ACOHC_DICDI
ID   ACOHC_DICDI             Reviewed;         894 AA.
AC   Q54X73;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Probable cytoplasmic aconitate hydratase {ECO:0000305};
DE            Short=Aconitase;
DE            EC=4.2.1.3 {ECO:0000250|UniProtKB:P21399};
DE   AltName: Full=Citrate hydro-lyase;
GN   Name=aco1; Synonyms=acnA; ORFNames=DDB_G0279159;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis-
CC       aconitate. {ECO:0000250|UniProtKB:P21399}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=citrate = D-threo-isocitrate; Xref=Rhea:RHEA:10336,
CC         ChEBI:CHEBI:15562, ChEBI:CHEBI:16947; EC=4.2.1.3;
CC         Evidence={ECO:0000250|UniProtKB:P21399};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:P21399};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit.
CC       {ECO:0000250|UniProtKB:P21399};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P21399}.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; AAFI02000028; EAL67861.1; -; Genomic_DNA.
DR   RefSeq; XP_641837.1; XM_636745.1.
DR   AlphaFoldDB; Q54X73; -.
DR   SMR; Q54X73; -.
DR   STRING; 44689.DDB0229908; -.
DR   PaxDb; Q54X73; -.
DR   EnsemblProtists; EAL67861; EAL67861; DDB_G0279159.
DR   GeneID; 8621900; -.
DR   KEGG; ddi:DDB_G0279159; -.
DR   dictyBase; DDB_G0279159; aco1.
DR   eggNOG; KOG0452; Eukaryota.
DR   HOGENOM; CLU_013476_2_1_1; -.
DR   InParanoid; Q54X73; -.
DR   OMA; NGGIMQY; -.
DR   PhylomeDB; Q54X73; -.
DR   Reactome; R-DDI-917937; Iron uptake and transport.
DR   PRO; PR:Q54X73; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR   GO; GO:0003994; F:aconitate hydratase activity; IBA:GO_Central.
DR   GO; GO:0047780; F:citrate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030350; F:iron-responsive element binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006101; P:citrate metabolic process; IBA:GO_Central.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR   CDD; cd01580; AcnA_IRP_Swivel; 1.
DR   Gene3D; 3.20.19.10; -; 1.
DR   Gene3D; 3.30.499.10; -; 2.
DR   InterPro; IPR044137; AcnA_IRP_Swivel.
DR   InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR   InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR   InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR   InterPro; IPR006249; Aconitase/IRP2.
DR   InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR   InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR   InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR   PANTHER; PTHR11670; PTHR11670; 1.
DR   Pfam; PF00330; Aconitase; 1.
DR   Pfam; PF00694; Aconitase_C; 1.
DR   PRINTS; PR00415; ACONITASE.
DR   SUPFAM; SSF53732; SSF53732; 1.
DR   TIGRFAMs; TIGR01341; aconitase_1; 1.
DR   PROSITE; PS00450; ACONITASE_1; 1.
DR   PROSITE; PS01244; ACONITASE_2; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Lyase; Metal-binding;
KW   Reference proteome; Tricarboxylic acid cycle.
FT   CHAIN           1..894
FT                   /note="Probable cytoplasmic aconitate hydratase"
FT                   /id="PRO_0000328573"
FT   BINDING         87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         207..209
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         438
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         504
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         507
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         537
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         542
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         781..782
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   894 AA;  97991 MW;  8CE9854114B55202 CRC64;
     MTTNNPFDKV KDVLKSQDQT YNFYNLSKLQ DPRIEKLPYS IRILLESAVR NCDNFEVHEK
     DVENILNWEN TANKVEIPFK PARVLLQDFT GVPAVVDLAA MRDAMKRLGG DPAKINPLVP
     VDLVIDHSVQ VDVSRTVDAL EQNQKIEFHR NHERFSFLKW GAQAFDGLFI APPGSGIVHQ
     VNLEYIAREV MNGTGNLLYP DSVVGTDSHT TMINGLGVCG WGVGGIEAEA VMLGQPMSMV
     LPEVVGYKFV GKLPDIATAT DLVLTVTNEL RKKGVVGKFV EFYGEGVSTL SVQDRATISN
     MAPEYGATMG FFPADENTID YLASTGRSNT KIEYIKNYLS SQGLMCNYKS QSHPIFTTTM
     ELDLSTVVPS LSGPKRPHDR ISLNSMKQDF NSCLSSPVGF KGFGLTADQI QKKATFTFKD
     KQYTIGHGAV TIAAITSCTN TSNPSVMLGA GLLAKNAVEH GLEVAPYIKT SLSPGSGVVT
     EYFSHSGLQE PLNKLGFDLT GYGCMTCIGN SGELAEPLAE AITKEDLVVA GVLSGNRNFE
     GRIHPLLRAN YLASPPLVVA YALAGTVDID FETTPLGVSK KTGQPVFLRD IWPSKDLIQQ
     TIKSSVLPDM YERVYSNVND GNKSWNELKV PTGLLYPWDE KSTYIHNPPF FKTMELTVSK
     RPAITNAYCL LNLGDSITTD HISPAGNINR KSSAARYLES KGVKPEDFNT YGSRRGNDEI
     MVRGTFANTR IVNKLAPAVG PQTTYVPTGE LMFISDAAEK YQSEGHQLIV LAGSDYGSGS
     SRDWAAKGPY LQGIKCVIAI SFERIHRSNL VGMGIIPLQF QPGQNASTLG LTGKEQFNIE
     LPTDKSLIKT GQTVKVTTNC GKSFETILRF DTPIEVEYWA NNGILSYVLR KLLH
 
 
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