UniProt: G3AE20

Database: UniProt
Entry: G3AE20_SPAPN

LinkDB:  G3AE20_SPAPN 
Original site:  G3AE20_SPAPN

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (12)   
   InterPro (8)   
   Pfam (2)   
   PROSITE (2)   
Literature (1)   
   PubMed (1)   
All databases (23)   

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ID   G3AE20_SPAPN            Unreviewed;       551 AA.
AC   G3AE20;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Homoaconitase, mitochondrial {ECO:0000256|ARBA:ARBA00021560, ECO:0000256|RuleBase:RU362038};
DE            EC=4.2.1.36 {ECO:0000256|ARBA:ARBA00012022, ECO:0000256|RuleBase:RU362038};
DE   AltName: Full=Homoaconitate hydratase {ECO:0000256|ARBA:ARBA00032706, ECO:0000256|RuleBase:RU362038};
GN   Name=LYS4 {ECO:0000313|EMBL:EGW35554.1};
GN   ORFNames=SPAPADRAFT_58782 {ECO:0000313|EMBL:EGW35554.1};
OS   Spathaspora passalidarum (strain NRRL Y-27907 / 11-Y1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX   NCBI_TaxID=619300 {ECO:0000313|Proteomes:UP000000709};
RN   [1] {ECO:0000313|EMBL:EGW35554.1, ECO:0000313|Proteomes:UP000000709}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-27907 / 11-Y1 {ECO:0000313|Proteomes:UP000000709};
RX   PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA   Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA   Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA   Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA   Barry K.W., Grigoriev I.V., Gasch A.P.;
RT   "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT   production.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
CC   -!- FUNCTION: Catalyzes the reversible hydration of cis-homoaconitate to
CC       (2R,3S)-homoisocitrate, a step in the alpha-aminoadipate pathway for
CC       lysine biosynthesis. {ECO:0000256|ARBA:ARBA00003422,
CC       ECO:0000256|RuleBase:RU362038}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R,3S)-homoisocitrate = cis-homoaconitate + H2O;
CC         Xref=Rhea:RHEA:15485, ChEBI:CHEBI:15377, ChEBI:CHEBI:15404,
CC         ChEBI:CHEBI:58174; EC=4.2.1.36;
CC         Evidence={ECO:0000256|ARBA:ARBA00029338,
CC         ECO:0000256|RuleBase:RU362038};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|RuleBase:RU362038};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit.
CC       {ECO:0000256|RuleBase:RU362038};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC       pathway; L-alpha-aminoadipate from 2-oxoglutarate: step 3/5.
CC       {ECO:0000256|ARBA:ARBA00005106, ECO:0000256|RuleBase:RU362038}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173,
CC       ECO:0000256|RuleBase:RU362038}.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC       {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|RuleBase:RU362038}.
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DR   EMBL; GL996499; EGW35554.1; -; Genomic_DNA.
DR   RefSeq; XP_007372966.1; XM_007372904.1.
DR   AlphaFoldDB; G3AE20; -.
DR   STRING; 619300.G3AE20; -.
DR   GeneID; 18872605; -.
DR   KEGG; spaa:SPAPADRAFT_58782; -.
DR   eggNOG; KOG0453; Eukaryota.
DR   HOGENOM; CLU_006714_3_1_1; -.
DR   InParanoid; G3AE20; -.
DR   OMA; LCDADNI; -.
DR   OrthoDB; 1122834at2759; -.
DR   UniPathway; UPA00033; UER01027.
DR   Proteomes; UP000000709; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004409; F:homoaconitate hydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IEA:UniProtKB-UniRule.
DR   CDD; cd01674; Homoaconitase_Swivel; 1.
DR   Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR   Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
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; IPR018136; Aconitase_4Fe-4S_BS.
DR   InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR   InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR   InterPro; IPR004418; Homoaconitase_mito.
DR   InterPro; IPR039386; Homoaconitase_swivel.
DR   NCBIfam; TIGR00139; h_aconitase; 1.
DR   PANTHER; PTHR43822:SF25; HOMOACONITASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43822; HOMOACONITASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00330; Aconitase; 1.
DR   Pfam; PF00694; Aconitase_C; 1.
DR   PRINTS; PR00415; ACONITASE.
DR   SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR   SUPFAM; SSF52016; LeuD/IlvD-like; 1.
DR   PROSITE; PS00450; ACONITASE_1; 1.
DR   PROSITE; PS01244; ACONITASE_2; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU362038};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU362038};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU362038};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU362038};
KW   Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154,
KW   ECO:0000256|RuleBase:RU362038};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU362038};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW   ECO:0000256|RuleBase:RU362038};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000709};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946,
KW   ECO:0000256|RuleBase:RU362038}.
FT   DOMAIN          1..322
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          354..478
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   551 AA;  58785 MW;  D07B7B3830C791FD CRC64;
     MIEEGYAFPL NLTVASDSHS NTYGGVGSLG TPIVRTDAAS IWATGQTWWQ IPPVAKVELR
     GELQKGVTGK DIIVALCGEF NNDEVLNHAI EFVGDGVNKL SIDYRLTIAN MTTEWGALSG
     LFPVDKTLVD FYKQRLQAVG PNHPRINETT VSELSNPLAS DNDAVYAKHL VIDLSSLSPS
     VSGPNSVKIS TSLNELAHQN IKINKAYLVS CTNSRLSDIQ AAADVISNHQ VHPDVEFYVA
     AASSLVQQDA EQVGAWQKLI DAGAKPLPAG CGPCIGLGAG LLKDGEVGIS ATNRNFKGRM
     GSRDALAYLA SPEVVAASAV LGRIGGVEEL QGEPVKPVTP IVKSITQESP VEATEEAAGA
     VEVLDGFPKS ISGELILCNA DNINTDGIYP GKYTYQDDIP KSKMAEVCME NYDSQFHSKT
     KPGDIIISGY NFGTGSSREQ AATCILARGI NLVVAGSFGN IFSRNSINNA LLTLEIPKLI
     DMLREKYSGS DELTIRTGWV LTWDVTTAQV KVVDADGNVV LQQKVGELGT NLQDIIVKGG
     LEGWVKAELS K
//

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