LYS4_ASPNC
ID LYS4_ASPNC Reviewed; 769 AA.
AC Q58FL6; A2R4G6;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Homoaconitase, mitochondrial;
DE EC=4.2.1.36;
DE AltName: Full=Homoaconitate hydratase;
DE Flags: Precursor;
GN Name=lysA; Synonyms=lys4; ORFNames=An15g00350;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA van de Vondervoort P.J.I., Langeveld S.M.J., Ram A.F.J., Visser J.,
RA Groot G., Pel H., van Peij N.N.M.E.;
RT "Comparison of the Aspergillus niger genomic DNA sequence with its genetic
RT map.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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:0000250}.
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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC pathway; L-alpha-aminoadipate from 2-oxoglutarate: step 3/5.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000305}.
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DR EMBL; AY955279; AAX53108.1; -; Genomic_DNA.
DR EMBL; AM270330; CAK42204.1; -; Genomic_DNA.
DR RefSeq; XP_001396574.1; XM_001396537.2.
DR AlphaFoldDB; Q58FL6; -.
DR SMR; Q58FL6; -.
DR PaxDb; Q58FL6; -.
DR EnsemblFungi; CAK42204; CAK42204; An15g00350.
DR GeneID; 4987626; -.
DR KEGG; ang:ANI_1_1106134; -.
DR VEuPathDB; FungiDB:An15g00350; -.
DR HOGENOM; CLU_006714_3_1_1; -.
DR UniPathway; UPA00033; UER01027.
DR Proteomes; UP000006706; Chromosome 3R.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0004409; F:homoaconitate hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IEA:UniProtKB-UniPathway.
DR CDD; cd01674; Homoaconitase_Swivel; 1.
DR Gene3D; 3.20.19.10; -; 1.
DR Gene3D; 3.30.499.10; -; 2.
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 Pfam; PF00330; Aconitase; 1.
DR Pfam; PF00694; Aconitase_C; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; SSF53732; 1.
DR TIGRFAMs; TIGR00139; h_aconitase; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Iron; Iron-sulfur; Lyase; Lysine biosynthesis;
KW Metal-binding; Mitochondrion; Reference proteome; Transit peptide.
FT TRANSIT 1..28
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 29..769
FT /note="Homoaconitase, mitochondrial"
FT /id="PRO_0000247917"
FT BINDING 391
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 460
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 463
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
SQ SEQUENCE 769 AA; 83363 MW; 2131A00345B50456 CRC64;
MQSRLLPSGP GRRWISLRVP NTPQRRAFAS TRFLFQDVFQ SQLDDPSSAA LFSSLQSSRA
VPQTLTEKIV QKYAVGLPDG KFVKSGDYVT IAPHRIMTHD NSWPVALKFM SIGASKMHDP
NQVVMTLDHD VQNKTEKNLQ KYRQIEEFAK QHGVEFYPAG RGIGHQIMVE EGFAWPGTLV
VASDSHSNTY GAVASVGTPI VRTDAASIWA TGKTWWQIPP VAKVTFTGIL PPGVTGKDVI
VALCGLFDKD DVLNHAIEFT GSEETMRSLP MDSRLTIANM TTEWGALSGL FPMDGVLKGW
LKGKATTAAM GLADGPFKTL AARNFTHPAI EQLFVNPLTA DKGAKYAKEL FLDLSTLSPY
VSGPNSVKIA TPLKELEAQD IKVDKAYLVS CTNSRASDIA AAAKVFKDAA EKNGGKVPKI
ADGVKFYIAA ASIPEQLAAE GAGDWQTLLE AGATALPAGC GPCIGLGTGL LEPGEVGISA
SNRNFKGRMG STEAKAYLGS PEIVAASALS GKLSGPGWYQ PPEGWTEVVR GEGDGIREED
RMLNTEQALE KLLGQLDDLV ADGEKRFAPE EKVEEEGGLT EVYPGFPERV SGEIVFCDAD
NLNTDAIYPG YWTYQDNVPV EKMAEVCMSN YDKEFASIAK EGDILVVGYN FGCGSSREQA
ATALLAKQIP LVVSGSFGNI FSRNSINNAL MGLEVPRLVS RLREEFGDKQ LTRRTGWTLT
WDVRRSQIEI QEGQNGPKWT HKVGELPPNV QEIIAKGGLE KWVKNAIEA
