LYS4_ASPOR
ID LYS4_ASPOR Reviewed; 775 AA.
AC Q2U9G3;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Homoaconitase, mitochondrial;
DE EC=4.2.1.36;
DE AltName: Full=Homoaconitate hydratase;
DE Flags: Precursor;
GN Name=lys4; ORFNames=AO090701000041;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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; AP007164; BAE61802.1; -; Genomic_DNA.
DR RefSeq; XP_001822935.2; XM_001822883.2.
DR AlphaFoldDB; Q2U9G3; -.
DR SMR; Q2U9G3; -.
DR STRING; 510516.Q2U9G3; -.
DR EnsemblFungi; BAE61802; BAE61802; AO090701000041.
DR GeneID; 5994992; -.
DR KEGG; aor:AO090701000041; -.
DR VEuPathDB; FungiDB:AO090701000041; -.
DR HOGENOM; CLU_006714_3_1_1; -.
DR OMA; VMIRPEH; -.
DR UniPathway; UPA00033; UER01027.
DR Proteomes; UP000006564; Chromosome 5.
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..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 30..775
FT /note="Homoaconitase, mitochondrial"
FT /id="PRO_0000247918"
FT BINDING 392
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 461
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 464
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
SQ SEQUENCE 775 AA; 83730 MW; 9BBD259B9643A3DA CRC64;
MQSRLMPSGG PGRRWAFLRV PSTPQRRAFA STRFYFQDIF QSQLEDPSSA AVYSSLQASR
AVPQTLTEKI VQKYSVGLAK DKFVKSGDYV TISPHRCMTH DNSWPVALKF MSIGATKLHD
PKQIVMTLDH DVQNKSEKNL QKYRQIEDFA KHQGVEFYPA GRGIGHQVMV EEGYAWPGTL
VVASDSHSNM YGGVGCLGTP IVRTDGASIW ATGKTWWQIP PVAKVTLTGV LPPGVTGKDV
IVALCGLFDK DDVLNHAIEF TGPEETMRSL SVDARLTIAN MTTEWGALSG LFPIDNVLKG
WLKGKATTAA MGLAEGPFKT LAPQHFTHPL LEQLFANPLT ADKGAKYAKE LFLDLSTLSP
YVSGPNSVKV ATPLKDLEAQ NIKVNKAYLV SCTNSRASDI AAAARVFKEA AEKNGGKVPK
IADGVEFYVA AASIPEQLAA EEAGDWQALL DAGATPLLPG CAQCIGLGTG LLEAGEVGIS
ASNRNFKGRM GSTDAKAYLG SPEVVAASAL TGKLSGPGWY QAPEGLTEVV RGEGDGIREE
DRMLTAEQAL EKLIGQIDNL VADGEKQFAP EESEESSGDS LTEVYPGFPE RVSGEIVFCD
ADNINTDGIY PGKYTYQDDV SQETMAQVCM SNYDAQFSSI AKEGDILVTG FNFGCGSSRE
QAATAILAKK IPLVVSGSFG NIFSRNSINN ALMGLEVPRL INRLRESFSG EGSDKSLTRR
TGWTLTWDVR RSRIEVQEGE NGPKWTHQVG ELPPNVQEII AKGGLEKWVK NEIGA
