LYS4_CRYNJ
ID LYS4_CRYNJ Reviewed; 728 AA.
AC P0CM02; Q55JP2; Q5K9V9;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Homoaconitase, mitochondrial;
DE EC=4.2.1.36;
DE AltName: Full=Homoaconitate hydratase;
DE Flags: Precursor;
GN Name=LYS4; OrderedLocusNames=CNK00580;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(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; AE017351; AAW46105.1; -; Genomic_DNA.
DR RefSeq; XP_567622.1; XM_567622.1.
DR AlphaFoldDB; P0CM02; -.
DR SMR; P0CM02; -.
DR STRING; 5207.AAW46105; -.
DR PaxDb; P0CM02; -.
DR EnsemblFungi; AAW46105; AAW46105; CNK00580.
DR GeneID; 3254569; -.
DR KEGG; cne:CNK00580; -.
DR VEuPathDB; FungiDB:CNK00580; -.
DR eggNOG; KOG0453; Eukaryota.
DR HOGENOM; CLU_006714_3_1_1; -.
DR InParanoid; P0CM02; -.
DR OMA; VMIRPEH; -.
DR OrthoDB; 265826at2759; -.
DR UniPathway; UPA00033; UER01027.
DR Proteomes; UP000002149; Chromosome 11.
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 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 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.
DR PROSITE; PS01244; ACONITASE_2; 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..24
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 25..728
FT /note="Homoaconitase, mitochondrial"
FT /id="PRO_0000247922"
FT BINDING 362
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 422
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 425
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
SQ SEQUENCE 728 AA; 77887 MW; CB331008B37D75DE CRC64;
MVAIPRLARL SVPAWALSAR GRFYATVSTP QTLVEKIVQK YAVGLSEGVK VRAGDYVMIK
PEHVMTHDNT GPVISKFLSL SCSKLDNPRQ PVFALDHDVQ NQSETNQKKY KKIQAFAKEH
GVDFYPAGRG IGHQIIVEEG YAWPGKMVVA SDSHSNHYGG VGCLGTAIVR TDAAGIWATG
KFWWQIPRIV SVSLDGRLSP GVTGKDVIVA LAGLFNKDEV LNAAIEFTGS GVEHLSIDER
LTIANMTTEW GAVAGVFPVD DKLKEWYQGI LRKAELRKFI SPTVPSTVGA KVHPRLNAAR
LDDAMTNRVV ADPGAHYAAR LSLDLSTLVP HVSGPNSVKV ATALPKLLDP PIPINKAYLV
SCTNSRASDI ASAAQVLRGK KVAPGVEFYI AAASSRVQED AEAAGDWQTL IDAGAKTLPA
GCGPCIGLGV GLLEKGEVGI SATNRNYKGR MGSPDAIAYL ASPAVVAASA AKGVICGPES
MDLSQLPQYE QPKFSIIEEG AAGEEKPVEV DEASLEPLLE GFPAYFEGPL LFAPQDNLTT
DGMYPGKYTY QDDITPERQA EVVMENYDPT FAATARELRT ALPTASSPST LPGAILLSGY
NFGTGSSREQ AATAIKNAGI PLVICGSFGD IFKRNSINNG LILIESPSLI KDMTERFAKD
GVRNKGGKDG KLTVVPEGWR IKVDSQRGLV TVNMGEEEEK TYPAAKVGRS VQELWVNGGL
EGFIRASL
