LYS4_CRYNB
ID LYS4_CRYNB Reviewed; 728 AA.
AC P0CM03; Q55JP2; Q5K9V9;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Homoaconitase, mitochondrial;
DE EC=4.2.1.36;
DE AltName: Full=Homoaconitate hydratase;
DE Flags: Precursor;
GN Name=LYS4; OrderedLocusNames=CNBK2910;
OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=283643;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-3501A;
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; AAEY01000052; EAL18273.1; -; Genomic_DNA.
DR RefSeq; XP_772920.1; XM_767827.1.
DR AlphaFoldDB; P0CM03; -.
DR SMR; P0CM03; -.
DR EnsemblFungi; EAL18273; EAL18273; CNBK2910.
DR GeneID; 4938991; -.
DR KEGG; cnb:CNBK2910; -.
DR VEuPathDB; FungiDB:CNBK2910; -.
DR HOGENOM; CLU_006714_3_1_1; -.
DR UniPathway; UPA00033; UER01027.
DR Proteomes; UP000001435; 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; Transit peptide.
FT TRANSIT 1..24
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 25..728
FT /note="Homoaconitase, mitochondrial"
FT /id="PRO_0000410002"
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; 77886 MW; AD3E7714C2BA6BAF 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 QPKFSIIKEG AAGEEKPVEV DEASLEPLLE GFPAYFEGPL LFAPQDNLTT
DGMYPGKYTY QDDITPERQA EVVMENYDPT FAATARELRT ALPTASSPST LPGAILLSGY
NFGTGSSREQ AATAIKNAGI PLVICGSFGD IFKRNSINNG LILIESPSLI KDMTERFAKD
GVRNKGGKDG KLTVVPEGWR IKVDSQRGLV TVNMGEEEEK TYPAAKVGRS VQELWVNGGL
EGFIRASL
