ID   LYS4_SCHPO              Reviewed;         721 AA.
AC   Q9UT74;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Homoaconitase, mitochondrial;
DE            EC=4.2.1.36;
DE   AltName: Full=Homoaconitate hydratase;
DE   Flags: Precursor;
GN   Name=lys2; Synonyms=lys4; ORFNames=SPAC343.16;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   IDENTIFICATION.
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=16491385; DOI=10.1007/s00294-006-0065-2;
RA   Hoffman R.L., Hoffman C.S.;
RT   "Cloning the Schizosaccharomyces pombe lys2 (+) gene and construction of
RT   new molecular genetic tools.";
RL   Curr. Genet. 49:414-420(2006).
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; CU329670; CAB52279.1; -; Genomic_DNA.
DR   PIR; T38665; T38665.
DR   RefSeq; NP_593437.1; NM_001018870.2.
DR   AlphaFoldDB; Q9UT74; -.
DR   SMR; Q9UT74; -.
DR   BioGRID; 279312; 38.
DR   STRING; 4896.SPAC343.16.1; -.
DR   iPTMnet; Q9UT74; -.
DR   MaxQB; Q9UT74; -.
DR   PaxDb; Q9UT74; -.
DR   PRIDE; Q9UT74; -.
DR   EnsemblFungi; SPAC343.16.1; SPAC343.16.1:pep; SPAC343.16.
DR   GeneID; 2542867; -.
DR   KEGG; spo:SPAC343.16; -.
DR   PomBase; SPAC343.16; lys2.
DR   VEuPathDB; FungiDB:SPAC343.16; -.
DR   eggNOG; KOG0453; Eukaryota.
DR   HOGENOM; CLU_006714_3_1_1; -.
DR   InParanoid; Q9UT74; -.
DR   OMA; VMIRPEH; -.
DR   PhylomeDB; Q9UT74; -.
DR   UniPathway; UPA00033; UER01027.
DR   PRO; PR:Q9UT74; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005739; C:mitochondrion; IMP:PomBase.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0004409; F:homoaconitate hydratase activity; ISO:PomBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006536; P:glutamate metabolic process; NAS:PomBase.
DR   GO; GO:0009085; P:lysine biosynthetic process; IMP:PomBase.
DR   GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IMP:PomBase.
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.
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..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..721
FT                   /note="Homoaconitase, mitochondrial"
FT                   /id="PRO_0000247927"
FT   BINDING         377
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         437
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         440
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   721 AA;  78025 MW;  94104C72278539C7 CRC64;
     MDSGEMHHPY QAFSKVGKCE ISQTNPSFSS GMRCLVRSAD IQFKGICGLT RGFASFNKPP
     QTITEKIVQK FAQNIPENKY VRSGDYVTIK PKHCMSHDNS WPVALKFMGI GAKKVFDNRQ
     IVCTLDHDVQ NKSEANLRKY KNIESFAKGQ GIDFYPAGRG IGHQIMVEQG YAMPGSMAVA
     SDSHSNTYGG VGCLGTPIVR TDAAAIWATG QTWWQIPPIA RVNLVGQLPK GLSGKDIIVS
     LCGAFNHDEV LNHAIEFYGE GLNSLSIESR LTIANMTTEW GALSGLFPTD EKLLAWYEDR
     LKFLGPNHPR VNRETLDAIK ASPILADEGA FYAKHLILDL STLSPAVSGP NSVKVYNSAA
     TLEKKDILIK KAYLVSCTNG RLSDIHDAAE TVKGKKVADG VEFYVGAASS EVEAAAQKNG
     DWQTLIDSGA RTLPAGCGPC IGLGTGLLKD GEVGISATNR NFKGRMGSRE ALAYLASPAV
     VAASAIAGKI VAPEGFKNAV SLVSAVDITD KVNKQTASKS STEAVDSETA IIDGFPSIVA
     GEIVFCDADN LNTDGIYPGR YTYRDDITKE EMAKVCMENY DSEFGKKTKK DDILVSGFNF
     GTGSSREQAA TAILSRGIPL VVGGSFSDIF KRNSINNALL AIQLPDLVQK LRTAFANESK
     ELTRRTGWHL KWDVRKSTVT VTTSDNKEMS WKIGELGNSV QSLFVRGGLE GWVKHEISKS
     N