ACON2_SCHPO
ID ACON2_SCHPO Reviewed; 918 AA.
AC Q9P7D4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 3.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Homocitrate dehydratase, mitochondrial;
DE EC=4.2.1.-;
DE AltName: Full=Aconitase 2;
DE Flags: Precursor;
GN ORFNames=SPBP4H10.15;
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 REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Catalyzes the reversible dehydration of (R)-homocitrate to
CC cis-homoaconitate, a step in the alpha-aminoadipate pathway for lysine
CC biosynthesis. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-homocitrate = cis-homoaconitate + H2O;
CC Xref=Rhea:RHEA:26101, ChEBI:CHEBI:15377, ChEBI:CHEBI:58174,
CC ChEBI:CHEBI:58884;
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 2/5.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAB83173.3; -; Genomic_DNA.
DR RefSeq; NP_596189.3; NM_001022108.3.
DR AlphaFoldDB; Q9P7D4; -.
DR SMR; Q9P7D4; -.
DR BioGRID; 277859; 7.
DR STRING; 4896.SPBP4H10.15.1; -.
DR iPTMnet; Q9P7D4; -.
DR MaxQB; Q9P7D4; -.
DR PaxDb; Q9P7D4; -.
DR EnsemblFungi; SPBP4H10.15.1; SPBP4H10.15.1:pep; SPBP4H10.15.
DR GeneID; 2541348; -.
DR KEGG; spo:SPBP4H10.15; -.
DR PomBase; SPBP4H10.15; -.
DR VEuPathDB; FungiDB:SPBP4H10.15; -.
DR eggNOG; KOG0453; Eukaryota.
DR HOGENOM; CLU_006714_2_2_1; -.
DR InParanoid; Q9P7D4; -.
DR OMA; GRASYMR; -.
DR BRENDA; 4.2.1.3; 5613.
DR UniPathway; UPA00033; UER00029.
DR PRO; PR:Q9P7D4; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005762; C:mitochondrial large ribosomal subunit; ISO:PomBase.
DR GO; GO:0005739; C:mitochondrion; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0003994; F:aconitate hydratase activity; ISO:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:PomBase.
DR GO; GO:0006536; P:glutamate metabolic process; NAS:PomBase.
DR GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IEA:UniProtKB-UniPathway.
DR GO; GO:0032543; P:mitochondrial translation; IMP:PomBase.
DR GO; GO:0006099; P:tricarboxylic acid cycle; ISS:PomBase.
DR Gene3D; 3.20.19.10; -; 1.
DR Gene3D; 3.30.499.10; -; 2.
DR Gene3D; 3.40.1060.10; -; 1.
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; IPR015932; Aconitase_dom2.
DR InterPro; IPR006248; Aconitase_mito-like.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR InterPro; IPR036164; L21-like_sf.
DR InterPro; IPR028909; L21p-like.
DR Pfam; PF00330; Aconitase; 1.
DR Pfam; PF00694; Aconitase_C; 1.
DR Pfam; PF00829; Ribosomal_L21p; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF141091; SSF141091; 1.
DR SUPFAM; SSF53732; SSF53732; 1.
DR TIGRFAMs; TIGR01340; aconitase_mito; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
DR PROSITE; PS01244; ACONITASE_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Amino-acid biosynthesis; Iron; Iron-sulfur; Lyase;
KW Lysine biosynthesis; Metal-binding; Mitochondrion; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..30
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 31..918
FT /note="Homocitrate dehydratase, mitochondrial"
FT /id="PRO_0000316198"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 198..200
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 394
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 457
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 484
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 489
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 680..681
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 918 AA; 99901 MW; A17A3132B7B21D90 CRC64;
MATFARMKLC LSGSSQAIPS KGISLVAARF QSTASRASYV TPPYEKLMGK LQQVRKFLPG
QKLTLAEKVL YSHLVNPEES FSGVSPSDIR GSLYLKLNPD RVAMQDASAQ MALLQFMTCG
LEKTMIPASI HCDHLIVGHR GANSDIPDSI ANNKEIFDFL QSAAKKYGIQ FWGPGSGIIH
QIVLENYAAP GGMMLGTDSH TPNAGGLGMI AIGVGGADAV DAMTNTPWEL KAPKIIGVNL
TGAMSGWTTP KDLILHLAGK LTVRGGTGHI IEYFGPGVAS LSCTGMATVC NMGAEVGATT
SIFPYTDSMR RYLIATHRAE VADAASEVHS EYNYLAADTG AKYDQIIDIN LSELTPSLNG
PFTPDLSTPV SKFGEAIEKN KWPKKLSAGL IGSCTNSSYQ DMTCVVDVVE QAISAGLKPK
VPFLVTPGSE QIRATIERDG ITERLEEAGA TVLANACGPC IGMWKRTDDI ASGEPNAILT
SFNRNFRSRN DGNPSTMNFL TSPVIVAAKI FSSDLAFDPT HDTLQTPDGK AFKFRPPQGV
ELPSAGFIAG DSSYIPEPNP QPVPETEVTI DPKSDRLEAL EPFEPYQGGE MENLKVAVKV
KGKCTTDHIS AAGKWLKYKG HLSNICNNTL IGAMNAATGE VNRAYDNGKG MTIPELMWKW
KKDGQPWLVV AEHNYGEGSA REHAALQPRA MNGRIILTKS FARIHETNLK KQGVLPLTFV
NEADYEKIDA EDKVSTRGIE QLLEGVLDQP ITLVVTKKDG SVVEIPCKHT MSKDQIEFFK
AGSALNLIRE KAHSGVVNQK VIDSIKQQPD HYADAYIFNR HFVIAKGDQL GLPFHLKGVQ
VGDTIRLDKI ASFGSRDFTL FGNPYVDPSL FTIEAVVLSF PKSALSVRVK HKRRHRHDRV
MKHKQTYTIL RVTELKLN
