ID R7SYV4_DICSQ Unreviewed; 730 AA.
AC R7SYV4;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Homoaconitase, mitochondrial {ECO:0000256|ARBA:ARBA00021560, ECO:0000256|RuleBase:RU362038};
DE EC=4.2.1.36 {ECO:0000256|ARBA:ARBA00012022, ECO:0000256|RuleBase:RU362038};
DE AltName: Full=Homoaconitate hydratase {ECO:0000256|ARBA:ARBA00032706, ECO:0000256|RuleBase:RU362038};
GN ORFNames=DICSQDRAFT_155148 {ECO:0000313|EMBL:EJF61369.1};
OS Dichomitus squalens (strain LYAD-421) (Western red white-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Dichomitus.
OX NCBI_TaxID=732165 {ECO:0000313|EMBL:EJF61369.1, ECO:0000313|Proteomes:UP000053319};
RN [1] {ECO:0000313|EMBL:EJF61369.1, ECO:0000313|Proteomes:UP000053319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LYAD-421 SS1 {ECO:0000313|EMBL:EJF61369.1,
RC ECO:0000313|Proteomes:UP000053319};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
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:0000256|ARBA:ARBA00003422,
CC ECO:0000256|RuleBase:RU362038}.
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 Evidence={ECO:0000256|ARBA:ARBA00029338,
CC ECO:0000256|RuleBase:RU362038};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|RuleBase:RU362038};
CC Note=Binds 1 [4Fe-4S] cluster per subunit.
CC {ECO:0000256|RuleBase:RU362038};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC pathway; L-alpha-aminoadipate from 2-oxoglutarate: step 3/5.
CC {ECO:0000256|ARBA:ARBA00005106, ECO:0000256|RuleBase:RU362038}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173,
CC ECO:0000256|RuleBase:RU362038}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|RuleBase:RU362038}.
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DR EMBL; JH719410; EJF61369.1; -; Genomic_DNA.
DR RefSeq; XP_007365814.1; XM_007365752.1.
DR AlphaFoldDB; R7SYV4; -.
DR GeneID; 18837458; -.
DR KEGG; dsq:DICSQDRAFT_155148; -.
DR HOGENOM; CLU_006714_3_1_1; -.
DR OMA; LCDADNI; -.
DR OrthoDB; 1122834at2759; -.
DR UniPathway; UPA00033; UER01027.
DR Proteomes; UP000053319; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004409; F:homoaconitate hydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR Gene3D; 3.20.19.10; Aconitase, domain 4; 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; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR InterPro; IPR004418; Homoaconitase_mito.
DR NCBIfam; TIGR00139; h_aconitase; 1.
DR PANTHER; PTHR43822:SF25; HOMOACONITASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43822; HOMOACONITASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00330; Aconitase; 1.
DR Pfam; PF00694; Aconitase_C; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR SUPFAM; SSF52016; LeuD/IlvD-like; 1.
DR PROSITE; PS01244; ACONITASE_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU362038};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU362038};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU362038};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU362038};
KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154,
KW ECO:0000256|RuleBase:RU362038};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU362038};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW ECO:0000256|RuleBase:RU362038};
KW Reference proteome {ECO:0000313|Proteomes:UP000053319};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946,
KW ECO:0000256|RuleBase:RU362038}.
FT DOMAIN 51..473
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 590..645
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 730 AA; 77721 MW; A406EF4663A0F6B1 CRC64;
MRIPARWGRR SLISLRGFAT VSSGSPRIPQ TVIEKVVQRY AVDLPAGKAV KAGDYVMIRP
EHVMTHDNTG PVISKFKSIG ATRIHNPKQL VFTLDHDVQN KSSKNLSKYA SIEAFARQHG
IDFYPAGRGI GHQVLVEEGY AFPHTLTVAS DSHSNMYGGI GCVGTPIVRT DAAALWATGK
TWWQVPRMIK VELRGRLPHG VTGKDVIVAL CGYFNKDEVL NGAIEFTGDG VSALSVDDRL
TIANMTTEWG ALAGVFPVDD VTLEWYERTL KRLEFRTFAS PAVSSSIPPP PEHPRINRAR
LDAIRATNLR SDPDAAYASH LVLDLSTLVP HVSGPNSVKV STPLPALESK HIPIQKAYLL
SCTNARASDI AAAAAVIKGR KVAPGVEFYV AAASSEVQLD AEKRGDWETL VLAGAKPLPA
GCGPCIGLGV GLLQEGETGI SATNRNYKGR MGHPNAQAYL ASPAVVAASA IKGYIASPDS
LDPSSLPPPG APKFSLVNPA QVESAPDTVP AAEEPVLDGF PASFSGPLLF APQDNLNTDA
LYPGKYTYQD DITLARQAEV VMENYDPAFA TLVASIRAKQ PESSDAFVKQ GVVLVSGYNF
GTGSSREQAA TALKAAGVPL VIAGSFGDIF KRNAINNGLV CVECPALVAD LTRSYARDGK
RGAGGIDGEL TVDRGHEVDV RVAEGRVDVK WPSGETKSYT VGRVGASVQE LWICGGLEGY
VLKSIKEAEA
//
