LYS4_ASPFU
ID LYS4_ASPFU Reviewed; 777 AA.
AC Q4WUL6; Q96VU1;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Homoaconitase, mitochondrial;
DE EC=4.2.1.36;
DE AltName: Full=Homoaconitate hydratase;
DE Flags: Precursor;
GN Name=lys4; Synonyms=lysF; ORFNames=AFUA_5G08890;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 46645 / NCPF 2109;
RX PubMed=15052376; DOI=10.1007/s00203-004-0667-3;
RA Liebmann B., Muehleisen T.W., Mueller M., Hecht M., Weidner G., Braun A.,
RA Brock M., Brakhage A.A.;
RT "Deletion of the Aspergillus fumigatus lysine biosynthesis gene lysF
RT encoding homoaconitase leads to attenuated virulence in a low-dose mouse
RT infection model of invasive aspergillosis.";
RL Arch. Microbiol. 181:378-383(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [3]
RP FUNCTION, AND INDUCTION.
RX PubMed=23106124; DOI=10.1111/mmi.12076;
RA Fazius F., Shelest E., Gebhardt P., Brock M.;
RT "The fungal alpha-aminoadipate pathway for lysine biosynthesis requires two
RT enzymes of the aconitase family for the isomerization of homocitrate to
RT homoisocitrate.";
RL Mol. Microbiol. 86:1508-1530(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:0000269|PubMed:23106124}.
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 -!- INDUCTION: Expression is slightly increased during growth on ethanol.
CC {ECO:0000269|PubMed:23106124}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000305}.
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DR EMBL; AJ320167; CAC48042.1; -; Genomic_DNA.
DR EMBL; AAHF01000003; EAL91710.1; -; Genomic_DNA.
DR RefSeq; XP_753748.1; XM_748655.1.
DR AlphaFoldDB; Q4WUL6; -.
DR SMR; Q4WUL6; -.
DR STRING; 746128.CADAFUBP00005524; -.
DR EnsemblFungi; EAL91710; EAL91710; AFUA_5G08890.
DR GeneID; 3511364; -.
DR KEGG; afm:AFUA_5G08890; -.
DR VEuPathDB; FungiDB:Afu5g08890; -.
DR eggNOG; KOG0453; Eukaryota.
DR HOGENOM; CLU_006714_3_1_1; -.
DR InParanoid; Q4WUL6; -.
DR OMA; VMIRPEH; -.
DR OrthoDB; 265826at2759; -.
DR UniPathway; UPA00033; UER01027.
DR PHI-base; PHI:2520; -.
DR PHI-base; PHI:362; -.
DR Proteomes; UP000002530; Chromosome 5.
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:0010106; P:cellular response to iron ion starvation; IEP:AspGD.
DR GO; GO:0009085; P:lysine biosynthetic process; IMP:AspGD.
DR GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IEA:UniProtKB-UniPathway.
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.
PE 2: Evidence at transcript level;
KW Amino-acid biosynthesis; Iron; Iron-sulfur; Lyase; Lysine biosynthesis;
KW Metal-binding; Mitochondrion; Reference proteome; Transit peptide.
FT TRANSIT 1..35
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 36..777
FT /note="Homoaconitase, mitochondrial"
FT /id="PRO_0000247916"
FT REGION 47..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 398
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 466
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 469
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT CONFLICT 51
FT /note="T -> A (in Ref. 1; CAC48042)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="K -> N (in Ref. 1; CAC48042)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 777 AA; 83716 MW; 4C2BCCA2DE0804A4 CRC64;
MFKRTGSLLL RCRASRVPVI GRPLISLSTS STSLSLSRPR SFATTSLRRY TEASSSTTQT
SPSSSSWPAP DAAPRVPQTL TEKIVQAYSL GLAEGQYVKA GDYVMLSPHR CMTHDNSWPT
ALKFMAIGAS KVHNPDQIVM TLDHDVQNKS EKNLKKYESI EKFAKQHGID FYPAGHGVGH
QIMIEEGYAF PGTVTVASDS HSNMYGGVGC LGTPMVRTDA ATIWATGRTW WKVPPIAKVQ
FTGTLPEGVT GKDVIVALSG LFNKDEVLNY AIEFTGSEET MKSLSVDTRL TIANMTTEWG
ALTGLFPIDS TLEQWLRHKA ATASRTETAR RFAEERINEL FANPTVADRG ARYAKYLYLD
LSTLSPYVSG PNSVKVATPL DELEKHKLKI DKAYLVSCTN SRASDIAAAA KVFKDAVART
GGPVRVADGV EFYVAAASKA EQKIAEEAGD WQALMDAGAI PLPAGCAVCI GLGAGLLKEG
EVGISASNRN FKGRMGSPDA KAYLASPEVV AASALNGVIS GPGIYKRPED WTGVSIGEGE
VVESGSRIDT TLEAMEKFIG QLDSMIDSSS KAVMPEESTG SGATEVDIVP GFPEKIEGEI
LFLDADNIST DGIYPGKYTY QDDVTKDKMA QVCMENYDPA FSGIARAGDI FVSGFNFGCG
SSREQAATSI LAKQLPLVVA GSIGNTFSRN AVNNALPLLE MPRLIERLRE AFGSEKQPTR
RTGWTFTWNV RTSQVTVQEG PGGETWSQSV PAFPPNLQDI IAQGGLEKWV KKEISKA
