ID L8G800_PSED2 Unreviewed; 757 AA.
AC L8G800;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=GMDG_08602 {ECO:0000313|EMBL:ELR08116.1};
OS Pseudogymnoascus destructans (strain ATCC MYA-4855 / 20631-21) (Bat
OS white-nose syndrome fungus) (Geomyces destructans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=658429 {ECO:0000313|EMBL:ELR08116.1, ECO:0000313|Proteomes:UP000011064};
RN [1] {ECO:0000313|Proteomes:UP000011064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4855 / 20631-21 {ECO:0000313|Proteomes:UP000011064};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C.A., Blehert D.S., Lorch J.M., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The genome sequence of Geomyces destructans 20631-21.";
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00007185, ECO:0000256|RuleBase:RU362038}.
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DR EMBL; GL573600; ELR08116.1; -; Genomic_DNA.
DR RefSeq; XP_012747064.1; XM_012891610.1.
DR AlphaFoldDB; L8G800; -.
DR STRING; 658429.L8G800; -.
DR VEuPathDB; FungiDB:GMDG_08602; -.
DR HOGENOM; CLU_006714_3_1_1; -.
DR InParanoid; L8G800; -.
DR OrthoDB; 1122834at2759; -.
DR UniPathway; UPA00033; UER01027.
DR Proteomes; UP000011064; 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 CDD; cd01674; Homoaconitase_Swivel; 1.
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 InterPro; IPR039386; Homoaconitase_swivel.
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; PS00450; ACONITASE_1; 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:UP000011064};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946,
KW ECO:0000256|RuleBase:RU362038}.
FT DOMAIN 72..493
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 561..683
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 757 AA; 81025 MW; 3B914D24A3733538 CRC64;
MNTRATQMRV NMQSLGPMRP RALPIVAGRL FHGSIVYRMS NASLSSLDKA QTLTEKIVQR
YSLGLPKDKV VKSGDFVTLS PHKCMTHDNS WPVASKFMSI GATKVNDPSQ MVFTLDHDVQ
NKSDTNLKKY QQIETFAEQQ GIRFFGAGKG IGHQLMIEEG YAWPGTVTVA SDSHSNMYGG
VGCLGTPIVR TDAASIWATG RTWWQVPPVA KCHFTGVLPV GVTGKDVIVA LCGLFNRDEV
LNHAIEFTGS EETMRSLPVD DRLAIANMTT EWGALSGLFP IDSVLLSWLR YKATTAAMYE
SGTGSKDRFS HAIIENLTTS PIRADRGATY AKSLFLDLST LSPYVSGPNS VKVATPLRDL
EAQKINIQKA YLVSCTNSRA SDLAAAAKVF TEAAKTGASP KVAPNVELYI AAASLAEQQT
AEEAGDWGVL LEAGAKPLPS GCGPCIGLGT GLLEAGEVGI SASNRNFKGR MGSPDAKAYL
ASPEVVAASA LSGYISCPGF YEAPEGVTKV VLGEGTGNIE ADKATSIEEA LAKLISEADS
LVDNAQSSLF GKAEEVTTEK EGAGLTEIVA GFPDKVRGEI VFCDADNLNT DAIYPGKYTY
QDGVSIEKMA EVCMENYDKE FGSVIREGDI LVSGFNFGCG SSREQAATAI LASKIPLVVS
GSFGNIFSRN SINNALLGLE VPRLVEGLRK QFSGADKALT RRTGWTFEWD VRRSEITVQE
GEGGANWTQA VGQMPPNVQE IIARGGLEKW VKAEIGL
//
