ID A0A177DCB1_ALTAL Unreviewed; 838 AA.
AC A0A177DCB1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=CC77DRAFT_1042638 {ECO:0000313|EMBL:OAG17474.1};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG17474.1, ECO:0000313|Proteomes:UP000077248};
RN [1] {ECO:0000313|EMBL:OAG17474.1, ECO:0000313|Proteomes:UP000077248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG17474.1,
RC ECO:0000313|Proteomes:UP000077248};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) 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; KV441486; OAG17474.1; -; Genomic_DNA.
DR RefSeq; XP_018382895.1; XM_018527274.1.
DR AlphaFoldDB; A0A177DCB1; -.
DR STRING; 5599.A0A177DCB1; -.
DR GeneID; 29112868; -.
DR KEGG; aalt:CC77DRAFT_1042638; -.
DR VEuPathDB; FungiDB:CC77DRAFT_1042638; -.
DR OMA; WVKNSIS; -.
DR OrthoDB; 1122834at2759; -.
DR UniPathway; UPA00033; UER01027.
DR Proteomes; UP000077248; 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:UP000077248};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946,
KW ECO:0000256|RuleBase:RU362038}.
FT DOMAIN 80..536
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 615..728
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT REGION 590..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 738..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 838 AA; 89687 MW; 3957B018DDCE5692 CRC64;
MAMSLRAARL LGRRQLAPRA GLALRAASFS PRPCLAPRTF ATTASRREAQ DVFPSMKENP
AASFLSSLNE TPKTPQTLTE KIVQRHAVGV AQGKVLRSGD YVTLQPHKCM THDNSWPVAL
KFMGIGATKI NDPKQIVMTL DHDVQNKTEK NLKKYSQIEE FAQKQDVVFY PAGRGIGHQI
MVEEGYAWPG TLAVASDSHS NMYGGIGCLG TPVVRTDAAS IWATGKTWWQ IPPVAKVTLN
GKMPQGVTGK DVIVALAGLF NKDEVLNHAI EFTGTDETLG SIPIDDRLTI ANMTTEWGAL
TGLFPIDSTL HGWLRARATL AAMGEGQAKD HHQQQFIHER IDQLFTATGI VGEKMGHIFK
PALAADKGAV YAKELFLDLS TLSPYVSGPN SVKVATPLLE LQSQNIPINK AYLVSCTNSR
ASDLAAAANV FKDAAVLNGG KIPKIPDNVN FYIAAASIPE QKAAEEAGDW QALLEAGAQP
LPSGCGPCIG LGTGLLEPGE VGISASNRNF KGRMGSPDAK AYLASPEVVA ASALSGKISG
PGWYEAPEGY AGVRRGEGDG VPEEERMMTI EDMLEKAIKD AEAAIDTFGN AEPETQSVDP
PATPGSEAEP LTEILPGFPE KISGEIVFCD ADNINTDGIY PGKYTYQDDV TREKMAEVCM
ENYDPNFGQI AKAGDVLVSG FNFGCGSSRE QAATAILAKG IPLVVSGSFG NIFSRNSINN
ALMGVEVPKL ANRLREVFSS QDASSSQQAI KEPSNNRESL DSPPPAAAAQ PSQAKQLTRR
TGWTLEWDVR RSTVSVQEGP NGAKWNVKVG ELPPNVQEII ALGGLENWVK KEIGSPPS
//
