UniProt: A0A177CKD3

Database: UniProt
Entry: A0A177CKD3_9PLEO

LinkDB:  A0A177CKD3_9PLEO 
Original site:  A0A177CKD3_9PLEO

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Ontology (5)   
   GO (5)   
Gene (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (11)   
   InterPro (8)   
   Pfam (2)   
   PROSITE (1)   
All databases (19)   

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ID   A0A177CKD3_9PLEO        Unreviewed;       823 AA.
AC   A0A177CKD3;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Aconitate hydratase, mitochondrial {ECO:0000256|RuleBase:RU362107};
DE            Short=Aconitase {ECO:0000256|RuleBase:RU362107};
DE            EC=4.2.1.- {ECO:0000256|RuleBase:RU362107};
GN   ORFNames=CC84DRAFT_1117533 {ECO:0000313|EMBL:OAG07300.1};
OS   Paraphaeosphaeria sporulosa.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC   Paraphaeosphaeria.
OX   NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG07300.1, ECO:0000313|Proteomes:UP000077069};
RN   [1] {ECO:0000313|EMBL:OAG07300.1, ECO:0000313|Proteomes:UP000077069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG07300.1,
RC   ECO:0000313|Proteomes:UP000077069};
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   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|RuleBase:RU362107};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit.
CC       {ECO:0000256|RuleBase:RU362107};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173,
CC       ECO:0000256|RuleBase:RU362107}.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC       {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|RuleBase:RU362107}.
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DR   EMBL; KV441551; OAG07300.1; -; Genomic_DNA.
DR   RefSeq; XP_018037665.1; XM_018175497.1.
DR   AlphaFoldDB; A0A177CKD3; -.
DR   STRING; 1460663.A0A177CKD3; -.
DR   GeneID; 28758983; -.
DR   InParanoid; A0A177CKD3; -.
DR   OrthoDB; 3266779at2759; -.
DR   Proteomes; UP000077069; 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:0003994; F:aconitate hydratase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   Gene3D; 3.40.1060.10; Aconitase, Domain 2; 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; IPR015932; Aconitase_dom2.
DR   InterPro; IPR006248; Aconitase_mito-like.
DR   InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR   NCBIfam; TIGR01340; aconitase_mito; 1.
DR   PANTHER; PTHR43160; ACONITATE HYDRATASE B; 1.
DR   PANTHER; PTHR43160:SF2; HOMOCITRATE DEHYDRATASE, MITOCHONDRIAL; 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   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU362107};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU362107};
KW   Lyase {ECO:0000256|RuleBase:RU362107};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU362107};
KW   Mitochondrion {ECO:0000256|RuleBase:RU362107};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077069};
KW   Transit peptide {ECO:0000256|RuleBase:RU362107}.
FT   DOMAIN          102..529
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          611..738
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   823 AA;  88377 MW;  4D29C74AF058822C CRC64;
     MRSPVMRAGQ AANCRSLLHA SLRTSPVPLR RCLATTHNVP PSQKFDIVSR TPPYQKLLGR
     LEEVRRVLGS TRQLTLAEKI LYSHLANPEE SLLSNTNNGK DIRGKANLKL KPDRVAMQDA
     SAQMALLQFM SCGLPSTAVP ASIHCDHMIV GEKGADTDLP NSIAGNKEVF DFLESAAKKY
     GIEFWPPGAG IIHQSVLENY SAPGLMMLGT DSHTPNAGGL GAIAIGVGGA DAVDALVDAP
     WELKAPKVLG VRLEGELSGW ASPKDVILKL AGELTVRGGT GFIIEYFGPG VQTLSSTGMS
     TICNMGAEVG ATTSLFPFSP AHVPYLEATH RGSIAQEALK IANSPMQRNL LRADPEAEYD
     KVITINLSTL EPHINGPFTP DLSTPLSKFK SVVEEKDWPR TFGAGLIGSC TNSSYQDMTR
     SEEIVKQAEA AGLKPKAEFF ITPGSEQIRA TLDRDNTLST FTSAGGIVLA NACGPCIGQW
     KRNDGPAKGE ANAIFTSYNR NFPGRNDGNR GTMNFLASPE LITAMSYSGS TTFNPMTDSI
     PTPSGEAFKF SPPRGSDLPS AGFADGNPEF FATPGIPDPS VEVVVDPNST RLELLDPFPA
     FPNSELKSLR VLYKVKGQCT TDTISAAGPW LKYKGHLTNI SENTLIGAVN AETDEVNVAY
     DVDGRKSGIP DLAKRWKENG QEWLVVAEHN YGEGSAREHA ALQPRFLGGR IILSKSFARI
     HETNLKKQGV VPLTFANEAD YDLLDSCDEV ATRGLLDVLK SGGKGEVELV VKKKDGSEKV
     IKTKHTLSED QCGFVLAGSA LNLLARSAAE AREEVTRQSE LSD
//

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