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Database: UniProt
Entry: A0A1V6TWZ8_9EURO
LinkDB: A0A1V6TWZ8_9EURO
Original site: A0A1V6TWZ8_9EURO 
ID   A0A1V6TWZ8_9EURO        Unreviewed;       653 AA.
AC   A0A1V6TWZ8;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Ig-like domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PENFLA_c003G08736 {ECO:0000313|EMBL:OQE30544.1};
OS   Penicillium flavigenum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=254877 {ECO:0000313|EMBL:OQE30544.1, ECO:0000313|Proteomes:UP000191342};
RN   [1] {ECO:0000313|Proteomes:UP000191342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 14082 {ECO:0000313|Proteomes:UP000191342};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
CC   -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC       {ECO:0000256|ARBA:ARBA00006486}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OQE30544.1}.
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DR   EMBL; MLQL01000003; OQE30544.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6TWZ8; -.
DR   STRING; 254877.A0A1V6TWZ8; -.
DR   OrthoDB; 238at2759; -.
DR   Proteomes; UP000191342; Unassembled WGS sequence.
DR   GO; GO:0016836; F:hydro-lyase activity; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
DR   GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR   Gene3D; 3.50.30.80; IlvD/EDD C-terminal domain-like; 1.
DR   InterPro; IPR042096; Dihydro-acid_dehy_C.
DR   InterPro; IPR000581; DiOHA_6PGluconate_deHydtase.
DR   InterPro; IPR020558; DiOHA_6PGluconate_deHydtase_CS.
DR   InterPro; IPR037237; IlvD/EDD_N.
DR   PANTHER; PTHR43183:SF1; HYPOTHETICAL DIHYDROXY-ACID DEHYDRATASE (EUROFUNG)-RELATED; 1.
DR   PANTHER; PTHR43183; HYPOTHETICAL DIHYDROXYACID DEHYDRATASE (EUROFUNG)-RELATED; 1.
DR   Pfam; PF00920; ILVD_EDD; 1.
DR   SUPFAM; SSF143975; IlvD/EDD N-terminal domain-like; 1.
DR   SUPFAM; SSF52016; LeuD/IlvD-like; 1.
DR   PROSITE; PS00886; ILVD_EDD_1; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191342}.
FT   COILED          25..52
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   653 AA;  71327 MW;  9029B9FF060EA888 CRC64;
     MACSDKKSCE GCSCSDDAKP QAINIEDCLS ELQALRRRNQ ELETRMGVAS KADNAQVPVK
     QPGRTLRSSA WFDCRSNPGM TAIYMERYFN YGITKEELMS GKPMIGIAQT GSDIAPCNRH
     HIELSKRVRE GIRTAGGIPF EFPTHPIQET SRRPTATLDR NLAYLGLVEI LTGYFLDGVV
     LLTGCDKTTP ACLMAAATMN IPAICMNVGP MLNGYSKETL TGAGTVLWHG RELYATGDID
     EHEFMDYIAR GTPSVGHCNT MGTASTMNAL AESLGMALPG SAAIPAAYRH RAQCAYETGK
     RIVEMVEADR KPCDIMTREA FENAIVANAA IGGSTNAPIH INAIAQHAGV EVSMDDWDTL
     GSTIPLLLNM QPSGEYLGEE YYRAGGLPAI MAELLDQGKL NGDALTCNGK TLAENVRGKH
     TWDRRVIKSY DDPLMKDAGF AHLKGNLFDS AIMKTCVISP AFRKRYLSNP DDPEAFEGSV
     VVFDGPEDYE HRLENTPHID EKTILVMRGV GPIGYPGAAE VVNMHPPGRL LKEGIDGLFC
     IGDGRQSGTS GSPSILNASP EAAAGGNLAI LKDGDRLRID LRKRRVDMLI TDEEIEHRRK
     ALGTEGYPIL PSGTPWQEIF RQETEQLSNG MVLRKAVKYQ RLAQEGQPLR HNH
//
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