ID Q2H7J0_CHAGB Unreviewed; 600 AA.
AC Q2H7J0;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Dihydroxy-acid dehydratase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CHGG_05375 {ECO:0000313|EMBL:EAQ88756.1};
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901 {ECO:0000313|EMBL:EAQ88756.1, ECO:0000313|Proteomes:UP000001056};
RN [1] {ECO:0000313|Proteomes:UP000001056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970
RC {ECO:0000313|Proteomes:UP000001056};
RX PubMed=25720678; DOI=10.1128/genomeA.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
CC -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC {ECO:0000256|ARBA:ARBA00006486}.
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DR EMBL; CH408031; EAQ88756.1; -; Genomic_DNA.
DR RefSeq; XP_001221470.1; XM_001221469.1.
DR AlphaFoldDB; Q2H7J0; -.
DR STRING; 306901.Q2H7J0; -.
DR GeneID; 4390061; -.
DR VEuPathDB; FungiDB:CHGG_05375; -.
DR eggNOG; KOG2448; Eukaryota.
DR HOGENOM; CLU_014271_4_1_1; -.
DR InParanoid; Q2H7J0; -.
DR OMA; YLMEDLY; -.
DR OrthoDB; 238at2759; -.
DR Proteomes; UP000001056; Unassembled WGS sequence.
DR GO; GO:0016836; F:hydro-lyase activity; IEA:InterPro.
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; PTHR21000:SF13; DIHYDROXY-ACID DEHYDRATASE; 1.
DR PANTHER; PTHR21000; DIHYDROXY-ACID DEHYDRATASE DAD; 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.
DR PROSITE; PS00887; ILVD_EDD_2; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Reference proteome {ECO:0000313|Proteomes:UP000001056}.
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 600 AA; 63293 MW; B39353F8E3C0D6EF CRC64;
MAPHADETPS GRNSGENEHG NGHSGDRNVP RSGDYLQFES LPPGGPLNRW SQVLTRGHDF
PGAQGHDEEC ATCGHRHRVV GGESVQGYGF YRMTAHVGTG MKFSLQSREI IADSIETVTC
AQRHDANISI PGCDKNMPGV VMAAARHNRP FLMIYGGTIR KGHSNLLDKQ INISTCYEAA
GAFAYNRLEA KCKKPSGADA TPSDVMEDIE RHACPGAGAC GGMYTANTMA TAIEAMGLTL
PGSSSFPATS PEKRRECERA AEAIRTCMEK DIRARDLMTR WAFENALVVT IVLGGSTNAV
LHFLAMANSA DVPLTLEDIA RTSNRTPFLA DLAPSGRYYM EDLYDVGGTP AVLKMLIAAN
LIDGSIPTVT GKTLAENVQS WPSLPPTQTI LRPLSNPIKP TGHIRVLHGN LSPGGAVAKI
TGKEGLSFTG SVRVFNKEQA LSDALAQNTI RPDAGNLVLV VRYEGPKGGP GMPEQLKASA
AIMGAGLTNV ALVTDGRYSG ASHGFIVGHV VPEAAVGGPI ALVEEGDVVT IDAVGNRIDV
VEIPGVGAGG DVVGRELERP EGRAWSPPKM KPTRGVLAKY ARLVGDASHG AVTDVGGSAW
//
