ID D4D542_TRIVH Unreviewed; 357 AA.
AC D4D542;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=Alcohol dehydrogenase iron-type/glycerol dehydrogenase GldA domain-containing protein {ECO:0000259|Pfam:PF00465};
GN ORFNames=TRV_02212 {ECO:0000313|EMBL:EFE43019.1};
OS Trichophyton verrucosum (strain HKI 0517).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663202 {ECO:0000313|EMBL:EFE43019.1, ECO:0000313|Proteomes:UP000008383};
RN [1] {ECO:0000313|Proteomes:UP000008383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HKI 0517 {ECO:0000313|Proteomes:UP000008383};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
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:EFE43019.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ACYE01000118; EFE43019.1; -; Genomic_DNA.
DR RefSeq; XP_003023637.1; XM_003023591.1.
DR AlphaFoldDB; D4D542; -.
DR GeneID; 9582183; -.
DR KEGG; tve:TRV_02212; -.
DR HOGENOM; CLU_007207_0_1_1; -.
DR OrthoDB; 1591034at2759; -.
DR Proteomes; UP000008383; Unassembled WGS sequence.
DR GO; GO:0090560; F:2-(3-amino-3-carboxypropyl)histidine synthase activity; IEA:InterPro.
DR GO; GO:0018506; F:maleylacetate reductase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0017183; P:protein histidyl modification to diphthamide; IEA:InterPro.
DR CDD; cd08177; MAR; 1.
DR Gene3D; 3.40.50.1970; -; 1.
DR Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1.
DR InterPro; IPR001670; ADH_Fe/GldA.
DR InterPro; IPR039697; Alcohol_dehydrogenase_Fe.
DR InterPro; IPR016435; DPH1/DPH2.
DR InterPro; IPR034786; MAR.
DR PANTHER; PTHR11496; ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR11496:SF105; REDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G07090)-RELATED; 1.
DR Pfam; PF00465; Fe-ADH; 1.
DR SFLD; SFLDS00032; Radical_SAM_3-amino-3-carboxyp; 1.
DR SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 10..340
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
SQ SEQUENCE 357 AA; 38141 MW; 9F255796DB4C77AD CRC64;
MKPFEYNAHP AHVLFGTGTI KQLSAEIERL GVNSPLLLYT LRQEKLVDDV RRQLQGKVAG
AFDGAVMHVP THVTEKALAY AKEHGADGIV SIGGGSVIGL GKAISLRTGL PHLCVPTTYS
GSEMTPILGE THDGVKSTRT DPKILPAAVI YDVDLTMSMP ASLSATSGMN AIAHAVEALY
AHNGNPIVNL LAREGIRSLS TALPDIVANP QSKSARSDAL YGAWLCGSCL GSVGMALHHK
LCHALGGSFN LPHAETHTAV LPHAVAYNSP NTPEAMTTLA ELLPGSQGDA IRGLNVLMQK
LQVKRGAREF GMKEEDIDKA AEIAMRNVYC NPREVKKDAI RELLRRVWAG EEARADL
//
