ID C5FFT5_ARTOC Unreviewed; 348 AA.
AC C5FFT5;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=L-threonine 3-dehydrogenase {ECO:0000313|EMBL:EEQ29620.1};
GN ORFNames=MCYG_02439 {ECO:0000313|EMBL:EEQ29620.1};
OS Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX NCBI_TaxID=554155 {ECO:0000313|EMBL:EEQ29620.1, ECO:0000313|Proteomes:UP000002035};
RN [1] {ECO:0000313|Proteomes:UP000002035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4605 / CBS 113480 {ECO:0000313|Proteomes:UP000002035};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|RuleBase:RU361277}.
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DR EMBL; DS995702; EEQ29620.1; -; Genomic_DNA.
DR RefSeq; XP_002849505.1; XM_002849459.1.
DR AlphaFoldDB; C5FFT5; -.
DR STRING; 554155.C5FFT5; -.
DR GeneID; 9223364; -.
DR VEuPathDB; FungiDB:MCYG_02439; -.
DR eggNOG; KOG0024; Eukaryota.
DR HOGENOM; CLU_026673_11_0_1; -.
DR OMA; QFGVADY; -.
DR OrthoDB; 2084524at2759; -.
DR Proteomes; UP000002035; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08234; threonine_DH_like; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43401; L-THREONINE 3-DEHYDROGENASE; 1.
DR PANTHER; PTHR43401:SF2; L-THREONINE 3-DEHYDROGENASE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000002035};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 33..138
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 177..308
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 348 AA; 37703 MW; A402A31DFDC1A9DF CRC64;
MASQLPKNMK ALRYSKPEEF GIVNIPLPEL RENDVMIKVK ACGVCGTDLH IHEGEFLAKF
PLVPGHETVG VVAAVGPKVK GFNIGDRVVA DNSELCGECF YCRRGEELLC EHFEAHGVTM
NGGFAEYCAY PAGRVFKIQN LSDVDATLLE PASCAAHGLD KISPKMGSTV LMFGAGPTGL
VLAQMLRLNG GCKVVIAAPE GLKMNLAKSL DAADEYIELS RKDPSAQFEA LKAANPYGFD
IVVEATGSVK ILEDAINYCR RGGKLVVYGV YANKDRVSWA PSKIFGDEIT IIGSFSETYK
FPAAIDYLDS GKVKVKGIVN KTFKLEQWAE CLESMKNKSA IKAAITFD
//
