ID E9E9I1_METAQ Unreviewed; 336 AA.
AC E9E9I1;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=L-threonine 3-dehydrogenase {ECO:0000313|EMBL:EFY87421.1};
GN ORFNames=MAC_06529 {ECO:0000313|EMBL:EFY87421.1};
OS Metarhizium acridum (strain CQMa 102).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=655827 {ECO:0000313|Proteomes:UP000002499};
RN [1] {ECO:0000313|EMBL:EFY87421.1, ECO:0000313|Proteomes:UP000002499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CQMa 102 {ECO:0000313|EMBL:EFY87421.1,
RC ECO:0000313|Proteomes:UP000002499};
RX PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y.,
RA Wang C.;
RT "Genome sequencing and comparative transcriptomics of the model
RT entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL PLoS Genet. 7:E1001264-E1001264(2011).
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; GL698527; EFY87421.1; -; Genomic_DNA.
DR RefSeq; XP_007812869.1; XM_007814678.1.
DR AlphaFoldDB; E9E9I1; -.
DR STRING; 655827.E9E9I1; -.
DR GeneID; 19250840; -.
DR KEGG; maw:MAC_06529; -.
DR eggNOG; KOG0024; Eukaryota.
DR HOGENOM; CLU_026673_11_0_1; -.
DR InParanoid; E9E9I1; -.
DR OMA; QFGVADY; -.
DR OrthoDB; 2084524at2759; -.
DR Proteomes; UP000002499; 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:UP000002499};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 38..125
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 165..295
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 336 AA; 36944 MW; 618A5BA6A9E9BB7C CRC64;
MANLPKQMKA LRYEKPEDWS IVTVPLPELR DSDVLVQHIH EGEFIAKFPL IPGHETVGVI
AAVGKNVKGF QIGDRVAADN SELCNECFYC RRGQLLLCEN FNAHGVTMNG GFAEYCAYPA
AKVFRIQNLN WVDATLLEPA SCACHGLEKI RPKLGSHVLM FGAGPTGLML AQLLRQNGGC
QVTIAAPKGL KMDLAKSLDA ADTYIELSRE SPQAQFDQLK KDNPYGFDIV VEATGSVKIL
EDAINYVRRG GTLVVYGVYA NADRVSWPPA KIFGDEITII GSFSETYMFP ATIDYLDSGK
VKTKGIVNKT FKLEEFDKAL ESIKDKTAIK AAIVFE
//
