ID A0A1H0FKX6_9ACTN Unreviewed; 391 AA.
AC A0A1H0FKX6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Threonine dehydrogenase {ECO:0000313|EMBL:SDN95428.1};
GN ORFNames=SAMN05428965_2080 {ECO:0000313|EMBL:SDN95428.1};
OS Geodermatophilus sp. DSM 45219.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=1881103 {ECO:0000313|EMBL:SDN95428.1, ECO:0000313|Proteomes:UP000198730};
RN [1] {ECO:0000313|EMBL:SDN95428.1, ECO:0000313|Proteomes:UP000198730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45219 {ECO:0000313|EMBL:SDN95428.1,
RC ECO:0000313|Proteomes:UP000198730};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC 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; FNIQ01000003; SDN95428.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0FKX6; -.
DR STRING; 1881103.SAMN05428965_2080; -.
DR OrthoDB; 3399630at2; -.
DR Proteomes; UP000198730; 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; cd08283; FDH_like_1; 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; PTHR42813:SF2; DEHYDROGENASE, ZINC-CONTAINING, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G02810)-RELATED; 1.
DR PANTHER; PTHR42813; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE; 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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 26..148
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 196..265
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 391 AA; 42063 MW; D683F80D495598BC CRC64;
MRAATWTGVN EVSVETVPDP TILNDHDVIL KVSRTTTCGS DLHLLGGYIP FMRAGDVLGH
EFMGEVVEVG RGVRDRRIGD RVVVNSFIAC GKCWYCTQEL YSLCDNGNPN PGITEALWGQ
SPGGCFGYSH AMGGWAGSHA EYIRVPYADV GAFVVPEGVS DERALFASDA VSTGWMGADL
AGTKPGDVVA VWGAGGVGQM AARAAMLLGA ERVYVIDRLP ERLAQVREHV GAEAIDYSRT
DVLAELREVT GGRGPDVCIE AVGMEAHSLG VQGAYDQVKQ QLRLQTDRPS AVREAILACR
KGGSVFVLGV YAQMVDKFPL GALMNKGLTV RGAQVHGQRY MPRILDHMAR GELTTEHLAT
HVMPLEDAAR GYRVFKDKAD GCVRSVFLPN G
//