ID W7J037_9PSEU Unreviewed; 394 AA.
AC W7J037; A0A8E2X627;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Threonine dehydrogenase {ECO:0000313|EMBL:EWC62322.1, ECO:0000313|EMBL:PWW66857.1};
GN ORFNames=DFQ13_101375 {ECO:0000313|EMBL:PWW66857.1}, UO65_2309
GN {ECO:0000313|EMBL:EWC62322.1};
OS Actinokineospora spheciospongiae.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinokineospora.
OX NCBI_TaxID=909613 {ECO:0000313|EMBL:EWC62322.1, ECO:0000313|Proteomes:UP000019277};
RN [1] {ECO:0000313|EMBL:EWC62322.1, ECO:0000313|Proteomes:UP000019277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EG49 {ECO:0000313|EMBL:EWC62322.1,
RC ECO:0000313|Proteomes:UP000019277};
RX PubMed=24604655;
RA Harjes J., Ryu T., Abdelmohsen U.R., Moitinho-Silva L., Horn H., Ravasi T.,
RA Hentschel U.;
RT "Draft Genome Sequence of the Antitrypanosomally Active Sponge-Associated
RT Bacterium Actinokineospora sp. Strain EG49.";
RL Genome Announc. 2:e00160-14(2014).
RN [2] {ECO:0000313|EMBL:PWW66857.1, ECO:0000313|Proteomes:UP000247287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8578 {ECO:0000313|EMBL:PWW66857.1,
RC ECO:0000313|Proteomes:UP000247287};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (MAY-2018) 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}.
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:EWC62322.1}.
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DR EMBL; AYXG01000081; EWC62322.1; -; Genomic_DNA.
DR EMBL; QHCP01000001; PWW66857.1; -; Genomic_DNA.
DR RefSeq; WP_035281522.1; NZ_QHCP01000001.1.
DR AlphaFoldDB; W7J037; -.
DR STRING; 909613.UO65_2309; -.
DR PATRIC; fig|909613.9.peg.2315; -.
DR eggNOG; COG1063; Bacteria.
DR OrthoDB; 241504at2; -.
DR Proteomes; UP000019277; Unassembled WGS sequence.
DR Proteomes; UP000247287; 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 Reference proteome {ECO:0000313|Proteomes:UP000019277};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 26..139
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 189..259
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 394 AA; 42384 MW; 58FFE56A8CBB3072 CRC64;
MKAVTWHGKR DVRVDTHPDP VIQDPTDTIV RITSSGLCGS DLHLYEVLGP FLTEGDILGH
EPMGVVEEVG PGVTSLKVGD RVVVPFNVSC GDCFMCGQGL HSQCETTQVR EQGMGASLFG
YTKLYGAVPG GQAELLRVPF ADKLPIKVPE GPPDERFVLL SDVLPTAWQA VQYAAVPKGG
SLAVIGLGPI GDMCTRIARL NGVENVIGID LVDERLARVT ARGVRTLDLR EHGAKLTEAV
RDLTDGRGPD SVIDAVGMEA HGAPVAKLAQ QATGFLPDAL AEKFMRTAGV DRLEALRLAI
DIVRRGGTIS LSGVYGGMAD PLPMLTMFDK QIQLRMGQAN VHRWVDDILP HLTDDDPLGV
DTFATHKVPL SQAPEAYDMF QRKQDGAVKI LFTP
//