ID A0A2S5W106_9MICO Unreviewed; 391 AA.
AC A0A2S5W106;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Glutathione-dependent formaldehyde dehydrogenase {ECO:0000313|EMBL:PPF79329.1};
GN ORFNames=C5B96_13105 {ECO:0000313|EMBL:PPF79329.1};
OS Subtercola sp. Z020.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Subtercola.
OX NCBI_TaxID=2080582 {ECO:0000313|EMBL:PPF79329.1, ECO:0000313|Proteomes:UP000238959};
RN [1] {ECO:0000313|EMBL:PPF79329.1, ECO:0000313|Proteomes:UP000238959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z020 {ECO:0000313|EMBL:PPF79329.1,
RC ECO:0000313|Proteomes:UP000238959};
RA Davis E.W.II., Tabima J.F., Weisberg A.J., Lopes L.D., Wiseman M.S.,
RA Wiseman M.S., Pupko T., Belcher M.S., Sechler A.J., Tancos M.A.,
RA Schroeder B.K., Murray T.D., Luster D.G., Schneider W.L., Rogers E.,
RA Andreote F.D., Grunwald N.J., Putnam M.L., Chang J.H.;
RT "Bacteriophage NCPPB3778 and a type I-E CRISPR drive the evolution of the
RT US Biological Select Agent, Rathayibacter toxicus.";
RL Submitted (FEB-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:PPF79329.1}.
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DR EMBL; PSTT01000100; PPF79329.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S5W106; -.
DR OrthoDB; 241504at2; -.
DR Proteomes; UP000238959; 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..146
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; 41963 MW; 262022FD2AFD6FA3 CRC64;
MKALCWTGVN KVEVEKVDDP TILNDRDVIV KVRLSTTCGS DLHLLGGYIP TMRSGDVLGH
EFMGEVVEVG SAVKNHRIGD RVVVCSFIAC GKCWYCTHEQ FSLCDNGNPN PGITETMWGS
PIGGCFAYSH ALGGFAGSHA EYIRVPFADQ GAFTVPDGVS DLAALFASDA APTGWTGADL
AGITPGDTVA VWGAGGVGQM AARAAMLLGA EQVVVIDRLP ERLDQVRRFI GAETLDYTRE
NIFAELKERT GGRGPDVCIE AVGMEAHSTG PAYLYDQVKQ QLRLQSDRPT ALREAIYACR
KGGSLFALGV FGGVVDKFPF GAIMNKGMTV RGAQQHGHRY IPAILDRIAA GEIDTEHLAT
HILPLDDGPR GYEMFKNKED GCVRAVFQPA A
//
