ID E1PKQ2_PANVC Unreviewed; 388 AA.
AC E1PKQ2;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE SubName: Full=Glutathione-dependent formaldehyde dehydrogenase {ECO:0000313|EMBL:ADO07977.1};
GN Name=fdh {ECO:0000313|EMBL:ADO07977.1};
GN OrderedLocusNames=Pvag_pPag10149 {ECO:0000313|EMBL:ADO07977.1};
OS Pantoea vagans (strain C9-1) (Pantoea agglomerans (strain C9-1)).
OG Plasmid pPag1 {ECO:0000313|EMBL:ADO07977.1,
OG ECO:0000313|Proteomes:UP000006631}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=712898 {ECO:0000313|EMBL:ADO07977.1, ECO:0000313|Proteomes:UP000006631};
RN [1] {ECO:0000313|EMBL:ADO07977.1, ECO:0000313|Proteomes:UP000006631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C9-1 {ECO:0000313|EMBL:ADO07977.1,
RC ECO:0000313|Proteomes:UP000006631};
RC PLASMID=pPag1 {ECO:0000313|EMBL:ADO07977.1};
RX PubMed=20952567; DOI=10.1128/JB.01122-10;
RA Smits T.H., Rezzonico F., Kamber T., Goesmann A., Ishimaru C.A.,
RA Stockwell V.O., Frey J.E., Duffy B.;
RT "The genome sequence of the biocontrol agent Pantoea vagans strain C9-1.";
RL J. Bacteriol. 192:6486-6487(2010).
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; CP001893; ADO07977.1; -; Genomic_DNA.
DR RefSeq; WP_013356641.1; NC_014561.1.
DR AlphaFoldDB; E1PKQ2; -.
DR KEGG; pva:Pvag_pPag10149; -.
DR eggNOG; COG1063; Bacteria.
DR HOGENOM; CLU_026673_11_3_6; -.
DR OMA; AMYGHRD; -.
DR OrthoDB; 9773078at2; -.
DR Proteomes; UP000006631; Plasmid pPag1.
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|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Plasmid {ECO:0000313|EMBL:ADO07977.1};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 25..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 388 AA; 42502 MW; 0F6351D88CB7AE03 CRC64;
MRALCWNGVN DLSVETVADP GLLNPHDAII RVRLTTTCGS DLHVIDGLIP SMREGDILGH
EFMGEVVEVG RAIKNIRRGD RVVVPSFISC GSCWYCQHQL PSCCDNTHPQ WEKGETVLGH
ATGGIYAYSH AFGGYAGSHA EYVRVPFADN DCFVVPEGVT DEQALFLSDA TPTGYMGADF
CNIHPGDTVV VWGCGGVGLM AQQSAWLMGA HQVIGIDRYP ERLAMARDFA GSITLDYTEV
DVNEVLLELT GGRGPDSCID AVGMEARGEG LSQVYDKTKQ MLHLETDVGA ALRQALYACR
KGGNIAILGV YGVMDKFPLG LMINKSLTIR TAQQHGQRYM HRLLEHVARN ELNPAFMATH
RFPLEEAPRG YEMFKHKEDG CVRAVFVP
//