ID R1I3S8_9PSEU Unreviewed; 391 AA.
AC R1I3S8;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Glutathione-dependent formaldehyde dehydrogenase {ECO:0000313|EMBL:EOD70430.1};
GN ORFNames=H480_01057 {ECO:0000313|EMBL:EOD70430.1};
OS Amycolatopsis vancoresmycina DSM 44592.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=1292037 {ECO:0000313|EMBL:EOD70430.1, ECO:0000313|Proteomes:UP000014139};
RN [1] {ECO:0000313|EMBL:EOD70430.1, ECO:0000313|Proteomes:UP000014139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44592 {ECO:0000313|EMBL:EOD70430.1,
RC ECO:0000313|Proteomes:UP000014139};
RA Kumar S., Kaur N., Kaur C., Raghava G.P.S., Mayilraj S.;
RT "Draft genome sequence of Amycolatopsis vancoresmycina strain DSM 44592T.";
RL Submitted (FEB-2013) 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:EOD70430.1}.
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DR EMBL; AOUO01000011; EOD70430.1; -; Genomic_DNA.
DR RefSeq; WP_003055102.1; NZ_AOUO01000011.1.
DR AlphaFoldDB; R1I3S8; -.
DR PATRIC; fig|1292037.4.peg.208; -.
DR eggNOG; COG1063; Bacteria.
DR OrthoDB; 241504at2; -.
DR Proteomes; UP000014139; 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 27..150
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 198..268
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 391 AA; 42326 MW; 7360E70159D0EF2D CRC64;
MRANTWSGRN KVEVRDVPDP RILNRRDAIV RITSTAICGS DLHLVDGYIP TMQDGDVMGH
EFMGEVVEVG AGVDPGRLRV GDRVVVPFPI ACGACGACAA ELYSCCENSN PNAGIAEKMF
GHPVAGIFGY SHLTGGFAGG QAEYARVPFA DVGPIKIESD LTDEQVLFLS DILPTGYMGA
EMCDIRSSDV VAVWGAGPVG QFAMDSARLL GAAKVIAIDK EPYRLELAER AGHLPVNFEE
VDVRSRLLEL TGGRGPDKCI DAVGLEATHG SAHVAAYDRV KQAVRSETER PHALRQAILS
CRSGGVVSVI GVYGGLLDKF PAGAWMNRSL TLRTGQCHVQ RYMEPLLRRI ENGELDPTRI
ITHTLPLEEA DRGFELFKNK QDNCEKVVLK P
//
