ID A0A062VP99_9MICO Unreviewed; 388 AA.
AC A0A062VP99;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:KDA05354.1};
GN ORFNames=DC31_16280 {ECO:0000313|EMBL:KDA05354.1};
OS Microbacterium sp. CH12i.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1479651 {ECO:0000313|EMBL:KDA05354.1, ECO:0000313|Proteomes:UP000027096};
RN [1] {ECO:0000313|EMBL:KDA05354.1, ECO:0000313|Proteomes:UP000027096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH12i {ECO:0000313|EMBL:KDA05354.1,
RC ECO:0000313|Proteomes:UP000027096};
RA Ferreras E.R., DeMaayer P., Guerrero L.D., Aislabie J.M., Cowan D.A.;
RT "Draft genome sequence of Microbacterium sp. strain CH12i, isolated from
RT shallow groundwater in Cape Hallet, Antarctica.";
RL Submitted (MAR-2014) 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:KDA05354.1}.
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DR EMBL; JHET01000008; KDA05354.1; -; Genomic_DNA.
DR RefSeq; WP_036280094.1; NZ_JHET01000008.1.
DR AlphaFoldDB; A0A062VP99; -.
DR STRING; 1479651.DC31_16280; -.
DR OrthoDB; 241504at2; -.
DR Proteomes; UP000027096; 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; cd08282; PFDH_like; 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:SF3; GLUTATHIONE-INDEPENDENT FORMALDEHYDE DEHYDROGENASE; 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 Reference proteome {ECO:0000313|Proteomes:UP000027096};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 25..140
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 188..288
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 388 AA; 41398 MW; C4759B10FD46AD88 CRC64;
MKAVVYEGPR QVSTKDVPDA KIERPTDVLV RVTTTNICGS DLHMYEGRTS FEVGRTFGHE
NMGEVIEVGS GVEKVRVGDR VVLPFNISCG FCKNCERGLT NYCLTTQPEP SFAGAAYGFA
DMGSYGGGQA ELLRVPFGDH NALRLGEDAE EKENDYVMLS DIFPTGYHAT EMAGVIPGDS
VVIAGAGPVG LMAALSAMIK GAAKVMVVDR HPDRLALAEQ IGAIAIDDSK VDPVQAVLDE
TMGLGADRGC ECVGYQAHDP QGNEDTAATL NMLINSVRFT GGIGTVGVFI PQDPGAKGEL
AKQGKAAIDF GTHWLKGQTM GNGQAPIKRY NRRLRDLIAA GKATPSWIVS HEISLDQAAD
AYKNFDARSK GWTKVLIKPG MSSGKKEN
//
