ID A0A418WKR5_9SPHN Unreviewed; 335 AA.
AC A0A418WKR5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:RJF90608.1};
GN ORFNames=D3876_10315 {ECO:0000313|EMBL:RJF90608.1};
OS Sphingomonas cavernae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=2320861 {ECO:0000313|EMBL:RJF90608.1, ECO:0000313|Proteomes:UP000286100};
RN [1] {ECO:0000313|EMBL:RJF90608.1, ECO:0000313|Proteomes:UP000286100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K2R01-6 {ECO:0000313|EMBL:RJF90608.1,
RC ECO:0000313|Proteomes:UP000286100};
RA Zhu H.;
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={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:RJF90608.1}.
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DR EMBL; QYUM01000003; RJF90608.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A418WKR5; -.
DR OrthoDB; 9809185at2; -.
DR Proteomes; UP000286100; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; PTHR43401:SF5; ALCOHOL DEHYDROGENASE-RELATED; 1.
DR PANTHER; PTHR43401; L-THREONINE 3-DEHYDROGENASE; 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:UP000286100};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 25..127
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 169..291
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 335 AA; 34717 MW; AADC3E810C4D9C3F CRC64;
MRAIVYPGAG APLVLERIPD PVPGPGELVI KVHRCGICGT DLHMTEGSGF EFPAGTVPGH
EYAGEVVAVG KEVTGWAEGD RLTALPSTGC GKCAACAQGN LVLCRDAPGV MGGFAEYLKV
PASVAVKLPS VLSLADGALI EPMAVGLYGM RQVPMDACSR VLVLGGGSVA LAAIWWARRL
GAGRIVAASR SPRRAEMALA MGADAFVAFG ENEAAEIREA LGGPPDTVVE CVGTSGFLGK
AVQHVASLGQ VLSMGFCTVP DTLIPAIAAT KGVTMRFPVG YALSDFERVA RDIDSCHADP
KMMISSVVSL DEVPATFDRL RAPNAETKVH ITFDS
//