ID A0A0T0Q070_9SPHN Unreviewed; 392 AA.
AC A0A0T0Q070;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:KQT35340.1};
GN ORFNames=ASG29_04390 {ECO:0000313|EMBL:KQT35340.1};
OS Sphingomonas sp. Leaf412.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736370 {ECO:0000313|EMBL:KQT35340.1, ECO:0000313|Proteomes:UP000051178};
RN [1] {ECO:0000313|EMBL:KQT35340.1, ECO:0000313|Proteomes:UP000051178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf412 {ECO:0000313|EMBL:KQT35340.1,
RC ECO:0000313|Proteomes:UP000051178};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQT35340.1, ECO:0000313|Proteomes:UP000051178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf412 {ECO:0000313|EMBL:KQT35340.1,
RC ECO:0000313|Proteomes:UP000051178};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQT35340.1}.
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DR EMBL; LMQP01000001; KQT35340.1; -; Genomic_DNA.
DR RefSeq; WP_055980551.1; NZ_LMQP01000001.1.
DR AlphaFoldDB; A0A0T0Q070; -.
DR STRING; 1736370.ASG29_04390; -.
DR OrthoDB; 9773078at2; -.
DR Proteomes; UP000051178; 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 Reference proteome {ECO:0000313|Proteomes:UP000051178};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 26..150
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 197..265
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 392 AA; 42445 MW; 1664E08866879070 CRC64;
MRALAWHGKH DVRVDTVDDP EIVNPRDCII KVTSTAICGS DLHLYDGYIP TMQAGDILGH
EFMGEVVETG PKSTLKKGQR VVVPFTIACG SCYHCGKHQY SACDNGNPAD NQDLGMELYG
QPMSGLFGYS HLTGGYAGGQ AEYVRVPFSD VGPIVIPDGV SDEKVLFLSD ILPTGWQAAE
NAQIEPGDTV AVWGCGPVGL FAVQSAFLMG AERVIAIDHF PKRLALAKRF GAETINFEES
AVYEALMEMT GGIGPDAVID SVGLEAHGLF VDNVVDQIKA STFLGTDRAH AIRQAIIACR
KGGRVSMPAV YGGFIDKFPL GAFMEKGLTL KTGQTHVQHY MPALLNAIME GKIDTEFLIS
HRMDLEEAPK GYKMFKDDQN EVTKVVLKPG FN
//
