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Database: UniProt
Entry: A0A0F5PC81_9SPHN
LinkDB: A0A0F5PC81_9SPHN
Original site: A0A0F5PC81_9SPHN 
ID   A0A0F5PC81_9SPHN        Unreviewed;       286 AA.
AC   A0A0F5PC81;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KKC26102.1};
GN   ORFNames=WP12_10900 {ECO:0000313|EMBL:KKC26102.1};
OS   Sphingomonas sp. SRS2.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=133190 {ECO:0000313|EMBL:KKC26102.1, ECO:0000313|Proteomes:UP000033680};
RN   [1] {ECO:0000313|EMBL:KKC26102.1, ECO:0000313|Proteomes:UP000033680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRS2 {ECO:0000313|EMBL:KKC26102.1,
RC   ECO:0000313|Proteomes:UP000033680};
RA   Nielsen T.K., Sorensen S.R., Hansen L.H.;
RT   "Draft genome sequence of isoproturon-mineralizing Sphingomonas sp. SRS2,
RT   isolated from an agricultural field in the United Kingdom.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00008072}.
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:KKC26102.1}.
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DR   EMBL; LARW01000084; KKC26102.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F5PC81; -.
DR   STRING; 133190.WP12_10900; -.
DR   PATRIC; fig|133190.4.peg.4062; -.
DR   Proteomes; UP000033680; 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; 2.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR031640; Glu_dehyd_C.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43161:SF23; (R,R)-BUTANEDIOL DEHYDROGENASE-RELATED; 1.
DR   PANTHER; PTHR43161; SORBITOL DEHYDROGENASE; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF16912; Glu_dehyd_C; 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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033680};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          2..33
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          73..263
FT                   /note="Glucose dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16912"
SQ   SEQUENCE   286 AA;  30039 MW;  A36196B3780A813B CRC64;
     MPGHEFAGIV TEAGADVVGF TRGDYVTADP MVHRFGLGDA PGAFTRFLRI TGPELGRTAF
     KLPVDLPPKL VSLVEPIAVG LHGVAVAKAQ PDDRALVLGA GTIGLCVAIA LRAQGVFDIT
     VRDPSPLRRA AAEAVGATAM DTAQPLPRSA DQADKPTLIF DCAGVGSALL EAQDAIADGG
     RTVILASYAQ PVLLDLHELM LRESAVLGAV GYGGQFPAAI AMVVDKRAVM ERLISHYFAL
     EQIREAFSVQ GDPLQSLKVI VEIGDRYGER PAIESADRPQ PLDTAV
//
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