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Database: UniProt
Entry: A0A0J7XRT3_9SPHN
LinkDB: A0A0J7XRT3_9SPHN
Original site: A0A0J7XRT3_9SPHN 
ID   A0A0J7XRT3_9SPHN        Unreviewed;       360 AA.
AC   A0A0J7XRT3;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=5-exo-alcohol dehydrogenase {ECO:0000313|EMBL:KMS53773.1};
GN   ORFNames=V473_16275 {ECO:0000313|EMBL:KMS53773.1};
OS   Sphingobium cupriresistens LL01.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=1420583 {ECO:0000313|EMBL:KMS53773.1, ECO:0000313|Proteomes:UP000052232};
RN   [1] {ECO:0000313|EMBL:KMS53773.1, ECO:0000313|Proteomes:UP000052232}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LL01 {ECO:0000313|EMBL:KMS53773.1,
RC   ECO:0000313|Proteomes:UP000052232};
RX   PubMed=25850427; DOI=10.1534/g3.114.015933;
RA   Pearce S.L., Oakeshott J.G., Pandey G.;
RT   "Insights into Ongoing Evolution of the Hexachlorocyclohexane Catabolic
RT   Pathway from Comparative Genomics of Ten Sphingomonadaceae Strains.";
RL   G3 (Bethesda) 5:1081-1094(2015).
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:KMS53773.1}.
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DR   EMBL; JACT01000004; KMS53773.1; -; Genomic_DNA.
DR   RefSeq; WP_066606397.1; NZ_KQ130435.1.
DR   AlphaFoldDB; A0A0J7XRT3; -.
DR   STRING; 1420583.V473_16275; -.
DR   PATRIC; fig|1420583.3.peg.3057; -.
DR   Proteomes; UP000052232; 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; cd08231; MDR_TM0436_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; PTHR43401:SF1; ALCOHOL DEHYDROGENASE, ZINC-CONTAINING; 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:UP000052232};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          27..137
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          185..317
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   360 AA;  37823 MW;  0BCD15B961520A7F CRC64;
     MHGKAAVLVE KNRLETWDVE VHAPEPGGAL VRTILGGVCG SDVHILTGEA GEMPFPIILG
     HEGVGEITQL GAGVSTDYAG TPVKAGDLVI WSPIALCHRC YSCTVLEQTP CENSQYFEDA
     AKPNWGSYAD YAWLPNNMPF YRLPDGAQPE AIAALGCALP TVLRGFDRCG PVRFGDSVVV
     QGAGPVGLSA ILVAAQAGAR EIIVIDGAQA RLDAAMTLGA TSTVSLSLSP DERKRMIYDR
     IGKQGPDIVI EAAGALPAFP EGVDISGIHS RYIILGLWGA IGTQPISPRD LTLKNLTIGG
     ASFPAPKNYY QGMQFAARVQ NQVPLAALVS HRFGISQAAE ALTVTKNGVA TKAVIDPTIS
//
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