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Database: UniProt
Entry: L7F8R2_9ACTN
LinkDB: L7F8R2_9ACTN
Original site: L7F8R2_9ACTN 
ID   L7F8R2_9ACTN            Unreviewed;       354 AA.
AC   L7F8R2;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Putative chlorophyll synthesis pathway protein BchC {ECO:0000313|EMBL:ELP68003.1};
GN   ORFNames=STRTUCAR8_07643 {ECO:0000313|EMBL:ELP68003.1};
OS   Streptomyces turgidiscabies Car8.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=698760 {ECO:0000313|EMBL:ELP68003.1, ECO:0000313|Proteomes:UP000010931};
RN   [1] {ECO:0000313|EMBL:ELP68003.1, ECO:0000313|Proteomes:UP000010931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Car8 {ECO:0000313|EMBL:ELP68003.1,
RC   ECO:0000313|Proteomes:UP000010931};
RX   PubMed=21087627; DOI=10.1016/j.plasmid.2010.11.002;
RA   Huguet-Tapia J.C., Badger J.H., Loria R., Pettis G.S.;
RT   "Streptomyces turgidiscabies Car8 contains a modular pathogenicity island
RT   that shares virulence genes with other actinobacterial plant pathogens.";
RL   Plasmid 65:118-124(2011).
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:ELP68003.1}.
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DR   EMBL; AEJB01000244; ELP68003.1; -; Genomic_DNA.
DR   AlphaFoldDB; L7F8R2; -.
DR   STRING; 85558.T45_08757; -.
DR   PATRIC; fig|698760.3.peg.3258; -.
DR   Proteomes; UP000010931; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd08232; idonate-5-DH; 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; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43161; SORBITOL DEHYDROGENASE; 1.
DR   PANTHER; PTHR43161:SF9; SORBITOL 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.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010931};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          29..143
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          184..308
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   354 AA;  36365 MW;  443E1658A19946ED CRC64;
     MNSSTMRAVV AHGAGDLRLE ERPVPEPGPG EVAVDIRYGG ICGSDLHYWR HGAVGEFRIR
     EPLVLGHEIV GRVRAAGPGT QAPPPGTPVA VHPLTSCGTC RQCLAGRRNT CLDTGYLGSA
     ARNPHVQGGF AEVLVVPAER VLPLPEGLDM RLAAVAEPAA VAWHAVRQAG DVRGKRVLVT
     GAGPIGCLVV AALRAAGAGE ITVTDVHEAP LAVAKQVGAT STVRVGGPAA ERDELEGLAA
     DIAIESSGNP AGLRTCVYGV DRGGLVVGLG LLPPGDTPVA ANAVITRELR LVGSFRFDTE
     LGEVLRALAD GRLPADPVVT SVLPVARTGA AFELAADPAR SCKVLLDFAD PTTP
//
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