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Database: UniProt
Entry: K1ZVJ0_9BACT
LinkDB: K1ZVJ0_9BACT
Original site: K1ZVJ0_9BACT 
ID   K1ZVJ0_9BACT            Unreviewed;       253 AA.
AC   K1ZVJ0;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=4,4'-diaponeurosporenoate glycosyltransferase {ECO:0000256|ARBA:ARBA00040345};
GN   ORFNames=ACD_61C00142G0002 {ECO:0000313|EMBL:EKD53141.1};
OS   uncultured bacterium.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD53141.1};
RN   [1] {ECO:0000313|EMBL:EKD53141.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23019650; DOI=10.1126/science.1224041;
RA   Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA   VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA   Long P.E., Banfield J.F.;
RT   "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT   bacterial phyla.";
RL   Science 337:1661-1665(2012).
CC   -!- FUNCTION: Catalyzes the glycosylation of 4,4'-diaponeurosporenoate,
CC       i.e. the esterification of glucose at the C1'' position with the
CC       carboxyl group of 4,4'-diaponeurosporenic acid, to form glycosyl-4,4'-
CC       diaponeurosporenoate. This is a step in the biosynthesis of
CC       staphyloxanthin, an orange pigment present in most staphylococci
CC       strains. {ECO:0000256|ARBA:ARBA00037281}.
CC   -!- PATHWAY: Carotenoid biosynthesis; staphyloxanthin biosynthesis;
CC       staphyloxanthin from farnesyl diphosphate: step 4/5.
CC       {ECO:0000256|ARBA:ARBA00037904}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. CrtQ
CC       subfamily. {ECO:0000256|ARBA:ARBA00038120}.
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:EKD53141.1}.
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DR   EMBL; AMFJ01025634; EKD53141.1; -; Genomic_DNA.
DR   AlphaFoldDB; K1ZVJ0; -.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR001173; Glyco_trans_2-like.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR10859:SF91; DOLICHYL-PHOSPHATE BETA-GLUCOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR10859; GLYCOSYL TRANSFERASE; 1.
DR   Pfam; PF00535; Glycos_transf_2; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   3: Inferred from homology;
KW   Transferase {ECO:0000313|EMBL:EKD53141.1}.
FT   DOMAIN          6..171
FT                   /note="Glycosyltransferase 2-like"
FT                   /evidence="ECO:0000259|Pfam:PF00535"
SQ   SEQUENCE   253 AA;  28865 MW;  25BCD768063D279D CRC64;
     MKPKLSIVLS NYNEHANLER GVLEQMSVYL KKAKYSWEVI INDDGSTDGG DIIIADYVKI
     HPGFKMVRGK HGGKAAGIWN GIQEAEGEIV LFTDMDQSTP LQEVEKLLPW FEKNYDVVFG
     SRGKMRDNFS FFRQISSWAF RSFRGLLLLH DVVDTQCGFK ALRADVAKKI FPMLSVIKDK
     KVVSKGWTVS AFDVELLFLA EKLGYRLKEV DVIWKNEDTS VSKQKSFIGE SIDMLKQIIQ
     VKVNDLQGKY DQK
//
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