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Database: UniProt
Entry: A0A0Q7NIX7_9NOCA
LinkDB: A0A0Q7NIX7_9NOCA
Original site: A0A0Q7NIX7_9NOCA 
ID   A0A0Q7NIX7_9NOCA        Unreviewed;       425 AA.
AC   A0A0Q7NIX7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=4,4'-diaponeurosporenoate glycosyltransferase {ECO:0000256|ARBA:ARBA00040345};
DE            EC=2.4.1.117 {ECO:0000256|ARBA:ARBA00012583};
GN   ORFNames=ASD42_13665 {ECO:0000313|EMBL:KQY39285.1};
OS   Nocardia sp. Root136.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=1736458 {ECO:0000313|EMBL:KQY39285.1, ECO:0000313|Proteomes:UP000051507};
RN   [1] {ECO:0000313|Proteomes:UP000051507}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root136 {ECO:0000313|Proteomes:UP000051507};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQY39285.1, ECO:0000313|Proteomes:UP000051507}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root136 {ECO:0000313|EMBL:KQY39285.1,
RC   ECO:0000313|Proteomes:UP000051507};
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   -!- 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=a dolichyl phosphate + UDP-alpha-D-glucose = a dolichyl beta-
CC         D-glucosyl phosphate + UDP; Xref=Rhea:RHEA:15401, Rhea:RHEA-
CC         COMP:9517, Rhea:RHEA-COMP:9528, ChEBI:CHEBI:57525, ChEBI:CHEBI:57683,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.117;
CC         Evidence={ECO:0000256|ARBA:ARBA00034053};
CC   -!- PATHWAY: Carotenoid biosynthesis; staphyloxanthin biosynthesis;
CC       staphyloxanthin from farnesyl diphosphate: step 4/5.
CC       {ECO:0000256|ARBA:ARBA00037904}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004648}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004648}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
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:KQY39285.1}.
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DR   EMBL; LMFE01000001; KQY39285.1; -; Genomic_DNA.
DR   RefSeq; WP_056814924.1; NZ_LMFE01000001.1.
DR   AlphaFoldDB; A0A0Q7NIX7; -.
DR   STRING; 1736458.ASD42_13665; -.
DR   Proteomes; UP000051507; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:InterPro.
DR   CDD; cd04188; DPG_synthase; 1.
DR   InterPro; IPR035518; DPG_synthase.
DR   InterPro; IPR001173; Glyco_trans_2-like.
DR   InterPro; IPR007267; GtrA_DPMS_TM.
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   Pfam; PF04138; GtrA; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Transferase {ECO:0000256|ARBA:ARBA00022676};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        279..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        306..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        345..366
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        372..392
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          21..187
FT                   /note="Glycosyltransferase 2-like"
FT                   /evidence="ECO:0000259|Pfam:PF00535"
FT   DOMAIN          281..397
FT                   /note="GtrA/DPMS transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF04138"
SQ   SEQUENCE   425 AA;  45686 MW;  68119EFF127DA30C CRC64;
     MTQTEAEQKA MQSSRAPVLD VVIPVYNEEV DLGLCVRRLH SYLRAGFPFT ARITIADNAS
     TDATLAVAEL LAAELDGVQV LHLDAKGRGR ALRTAWEGSD AAVVAYMDVD LSTDLNALLP
     LIAPLVSGHS DLAIGTRLDS SSRVVRGPKR EIISRCYNLL LKTTLRAGFS DAQCGFKAVR
     TEVARELLPL VRDGEWFFDT ELLVLAERAG LRIHEVPVDW IDDPDSRVDI IDTARKDLRG
     IWRLTRALTT GALPVDELRA AVGREPLVAG VPLGMVGQLV RFAIVGVTST LAYIALYLLL
     QPLVGSQGAN LVSLLITAVG NTAANRAFTF GVRGRGNAVS HQFQGLAIFA FGLAITSGSL
     FALHRWAPDA PVAVELTVLI TANLVATLAR FVGLRWVFRH AGVGDATVTP VVGSAERMSA
     LGVRR
//
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