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Database: UniProt
Entry: X6L3L8_9RHOB
LinkDB: X6L3L8_9RHOB
Original site: X6L3L8_9RHOB 
ID   X6L3L8_9RHOB            Unreviewed;       641 AA.
AC   X6L3L8;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=N-acetylglucosamine transferase {ECO:0000313|EMBL:ETA53180.1};
GN   ORFNames=P279_04720 {ECO:0000313|EMBL:ETA53180.1};
OS   Rhodobacteraceae bacterium PD-2.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=1169855 {ECO:0000313|EMBL:ETA53180.1, ECO:0000313|Proteomes:UP000023196};
RN   [1] {ECO:0000313|EMBL:ETA53180.1, ECO:0000313|Proteomes:UP000023196}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PD-2 {ECO:0000313|EMBL:ETA53180.1,
RC   ECO:0000313|Proteomes:UP000023196};
RX   PubMed=25700405;
RA   Zheng L., Cui Z., Xu L., Sun C., Powell R.J., Hill R.T.;
RT   "Draft Genome Sequence of Rhodobacteraceae Strain PD-2, an Algicidal
RT   Bacterium with a Quorum-Sensing System, Isolated from the Marine Microalga
RT   Prorocentrum donghaiense.";
RL   Genome Announc. Announc.3:e01549-14(2015).
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
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:ETA53180.1}.
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DR   EMBL; AWRV02000024; ETA53180.1; -; Genomic_DNA.
DR   AlphaFoldDB; X6L3L8; -.
DR   PATRIC; fig|1169855.3.peg.829; -.
DR   HOGENOM; CLU_001570_17_4_5; -.
DR   Proteomes; UP000023196; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   CDD; cd06201; SiR_like2; 1.
DR   Gene3D; 3.40.50.360; -; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR005625; PepSY-ass_TM.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR19384:SF17; NADPH--CYTOCHROME P450 REDUCTASE; 1.
DR   PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   Pfam; PF03929; PepSY_TM; 1.
DR   PRINTS; PR00371; FPNCR.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF52218; Flavoproteins; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   4: Predicted;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000023196};
KW   Transferase {ECO:0000313|EMBL:ETA53180.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        28..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        196..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          239..375
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   DOMAIN          391..504
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   641 AA;  67562 MW;  66D2E1BAF160301A CRC64;
     MASADPNQAE RWLTNLHRSL FLGDGGRIAM AAGAAAMLVL SLSGAALVAR RAGGWRHWFA
     RLRGPLAGRL HVEIARIAVA GLVLSSTTAL WMTASTFDLL PDGGAMPATP AEVSGEIGFA
     PGRMPTLRQT PVAALRELSF PYPGDPTDVF TLKTDRGTGY LDQGDGTLLA WADLTGWARL
     SETIYMLHTG QGAATLGLVL GLMALGVPAM GATGVLVWLA GRRGRPRIRG NQPAGRAETI
     LLVGSEGGST WGFAATLHAA LTQAGQSVHV GPMSGFGPER YTNARRIILL AATYGDGAAP
     ASAKGFLDRL TASDPAAEIP LAVLGFGDRS FPAYCAFARD VATAAQTKGW PELMPLDTID
     RQSPQDFARW GRTLGDVLGI DLELAHQPVQ PQATTLTLVS RRDYGAEVQA PTAILRFALP
     RASLWQRLRG GGFARFQAGD LIGVLPEGSA VPRLYSLASG HRDGFVEIVV KKHPGGLCSG
     QLTALEPGDT VAAFLRRNPG FRAGRGKAPL ILIGAGTGIG PLAGFIRGNA RRRPVHLFFG
     MRHPDSDFFY GEDIAGWQDE GRLTGLVTAV SRGARPHYVQ DALRGEAAQV ADLIRNGARV
     MVCGGRDMAA GVADALAEIL APTGLTPAVL KAEGRYVEDV Y
//
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