ID L0GV92_9GAMM Unreviewed; 277 AA.
AC L0GV92;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Nicotinate-mononucleotide:5, 6-dimethylbenzimidazole phosphoribosyltransferase CobT {ECO:0000313|EMBL:AGA89219.1};
GN ORFNames=Thimo_0350 {ECO:0000313|EMBL:AGA89219.1};
OS Thioflavicoccus mobilis 8321.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thioflavicoccus.
OX NCBI_TaxID=765912 {ECO:0000313|EMBL:AGA89219.1, ECO:0000313|Proteomes:UP000010816};
RN [1] {ECO:0000313|EMBL:AGA89219.1, ECO:0000313|Proteomes:UP000010816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8321 {ECO:0000313|EMBL:AGA89219.1,
RC ECO:0000313|Proteomes:UP000010816};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K., Liu Z., Imhoff J.,
RA Thiel V., Frigaard N.-U., Bryant D., Woyke T.;
RT "Complete sequence of chromosome of Thioflavicoccus mobilis 8321.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP003051; AGA89219.1; -; Genomic_DNA.
DR RefSeq; WP_015279369.1; NC_019940.1.
DR AlphaFoldDB; L0GV92; -.
DR STRING; 765912.Thimo_0350; -.
DR KEGG; tmb:Thimo_0350; -.
DR eggNOG; COG1873; Bacteria.
DR HOGENOM; CLU_1004496_0_0_6; -.
DR OrthoDB; 286778at2; -.
DR Proteomes; UP000010816; Chromosome.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.30.30.240; PRC-barrel domain; 1.
DR InterPro; IPR027275; PRC-brl_dom.
DR InterPro; IPR011033; PRC_barrel-like_sf.
DR PANTHER; PTHR36505; BLR1072 PROTEIN; 1.
DR PANTHER; PTHR36505:SF1; BLR1072 PROTEIN; 1.
DR Pfam; PF05239; PRC; 1.
DR SUPFAM; SSF50346; PRC-barrel domain; 1.
PE 4: Predicted;
KW Glycosyltransferase {ECO:0000313|EMBL:AGA89219.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010816};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:AGA89219.1}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..277
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003943135"
FT DOMAIN 90..157
FT /note="PRC-barrel"
FT /evidence="ECO:0000259|Pfam:PF05239"
FT REGION 29..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 277 AA; 28948 MW; 5B6272241A48E43E CRC64;
MKAPQAARLS SLVLAMALVS PAIFAVEPAQ QTDASSMQDN AMDTQKTSAD SAMATGTSST
DSEEQPAAAG LTDSYEDKIT DATSEGTRVE QVTGMKVVNG SDEEIGEVSK VVRGKEDGEL
SAVVSVGGFL GIGDKEVVVP LKDLTMKDDK LMAPDDASTE EQLKSMPEYE ESDYEAVWDR
ETVEPGSDST ESGSMDGDEQ TGAMSSGDEK GGAVTDPESA HASSEDNMGA VNQAETADEN
KTAGDEPTED KSATEGENDA SEMEGEDAMQ DQPSESQ
//
