ID   S2VHY1_9ACTO            Unreviewed;       360 AA.
AC   S2VHY1;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase {ECO:0000313|EMBL:EPD26346.1};
GN   ORFNames=HMPREF9237_01626 {ECO:0000313|EMBL:EPD26346.1};
OS   Actinotignum schaalii FB123-CNA-2.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Actinotignum.
OX   NCBI_TaxID=883067 {ECO:0000313|EMBL:EPD26346.1, ECO:0000313|Proteomes:UP000014393};
RN   [1] {ECO:0000313|EMBL:EPD26346.1, ECO:0000313|Proteomes:UP000014393}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FB123-CNA-2 {ECO:0000313|EMBL:EPD26346.1,
RC   ECO:0000313|Proteomes:UP000014393};
RG   The Broad Institute Genomics Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Saerens B., Vaneechoutte M.,
RA   Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Actinobaculum schaalii FB123-CNA2.";
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
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:EPD26346.1}.
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DR   EMBL; AGWM01000012; EPD26346.1; -; Genomic_DNA.
DR   AlphaFoldDB; S2VHY1; -.
DR   STRING; 59505.FB03_04600; -.
DR   PATRIC; fig|883067.3.peg.1599; -.
DR   eggNOG; COG1207; Bacteria.
DR   HOGENOM; CLU_029499_15_0_11; -.
DR   OrthoDB; 9775031at2; -.
DR   Proteomes; UP000014393; Unassembled WGS sequence.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   CDD; cd02540; GT2_GlmU_N_bac; 1.
DR   Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR   InterPro; IPR025877; MobA-like_NTP_Trfase.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR43584:SF3; BIFUNCTIONAL PROTEIN GLMU; 1.
DR   PANTHER; PTHR43584; NUCLEOTIDYL TRANSFERASE; 1.
DR   Pfam; PF12804; NTP_transf_3; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   4: Predicted;
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014393};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EPD26346.1}.
FT   DOMAIN          6..143
FT                   /note="MobA-like NTP transferase"
FT                   /evidence="ECO:0000259|Pfam:PF12804"
SQ   SEQUENCE   360 AA;  37754 MW;  0F7A4B23E89F5621 CRC64;
     MDLSAVVILA AGQGTRMKSA TPKLLHEVCG RTLLGHAITA ARSLNPQHIV VVVRHERDRV
     AAHALELDDS VIIADQDEIK GTGRAVWCGM EALGASVTGP VLVMAGDTPL LGGEILGELA
     RAHGNGGGGN DAAATASATP ASPAVTVLSA RVPDPAGYGR IVRDGEGTIC AVVEDKDAST
     QQRAINEINT STYIFDAAFL REALAGLGTD NAQGEMYLTD VVARAYQLGA GVGSYVSSDY
     LAAEGANDLV QLAALRREMN RRIGERWMRS GVSIIDPATA WIDVQVELEP DCVVEPHTIL
     RGTTRVARFG HVGPGELANV IVEEGARARH VYLRDCLIPA GKCARHAVAL GEAPQHRCGG
//