ID A0A0G0WMQ2_9BACT Unreviewed; 417 AA.
AC A0A0G0WMQ2;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Bifunctional protein GlmU {ECO:0000313|EMBL:KKR76627.1};
GN ORFNames=UU21_C0006G0018 {ECO:0000313|EMBL:KKR76627.1};
OS Candidatus Levybacteria bacterium GW2011_GWA2_40_8.
OC Bacteria; Candidatus Levybacteria.
OX NCBI_TaxID=1618459 {ECO:0000313|EMBL:KKR76627.1, ECO:0000313|Proteomes:UP000034541};
RN [1] {ECO:0000313|EMBL:KKR76627.1, ECO:0000313|Proteomes:UP000034541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP =
CC diphosphate + UDP-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13509,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398,
CC ChEBI:CHEBI:57705, ChEBI:CHEBI:57776; EC=2.7.7.23;
CC Evidence={ECO:0000256|ARBA:ARBA00001851};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-
CC acetyl-alpha-D-glucosamine 1-phosphate; Xref=Rhea:RHEA:13725,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57776, ChEBI:CHEBI:58516; EC=2.3.1.157;
CC Evidence={ECO:0000256|ARBA:ARBA00000731};
CC -!- SIMILARITY: In the C-terminal section; belongs to the transferase
CC hexapeptide repeat family. {ECO:0000256|ARBA:ARBA00007707}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the N-
CC acetylglucosamine-1-phosphate uridyltransferase family.
CC {ECO:0000256|ARBA:ARBA00007947}.
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:KKR76627.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LBZT01000006; KKR76627.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0WMQ2; -.
DR Proteomes; UP000034541; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR018357; Hexapep_transf_CS.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR PANTHER; PTHR43584:SF3; BIFUNCTIONAL PROTEIN GLMU; 1.
DR PANTHER; PTHR43584; NUCLEOTIDYL TRANSFERASE; 1.
DR Pfam; PF00132; Hexapep; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 3..211
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 417 AA; 45750 MW; E1966D5DFBFFB37A CRC64;
MQVVLLAAGQ SSRFYPFNKE HKSLISVMGK SIIVHTIESI NKKSGIEKFL IVTDPKNEAR
QILGDGSDLG VKVEYVILEK PTGMGDALLA AEKKIFDNFF LVHSYHVDFP EIVENFDLEN
PSDSTLFIKK EKDITGFGIV TLDGKSVTSV VEKPENSSSL SDNKIVGIYF LKKDFIPTLK
KIKPEHYSFE KALDEYAKQG KLKAEVIKSD TVTLKYPWDL LGLKNYLLSH AKKSISLKAS
ISDSAKLEGL IIVEDGAVIS DNSIIKGPCF IGKNVFVGTN SLVRDGSCLE ENVKVGAFME
IKNSLVMEGT TFHSGYLGDS LIGKDCKIGS QFNTANVRLD RGNVRVLVND KKIDTGMKYL
GGIVGNDVLV GGNVSVMPGV IVGDNVNIGP STTVMKNIPP NTVFYTKFKE HVEKSRK
//
