ID A0A108CEU9_9BURK Unreviewed; 457 AA.
AC A0A108CEU9;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=MobA-like NTP transferase domain-containing protein {ECO:0000259|Pfam:PF12804};
DE Flags: Fragment;
GN ORFNames=WM16_16375 {ECO:0000313|EMBL:KWK73388.1};
OS Burkholderia ubonensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=101571 {ECO:0000313|EMBL:KWK73388.1, ECO:0000313|Proteomes:UP000065504};
RN [1] {ECO:0000313|EMBL:KWK73388.1, ECO:0000313|Proteomes:UP000065504}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSMB782WGS {ECO:0000313|EMBL:KWK73388.1,
RC ECO:0000313|Proteomes:UP000065504};
RA Sahl J., Keim P., Wagner D.;
RT "Expanding the genomic diversity of Burkholderia species for the
RT development of highly accurate diagnostics.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:KWK73388.1}.
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DR EMBL; LPLU01000092; KWK73388.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A108CEU9; -.
DR Proteomes; UP000065504; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019134; F:glucosamine-1-phosphate N-acetyltransferase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IEA:InterPro.
DR GO; GO:0000902; P:cell morphogenesis; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:InterPro.
DR CDD; cd02540; GT2_GlmU_N_bac; 1.
DR CDD; cd03353; LbH_GlmU_C; 1.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR HAMAP; MF_01631; GlmU; 1.
DR InterPro; IPR005882; Bifunctional_GlmU.
DR InterPro; IPR038009; GlmU_C_LbH.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR018357; Hexapep_transf_CS.
DR InterPro; IPR025877; MobA-like_NTP_Trfase.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR NCBIfam; TIGR01173; glmU; 1.
DR PANTHER; PTHR43584:SF3; BIFUNCTIONAL PROTEIN GLMU; 1.
DR PANTHER; PTHR43584; NUCLEOTIDYL TRANSFERASE; 1.
DR Pfam; PF00132; Hexapep; 2.
DR Pfam; PF12804; NTP_transf_3; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 2.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 8..134
FT /note="MobA-like NTP transferase"
FT /evidence="ECO:0000259|Pfam:PF12804"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KWK73388.1"
SQ SEQUENCE 457 AA; 48158 MW; 2BAD78B73A9A0FBE CRC64;
QAGAMNIVIL AAGTGKRMRS ALPKVLHPLA GRPLLSHVIA TARALQPSRL VVVVGHGAEQ
VQAAVAAPDV QFAVQAEQLG TGHAVRQALP LLDPAQPTLV LYGDVPLTRV STLERLVAAA
REGRYGILTV TLDDPTGYGR IVRDPAGFVT RIVEQKDASP EEQKIAEINT GIVVTPTAQL
AMWLGALNND NAQGEYYLTD VVELAIDAGF EVVTAQPDAE WETLGVNSKA QLAELERVHQ
RNLADALLVD GVTLADPARL DVRGTLRCGR DVSIDVNCVF EGNVTLADDV TIGANCVIRN
ASIGAGARID AFTHIDGAEL GAHTVIGPYA RLRPGAQLAD EAHVGNFVEV KNAVIGHGSK
ANHLTYIGDA DIGARVNIGA GTITCNYDGA NKFRTVIEDD VFVGSDTQLV APVRVGRGVT
IAAGTTIWKD VAEGMLALND KTQTAKSGYV RPVKKKG
//
