ID A0A099VYU2_9LIST Unreviewed; 457 AA.
AC A0A099VYU2;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Bifunctional protein GlmU {ECO:0000256|HAMAP-Rule:MF_01631};
DE Includes:
DE RecName: Full=UDP-N-acetylglucosamine pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_01631};
DE EC=2.7.7.23 {ECO:0000256|HAMAP-Rule:MF_01631};
DE AltName: Full=N-acetylglucosamine-1-phosphate uridyltransferase {ECO:0000256|HAMAP-Rule:MF_01631};
DE Includes:
DE RecName: Full=Glucosamine-1-phosphate N-acetyltransferase {ECO:0000256|HAMAP-Rule:MF_01631};
DE EC=2.3.1.157 {ECO:0000256|HAMAP-Rule:MF_01631};
GN Name=glmU {ECO:0000256|HAMAP-Rule:MF_01631,
GN ECO:0000313|EMBL:KGL37611.1};
GN ORFNames=EP57_16410 {ECO:0000313|EMBL:KGL37611.1}, HB836_12405
GN {ECO:0000313|EMBL:MBC1402385.1}, HB847_10490
GN {ECO:0000313|EMBL:MBC1372793.1}, HB900_14730
GN {ECO:0000313|EMBL:MBC1575724.1}, HB902_07900
GN {ECO:0000313|EMBL:MBC1561995.1}, HB904_07130
GN {ECO:0000313|EMBL:MBC1615953.1}, HCA72_08540
GN {ECO:0000313|EMBL:MBC2047915.1}, HCA81_12315
GN {ECO:0000313|EMBL:MBC2021838.1}, HCB06_02795
GN {ECO:0000313|EMBL:MBC2115538.1}, HCB08_02530
GN {ECO:0000313|EMBL:MBC2205683.1}, HCB25_12345
GN {ECO:0000313|EMBL:MBC2244862.1}, HCB35_06880
GN {ECO:0000313|EMBL:MBC2240194.1}, HCB69_10745
GN {ECO:0000313|EMBL:MBC2284857.1}, HCB83_08045
GN {ECO:0000313|EMBL:MBC2304804.1}, HCC36_13255
GN {ECO:0000313|EMBL:MBC2294204.1}, HCJ32_09820
GN {ECO:0000313|EMBL:MBC1945261.1}, HCJ43_13130
GN {ECO:0000313|EMBL:MBC1976219.1}, HCJ81_13570
GN {ECO:0000313|EMBL:MBC2311918.1};
OS Listeria booriae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=1552123 {ECO:0000313|EMBL:KGL37611.1, ECO:0000313|Proteomes:UP000029844};
RN [1] {ECO:0000313|EMBL:KGL37611.1, ECO:0000313|Proteomes:UP000029844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL A5-0281 {ECO:0000313|EMBL:KGL37611.1,
RC ECO:0000313|Proteomes:UP000029844};
RA den Bakker H.C.;
RT "Novel Listeriaceae from food processing environments.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000526161, ECO:0000313|Proteomes:UP000529446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL L7-0035 {ECO:0000313|EMBL:MBC2304804.1,
RC ECO:0000313|Proteomes:UP000526161}, FSL L7-0039
RC {ECO:0000313|EMBL:MBC2311918.1, ECO:0000313|Proteomes:UP000565628},
RC FSL L7-0051 {ECO:0000313|EMBL:MBC2294204.1,
RC ECO:0000313|Proteomes:UP000543005}, FSL L7-0054
RC {ECO:0000313|EMBL:MBC2284857.1, ECO:0000313|Proteomes:UP000585696},
RC FSL L7-0149 {ECO:0000313|EMBL:MBC2240194.1,
RC ECO:0000313|Proteomes:UP000553016}, FSL L7-0153
RC {ECO:0000313|EMBL:MBC2244862.1, ECO:0000313|Proteomes:UP000550367},
RC FSL L7-0217 {ECO:0000313|EMBL:MBC2205683.1,
RC ECO:0000313|Proteomes:UP000572892}, FSL L7-0360
RC {ECO:0000313|EMBL:MBC2115538.1, ECO:0000313|Proteomes:UP000529446},
RC FSL L7-0385 {ECO:0000313|EMBL:MBC2021838.1,
RC ECO:0000313|Proteomes:UP000587422}, FSL L7-0514
RC {ECO:0000313|EMBL:MBC2047915.1, ECO:0000313|Proteomes:UP000588249},
RC FSL L7-0520 {ECO:0000313|EMBL:MBC1976219.1,
RC ECO:0000313|Proteomes:UP000587214}, FSL L7-0729
RC {ECO:0000313|EMBL:MBC1945261.1, ECO:0000313|Proteomes:UP000552349},
RC FSL L7-1299 {ECO:0000313|EMBL:MBC1615953.1,
RC ECO:0000313|Proteomes:UP000574104}, FSL L7-1385
RC {ECO:0000313|EMBL:MBC1575724.1, ECO:0000313|Proteomes:UP000571880},
RC FSL L7-1387 {ECO:0000313|EMBL:MBC1561995.1,
RC ECO:0000313|Proteomes:UP000541955}, FSL L7-1658
RC {ECO:0000313|EMBL:MBC1402385.1, ECO:0000313|Proteomes:UP000544413},
RC and FSL L7-1681 {ECO:0000313|EMBL:MBC1372793.1,
RC ECO:0000313|Proteomes:UP000591929};
RA Liao J., Wiedmann M.;
RT "Soil Listeria distribution.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the last two sequential reactions in the de novo
CC biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-
CC terminal domain catalyzes the transfer of acetyl group from acetyl
CC coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-
CC acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into
CC UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-
CC triphosphate), a reaction catalyzed by the N-terminal domain.
CC {ECO:0000256|HAMAP-Rule:MF_01631}.
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, ECO:0000256|HAMAP-
CC Rule:MF_01631};
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, ECO:0000256|HAMAP-
CC Rule:MF_01631};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01631};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01631};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_01631}.
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
CC glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from
CC alpha-D-glucosamine 6-phosphate (route II): step 2/2.
CC {ECO:0000256|HAMAP-Rule:MF_01631}.
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
CC glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-
CC acetyl-alpha-D-glucosamine 1-phosphate: step 1/1. {ECO:0000256|HAMAP-
CC Rule:MF_01631}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_01631}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_01631}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the transferase
CC hexapeptide repeat family. {ECO:0000256|ARBA:ARBA00007707,
CC ECO:0000256|HAMAP-Rule:MF_01631}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the N-
CC acetylglucosamine-1-phosphate uridyltransferase family.
CC {ECO:0000256|ARBA:ARBA00007947, ECO:0000256|HAMAP-Rule:MF_01631}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01631}.
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:KGL37611.1}.
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; JNFA01000031; KGL37611.1; -; Genomic_DNA.
DR EMBL; JAARPL010000007; MBC1372793.1; -; Genomic_DNA.
DR EMBL; JAARPT010000007; MBC1402385.1; -; Genomic_DNA.
DR EMBL; JAARRW010000003; MBC1561995.1; -; Genomic_DNA.
DR EMBL; JAARRX010000008; MBC1575724.1; -; Genomic_DNA.
DR EMBL; JAARSH010000004; MBC1615953.1; -; Genomic_DNA.
DR EMBL; JAASVH010000005; MBC1945261.1; -; Genomic_DNA.
DR EMBL; JAASWF010000009; MBC1976219.1; -; Genomic_DNA.
DR EMBL; JAARWY010000005; MBC2021838.1; -; Genomic_DNA.
DR EMBL; JAARWT010000002; MBC2047915.1; -; Genomic_DNA.
DR EMBL; JAARXI010000001; MBC2115538.1; -; Genomic_DNA.
DR EMBL; JAARYN010000001; MBC2205683.1; -; Genomic_DNA.
DR EMBL; JAARZA010000002; MBC2240194.1; -; Genomic_DNA.
DR EMBL; JAARYY010000007; MBC2244862.1; -; Genomic_DNA.
DR EMBL; JAARZS010000027; MBC2284857.1; -; Genomic_DNA.
DR EMBL; JAARZT010000027; MBC2294204.1; -; Genomic_DNA.
DR EMBL; JAARZW010000007; MBC2304804.1; -; Genomic_DNA.
DR EMBL; JAASWV010000021; MBC2311918.1; -; Genomic_DNA.
DR RefSeq; WP_036088376.1; NZ_UGPF01000001.1.
DR AlphaFoldDB; A0A099VYU2; -.
DR STRING; 1552123.EP57_16410; -.
DR GeneID; 58718914; -.
DR eggNOG; COG1207; Bacteria.
DR OrthoDB; 9775031at2; -.
DR UniPathway; UPA00113; UER00532.
DR UniPathway; UPA00973; -.
DR Proteomes; UP000029844; Unassembled WGS sequence.
DR Proteomes; UP000526161; Unassembled WGS sequence.
DR Proteomes; UP000529446; Unassembled WGS sequence.
DR Proteomes; UP000541955; Unassembled WGS sequence.
DR Proteomes; UP000543005; Unassembled WGS sequence.
DR Proteomes; UP000544413; Unassembled WGS sequence.
DR Proteomes; UP000550367; Unassembled WGS sequence.
DR Proteomes; UP000552349; Unassembled WGS sequence.
DR Proteomes; UP000553016; Unassembled WGS sequence.
DR Proteomes; UP000565628; Unassembled WGS sequence.
DR Proteomes; UP000571880; Unassembled WGS sequence.
DR Proteomes; UP000572892; Unassembled WGS sequence.
DR Proteomes; UP000574104; Unassembled WGS sequence.
DR Proteomes; UP000585696; Unassembled WGS sequence.
DR Proteomes; UP000587214; Unassembled WGS sequence.
DR Proteomes; UP000587422; Unassembled WGS sequence.
DR Proteomes; UP000588249; Unassembled WGS sequence.
DR Proteomes; UP000591929; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019134; F:glucosamine-1-phosphate N-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000902; P:cell morphogenesis; IEA:UniProtKB-UniRule.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR005835; NTP_transferase_dom.
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; PF14602; Hexapep_2; 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, ECO:0000256|HAMAP-
KW Rule:MF_01631};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW Rule:MF_01631};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|HAMAP-Rule:MF_01631};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01631};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01631};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01631};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW Rule:MF_01631};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_01631};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW Rule:MF_01631}; Reference proteome {ECO:0000313|Proteomes:UP000029844};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_01631};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01631}.
FT DOMAIN 6..217
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
FT REGION 1..230
FT /note="Pyrophosphorylase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT REGION 231..251
FT /note="Linker"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT REGION 252..457
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT ACT_SITE 363
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT BINDING 9..12
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT BINDING 23
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT BINDING 73
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT BINDING 78..79
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT BINDING 103
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT BINDING 140
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT BINDING 155
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT BINDING 170
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT BINDING 228
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT BINDING 228
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT BINDING 333
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT BINDING 351
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT BINDING 366
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT BINDING 377
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT BINDING 386..387
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT BINDING 423
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT BINDING 440
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
SQ SEQUENCE 457 AA; 49929 MW; FAD429BE416169FD CRC64;
MMNRYAIVLA AGQGTRMKSK LYKVLHPVCG KPMVEHVVDQ ISQLQPEEIV TIVGHGAEAV
QTHLKDRSTF AVQEEQLGTA HAVLQAKIAL GDKDGLTLVV CGDTPLIQGH TMEALMKYHH
EKRAKATILT TVLDNPTGYG RIIRDDLGIV EKIVEQKDAS EKEQRVNEIN TGTYCFDNLA
LFEALEKVSN ENAQGEYYLP DVIKILKDED EVVAAYRMEN AKESLGVNDR VALAEAQEIM
RHRINEKHMR NGVTLIDPAN TYIDVDVEIG QDTIIGPNVS IHGKTVIGDD CEITGASLLD
NAILGERVKV RHSSIYDSKV GDDVQVGPYS HLRPESEISE GVKIGNFVET KKATIGKNSK
IPHFIYMGDA EIGENVNIGC GSIAVNYDGK NKAKTIIGDD VFIGCNSNLV APVKIGDKAF
VAAGSTITKD VPEGALAISR VKQENKEGYA KRLNFGK
//
