GLMU_STRMK
ID GLMU_STRMK Reviewed; 455 AA.
AC B2FHY5;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Bifunctional protein GlmU {ECO:0000255|HAMAP-Rule:MF_01631};
DE Includes:
DE RecName: Full=UDP-N-acetylglucosamine pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_01631};
DE EC=2.7.7.23 {ECO:0000255|HAMAP-Rule:MF_01631};
DE AltName: Full=N-acetylglucosamine-1-phosphate uridyltransferase {ECO:0000255|HAMAP-Rule:MF_01631};
DE Includes:
DE RecName: Full=Glucosamine-1-phosphate N-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01631};
DE EC=2.3.1.157 {ECO:0000255|HAMAP-Rule:MF_01631};
GN Name=glmU {ECO:0000255|HAMAP-Rule:MF_01631}; OrderedLocusNames=Smlt4108;
OS Stenotrophomonas maltophilia (strain K279a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=522373;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K279a;
RX PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E.,
RA Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S.,
RA Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D.,
RA Parkhill J., Thomson N.R., Avison M.B.;
RT "The complete genome, comparative and functional analysis of
RT Stenotrophomonas maltophilia reveals an organism heavily shielded by drug
RT resistance determinants.";
RL Genome Biol. 9:R74.1-R74.13(2008).
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:0000255|HAMAP-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:0000255|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:0000255|HAMAP-Rule:MF_01631};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01631};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|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:0000255|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:0000255|HAMAP-
CC Rule:MF_01631}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01631}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_01631}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01631}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the N-
CC acetylglucosamine-1-phosphate uridyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_01631}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the transferase
CC hexapeptide repeat family. {ECO:0000255|HAMAP-Rule:MF_01631}.
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DR EMBL; AM743169; CAQ47499.1; -; Genomic_DNA.
DR RefSeq; WP_012481318.1; NC_010943.1.
DR PDB; 7K47; X-ray; 2.90 A; A=1-455.
DR PDBsum; 7K47; -.
DR AlphaFoldDB; B2FHY5; -.
DR SMR; B2FHY5; -.
DR STRING; 522373.Smlt4108; -.
DR EnsemblBacteria; CAQ47499; CAQ47499; Smlt4108.
DR KEGG; sml:Smlt4108; -.
DR PATRIC; fig|522373.3.peg.3879; -.
DR eggNOG; COG1207; Bacteria.
DR HOGENOM; CLU_029499_15_2_6; -.
DR OMA; TAIVEHK; -.
DR OrthoDB; 1381953at2; -.
DR UniPathway; UPA00113; UER00532.
DR UniPathway; UPA00113; UER00533.
DR UniPathway; UPA00973; -.
DR Proteomes; UP000008840; Chromosome.
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; cd03353; LbH_GlmU_C; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR HAMAP; MF_01631; GlmU; 1.
DR InterPro; IPR005882; Bifunctional_GlmU.
DR InterPro; IPR038009; GlmU_C_LbH.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR025877; MobA-like_NTP_Trfase.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR Pfam; PF00132; Hexapep; 2.
DR Pfam; PF14602; Hexapep_2; 1.
DR Pfam; PF12804; NTP_transf_3; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR TIGRFAMs; TIGR01173; glmU; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cell shape;
KW Cell wall biogenesis/degradation; Cytoplasm; Magnesium; Metal-binding;
KW Multifunctional enzyme; Nucleotidyltransferase; Peptidoglycan synthesis;
KW Reference proteome; Repeat; Transferase.
FT CHAIN 1..455
FT /note="Bifunctional protein GlmU"
FT /id="PRO_1000186495"
FT REGION 1..228
FT /note="Pyrophosphorylase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT REGION 229..249
FT /note="Linker"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT REGION 250..455
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT ACT_SITE 362
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 10..13
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 24
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 76
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 81..82
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 103..105
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 105
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 138
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 153
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 168
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 226
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 226
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 332
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 350
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 365
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 376
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 379
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 385..386
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 404
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 422
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 439
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT STRAND 5..11
FT /evidence="ECO:0007829|PDB:7K47"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:7K47"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:7K47"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:7K47"
FT STRAND 27..33
FT /evidence="ECO:0007829|PDB:7K47"
FT HELIX 34..43
FT /evidence="ECO:0007829|PDB:7K47"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:7K47"
FT HELIX 58..64
FT /evidence="ECO:0007829|PDB:7K47"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:7K47"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:7K47"
FT HELIX 82..89
FT /evidence="ECO:0007829|PDB:7K47"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:7K47"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:7K47"
FT HELIX 111..118
FT /evidence="ECO:0007829|PDB:7K47"
FT STRAND 122..130
FT /evidence="ECO:0007829|PDB:7K47"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:7K47"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:7K47"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:7K47"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:7K47"
FT STRAND 166..175
FT /evidence="ECO:0007829|PDB:7K47"
FT HELIX 176..185
FT /evidence="ECO:0007829|PDB:7K47"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:7K47"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:7K47"
FT HELIX 200..206
FT /evidence="ECO:0007829|PDB:7K47"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:7K47"
FT HELIX 219..222
FT /evidence="ECO:0007829|PDB:7K47"
FT HELIX 228..248
FT /evidence="ECO:0007829|PDB:7K47"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:7K47"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:7K47"
FT STRAND 259..267
FT /evidence="ECO:0007829|PDB:7K47"
FT STRAND 275..285
FT /evidence="ECO:0007829|PDB:7K47"
FT STRAND 293..302
FT /evidence="ECO:0007829|PDB:7K47"
FT STRAND 310..321
FT /evidence="ECO:0007829|PDB:7K47"
FT STRAND 327..331
FT /evidence="ECO:0007829|PDB:7K47"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:7K47"
FT STRAND 342..354
FT /evidence="ECO:0007829|PDB:7K47"
FT STRAND 359..371
FT /evidence="ECO:0007829|PDB:7K47"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:7K47"
FT STRAND 386..389
FT /evidence="ECO:0007829|PDB:7K47"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:7K47"
FT STRAND 407..414
FT /evidence="ECO:0007829|PDB:7K47"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:7K47"
SQ SEQUENCE 455 AA; 48117 MW; 1C072834506AF0C5 CRC64;
MTQPLHVIIL AAGAGKRMKS VLPKVLQPIA GQPMLAHVID AARELQPAAI HVVHGHGGEA
VRQYFAGQPD LQWAEQAQQL GTGHAVAQAM PQVPDLAQVL VLYGDVPLIR AQTLRDLLAQ
PGRLAVLVAD VDDPTGYGRV LRDAEGKVGA IIEQKDATDD QLRVRTINTG IIAAESTALR
RWLSQLSNSN AQGEYYLTDV FAFAAHEYTP AEMALVADAQ EAEGANDPWQ LSQLERAWQR
RAVRALCAQG ARVRDPARLD IRGTVTVGSD VLIDVDVVLE GKVVLGDGVT VGPFNRLKDV
NLGPGTDVRA HCDLEGVVTE GAAQIGPFAR LRPGTVLADG VHVGNFVETK KVTLGVGSKA
NHLTYLGDAV IGSKVNIGAG TITCNYDGVN KSTTTIGDNA FIGSNSSLVA PVTIGDGATI
AAGSVITRNA PDGKLTLARA RQETIDGWKR PLKKS
