GLMU_STRR6
ID GLMU_STRR6 Reviewed; 459 AA.
AC Q8DQ18;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 125.
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=spr0891;
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=22297115; DOI=10.1016/j.bmcl.2012.01.016;
RA Green O.M., McKenzie A.R., Shapiro A.B., Otterbein L., Ni H., Patten A.,
RA Stokes S., Albert R., Kawatkar S., Breed J.;
RT "Inhibitors of acetyltransferase domain of N-acetylglucosamine-1-phosphate-
RT uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU). Part 1:
RT Hit to lead evaluation of a novel arylsulfonamide series.";
RL Bioorg. Med. Chem. Lett. 22:1510-1519(2012).
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:0000250, ECO:0000255|HAMAP-Rule:MF_01631};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250, ECO:0000255|HAMAP-
CC 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:0000250, ECO:0000255|HAMAP-Rule:MF_01631}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250, ECO:0000255|HAMAP-
CC 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, ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the transferase
CC hexapeptide repeat family. {ECO:0000255|HAMAP-Rule:MF_01631,
CC ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK99695.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE007317; AAK99695.1; ALT_INIT; Genomic_DNA.
DR PIR; C97983; C97983.
DR RefSeq; NP_358485.1; NC_003098.1.
DR RefSeq; WP_000064394.1; NC_003098.1.
DR PDB; 4AAW; X-ray; 2.20 A; A=1-459.
DR PDB; 4AC3; X-ray; 2.10 A; A=1-459.
DR PDBsum; 4AAW; -.
DR PDBsum; 4AC3; -.
DR AlphaFoldDB; Q8DQ18; -.
DR SMR; Q8DQ18; -.
DR STRING; 171101.spr0891; -.
DR BindingDB; Q8DQ18; -.
DR EnsemblBacteria; AAK99695; AAK99695; spr0891.
DR GeneID; 60234081; -.
DR KEGG; spr:spr0891; -.
DR PATRIC; fig|171101.6.peg.978; -.
DR eggNOG; COG1207; Bacteria.
DR HOGENOM; CLU_029499_15_2_9; -.
DR UniPathway; UPA00113; UER00532.
DR UniPathway; UPA00113; UER00533.
DR UniPathway; UPA00973; -.
DR PRO; PR:Q8DQ18; -.
DR Proteomes; UP000000586; 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; IPR018357; Hexapep_transf_CS.
DR InterPro; IPR005835; NTP_transferase_dom.
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; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR TIGRFAMs; TIGR01173; glmU; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 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..459
FT /note="Bifunctional protein GlmU"
FT /id="PRO_0000233851"
FT REGION 1..229
FT /note="Pyrophosphorylase"
FT /evidence="ECO:0000250, ECO:0000255|HAMAP-Rule:MF_01631"
FT REGION 230..250
FT /note="Linker"
FT /evidence="ECO:0000250, ECO:0000255|HAMAP-Rule:MF_01631"
FT REGION 251..459
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000250, ECO:0000255|HAMAP-Rule:MF_01631"
FT ACT_SITE 362
FT /note="Proton acceptor"
FT /evidence="ECO:0000250, ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 8..11
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250, ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 22
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250, ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 72
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250, ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 77..78
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250, ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 102
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250, ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 139
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250, ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 154
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250, ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 169
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250, ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 227
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250, ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 227
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250, 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:0000250, ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 422
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250, ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 439
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250, ECO:0000255|HAMAP-Rule:MF_01631"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:4AC3"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:4AC3"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:4AC3"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:4AC3"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:4AC3"
FT HELIX 32..41
FT /evidence="ECO:0007829|PDB:4AC3"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:4AC3"
FT HELIX 56..62
FT /evidence="ECO:0007829|PDB:4AC3"
FT TURN 63..66
FT /evidence="ECO:0007829|PDB:4AC3"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:4AC3"
FT HELIX 78..83
FT /evidence="ECO:0007829|PDB:4AC3"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:4AC3"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:4AC3"
FT HELIX 108..120
FT /evidence="ECO:0007829|PDB:4AC3"
FT STRAND 124..131
FT /evidence="ECO:0007829|PDB:4AC3"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:4AC3"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:4AC3"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:4AC3"
FT HELIX 160..163
FT /evidence="ECO:0007829|PDB:4AC3"
FT STRAND 167..176
FT /evidence="ECO:0007829|PDB:4AC3"
FT HELIX 177..189
FT /evidence="ECO:0007829|PDB:4AC3"
FT HELIX 198..207
FT /evidence="ECO:0007829|PDB:4AC3"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:4AC3"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:4AC3"
FT HELIX 229..249
FT /evidence="ECO:0007829|PDB:4AC3"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:4AC3"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:4AAW"
FT STRAND 279..283
FT /evidence="ECO:0007829|PDB:4AC3"
FT STRAND 297..300
FT /evidence="ECO:0007829|PDB:4AC3"
FT STRAND 313..316
FT /evidence="ECO:0007829|PDB:4AC3"
FT STRAND 342..351
FT /evidence="ECO:0007829|PDB:4AC3"
FT STRAND 359..371
FT /evidence="ECO:0007829|PDB:4AC3"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:4AC3"
FT STRAND 386..389
FT /evidence="ECO:0007829|PDB:4AC3"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:4AC3"
FT STRAND 407..414
FT /evidence="ECO:0007829|PDB:4AC3"
FT HELIX 448..451
FT /evidence="ECO:0007829|PDB:4AC3"
FT HELIX 456..458
FT /evidence="ECO:0007829|PDB:4AC3"
SQ SEQUENCE 459 AA; 49428 MW; 5D1E226A8B9606E1 CRC64;
MSNFAIILAA GKGTRMKSDL PKVLHKVAGI SMLEHVFRSV GAIQPEKTVT VVGHKAELVE
EVLAEQTEFV TQSEQLGTGH AVMMTEPILE GLSGHTLVIA GDTPLITGES LKNLIDFHIN
HKNVATILTA ETDNPFGYGR IVRNDNAEVL RIVEQKDATD FEKQIKEINT GTYVFDNERL
FEALKNINTN NAQGEYYITD VIGIFRETGE KVGAYTLKDF DESLGVNDRV ALATAESVMR
RRINHKHMVN GVSFVNPEAT YIDIDVEIAP EVQIEANVIL KGQTKIGAET VLTNGTYVVD
STIGAGAVIT NSMIEESSVA DGVTVGPYAH IRPNSSLGAQ VHIGNFVEVK GSSIGENTKA
GHLTYIGNCE VGSNVNFGAG TITVNYDGKN KYKTVIGDNV FVGSNSTIIA PVELGDNSLV
GAGSTITKDV PADAIAIGRG RQINKDEYAT RLPHHPKNQ
