GLMU_STRPN
ID GLMU_STRPN Reviewed; 459 AA.
AC Q97R46;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
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=SP_0988;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF NATIVE PROTEIN AND IN COMPLEX
RP WITH ACETYL-COA; CALCIUM ION AND UDP-GLCNAC, SUBUNIT, AND COFACTOR.
RC STRAIN=R6 / R800;
RX PubMed=11118459; DOI=10.1074/jbc.m011225200;
RA Sulzenbacher G., Gal L., Peneff C., Fassy F., Bourne Y.;
RT "Crystal structure of Streptococcus pneumoniae N-acetylglucosamine-1-
RT phosphate uridyltransferase bound to acetyl-coenzyme A reveals a novel
RT active site architecture.";
RL J. Biol. Chem. 276:11844-11851(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF NATIVE PROTEIN AND IN COMPLEX
RP WITH BOTH UDP-GLCNAC AND MAGNESIUM, SUBUNIT, AND COFACTOR.
RX PubMed=11124906; DOI=10.1006/jmbi.2000.4296;
RA Kostrewa D., D'Arcy A., Takacs B., Kamber M.;
RT "Crystal structures of Streptococcus pneumoniae N-acetylglucosamine-1-
RT phosphate uridyltransferase, GlmU, in apo form at 2.33 A resolution and in
RT complex with UDP-N-acetylglucosamine and Mg(2+) at 1.96 A resolution.";
RL J. Mol. Biol. 305:279-289(2001).
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:0000269|PubMed:11124906};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:11118459};
CC Note=Binds 1 Mg(2+) ion per subunit (PubMed:11124906). Can also use
CC Ca(2+) ion to a lesser extent (PubMed:11118459).
CC {ECO:0000269|PubMed:11118459, ECO:0000269|PubMed:11124906};
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 ECO:0000269|PubMed:11118459, ECO:0000269|PubMed:11124906}.
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, 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}.
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DR EMBL; AE005672; AAK75107.1; -; Genomic_DNA.
DR PIR; B95114; B95114.
DR RefSeq; WP_000064406.1; NZ_AKVY01000001.1.
DR PDB; 1G95; X-ray; 2.33 A; A=1-459.
DR PDB; 1G97; X-ray; 1.96 A; A=1-459.
DR PDB; 1HM0; X-ray; 2.30 A; A/B=2-459.
DR PDB; 1HM8; X-ray; 2.50 A; A/B=2-459.
DR PDB; 1HM9; X-ray; 1.75 A; A/B=2-459.
DR PDBsum; 1G95; -.
DR PDBsum; 1G97; -.
DR PDBsum; 1HM0; -.
DR PDBsum; 1HM8; -.
DR PDBsum; 1HM9; -.
DR AlphaFoldDB; Q97R46; -.
DR SMR; Q97R46; -.
DR STRING; 170187.SP_0988; -.
DR BindingDB; Q97R46; -.
DR ChEMBL; CHEMBL1949487; -.
DR DrugBank; DB03397; Uridine-Diphosphate-N-Acetylglucosamine.
DR EnsemblBacteria; AAK75107; AAK75107; SP_0988.
DR KEGG; spn:SP_0988; -.
DR eggNOG; COG1207; Bacteria.
DR OMA; TAIVEHK; -.
DR PhylomeDB; Q97R46; -.
DR BioCyc; SPNE170187:G1FZB-1017-MON; -.
DR BRENDA; 2.3.1.157; 1960.
DR BRENDA; 2.7.7.23; 1960.
DR UniPathway; UPA00113; UER00532.
DR UniPathway; UPA00113; UER00533.
DR UniPathway; UPA00973; -.
DR EvolutionaryTrace; Q97R46; -.
DR PRO; PR:Q97R46; -.
DR Proteomes; UP000000585; 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 Repeat; Transferase.
FT CHAIN 1..459
FT /note="Bifunctional protein GlmU"
FT /id="PRO_0000233850"
FT REGION 1..229
FT /note="Pyrophosphorylase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT REGION 230..250
FT /note="Linker"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT REGION 251..459
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 8..11
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631,
FT ECO:0000269|PubMed:11118459, ECO:0000269|PubMed:11124906"
FT BINDING 22
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631,
FT ECO:0000269|PubMed:11118459"
FT BINDING 72
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631,
FT ECO:0000269|PubMed:11118459, ECO:0000269|PubMed:11124906"
FT BINDING 77..78
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631,
FT ECO:0000269|PubMed:11118459, ECO:0000269|PubMed:11124906"
FT BINDING 101..102
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000269|PubMed:11118459,
FT ECO:0000269|PubMed:11124906"
FT BINDING 102
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:11118459"
FT BINDING 102
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:11124906,
FT ECO:0007744|PDB:1G97"
FT BINDING 139
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631,
FT ECO:0000269|PubMed:11118459, ECO:0000269|PubMed:11124906"
FT BINDING 154
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631,
FT ECO:0000269|PubMed:11118459, ECO:0000269|PubMed:11124906"
FT BINDING 169
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631,
FT ECO:0000269|PubMed:11118459, ECO:0000269|PubMed:11124906"
FT BINDING 227
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:11118459"
FT BINDING 227
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:11124906,
FT ECO:0007744|PDB:1G97"
FT BINDING 227
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631,
FT ECO:0000269|PubMed:11118459"
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 ECO:0000269|PubMed:11118459"
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 3..8
FT /evidence="ECO:0007829|PDB:1HM9"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:1HM9"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:1HM9"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:1HM9"
FT HELIX 32..41
FT /evidence="ECO:0007829|PDB:1HM9"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:1HM9"
FT HELIX 56..61
FT /evidence="ECO:0007829|PDB:1HM9"
FT STRAND 62..71
FT /evidence="ECO:0007829|PDB:1HM9"
FT HELIX 78..83
FT /evidence="ECO:0007829|PDB:1HM9"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:1HM9"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:1HM9"
FT HELIX 108..120
FT /evidence="ECO:0007829|PDB:1HM9"
FT STRAND 124..131
FT /evidence="ECO:0007829|PDB:1HM9"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:1HM9"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:1HM9"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:1HM9"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:1HM9"
FT STRAND 167..176
FT /evidence="ECO:0007829|PDB:1HM9"
FT HELIX 177..184
FT /evidence="ECO:0007829|PDB:1HM9"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:1HM0"
FT HELIX 200..208
FT /evidence="ECO:0007829|PDB:1HM9"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:1HM9"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:1HM9"
FT HELIX 229..249
FT /evidence="ECO:0007829|PDB:1HM9"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:1HM9"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:1HM9"
FT STRAND 279..283
FT /evidence="ECO:0007829|PDB:1HM9"
FT STRAND 297..300
FT /evidence="ECO:0007829|PDB:1HM9"
FT STRAND 313..316
FT /evidence="ECO:0007829|PDB:1HM9"
FT STRAND 333..337
FT /evidence="ECO:0007829|PDB:1G95"
FT STRAND 342..351
FT /evidence="ECO:0007829|PDB:1HM9"
FT STRAND 359..371
FT /evidence="ECO:0007829|PDB:1HM9"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:1HM9"
FT STRAND 386..389
FT /evidence="ECO:0007829|PDB:1G97"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:1HM9"
FT STRAND 407..411
FT /evidence="ECO:0007829|PDB:1HM9"
FT HELIX 448..451
FT /evidence="ECO:0007829|PDB:1HM9"
FT HELIX 456..458
FT /evidence="ECO:0007829|PDB:1HM9"
SQ SEQUENCE 459 AA; 49345 MW; F4EFE18D768DC4A3 CRC64;
MSNFAIILAA GKGTRMKSDL PKVLHKVAGI SMLEHVFRSV GAIQPEKTVT VVGHKAELVE
EVLAGQTEFV TQSEQLGTGH AVMMTEPILE GLSGHTLVIA GDTPLITGES LKNLIDFHIN
HKNVATILTA ETDNPFGYGR IVRNDNAEVL RIVEQKDATD FEKQIKEINT GTYVFDNERL
FEALKNINTN NAQGEYYITD VIGIFRETGE KVGAYTLKDF DESLGVNDRV ALATAESVMR
RRINHKHMVN GVSFVNPEAT YIDIDVEIAS EVQIEANVTL KGQTKIGAET VLTNGTYVVD
STIGAGAVIT NSMIEESSVA DGVIVGPYAH IRPNSSLGAQ VHIGNFVEVK GSSIGENTKA
GHLTYIGNCE VGSNVNFGAG TITVNYDGKN KYKTVIGNNV FVGSNSTIIA PVELGDNSLV
GAGSTITKDV PADAIAIGRG RQINKDEYAT RLPHHPKNQ
