GLMU_MYCTA
ID GLMU_MYCTA Reviewed; 495 AA.
AC A5U161;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=MRA_1026;
OS Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=419947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25177 / H37Ra;
RX PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA Wang H., Wang S., Zhao G., Zhang Y.;
RT "Genetic basis of virulence attenuation revealed by comparative genomic
RT analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL PLoS ONE 3:E2375-E2375(2008).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS).
RX PubMed=19121323; DOI=10.1016/j.jmb.2008.12.031;
RA Parikh A., Verma S.K., Khan S., Prakash B., Nandicoori V.K.;
RT "PknB-mediated phosphorylation of a novel substrate, N-acetylglucosamine-1-
RT phosphate uridyltransferase, modulates its acetyltransferase activity.";
RL J. Mol. Biol. 386:451-464(2009).
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}.
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DR EMBL; CP000611; ABQ72761.1; -; Genomic_DNA.
DR RefSeq; WP_003405267.1; NZ_CP016972.1.
DR PDB; 3DK5; X-ray; 2.23 A; A=1-495.
DR PDBsum; 3DK5; -.
DR AlphaFoldDB; A5U161; -.
DR SMR; A5U161; -.
DR STRING; 419947.MRA_1026; -.
DR EnsemblBacteria; ABQ72761; ABQ72761; MRA_1026.
DR KEGG; mra:MRA_1026; -.
DR eggNOG; COG1207; Bacteria.
DR HOGENOM; CLU_029499_15_2_11; -.
DR OMA; TAIVEHK; -.
DR OrthoDB; 1381953at2; -.
DR BRENDA; 2.3.1.157; 3445.
DR BRENDA; 2.7.7.23; 3445.
DR UniPathway; UPA00113; UER00532.
DR UniPathway; UPA00113; UER00533.
DR UniPathway; UPA00973; -.
DR EvolutionaryTrace; A5U161; -.
DR Proteomes; UP000001988; 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; 3.
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 Repeat; Transferase.
FT CHAIN 1..495
FT /note="Bifunctional protein GlmU"
FT /id="PRO_0000337733"
FT REGION 1..241
FT /note="Pyrophosphorylase"
FT /evidence="ECO:0000250, ECO:0000255|HAMAP-Rule:MF_01631"
FT REGION 242..262
FT /note="Linker"
FT /evidence="ECO:0000250, ECO:0000255|HAMAP-Rule:MF_01631"
FT REGION 263..495
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000250, ECO:0000255|HAMAP-Rule:MF_01631"
FT REGION 457..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 374
FT /note="Proton acceptor"
FT /evidence="ECO:0000250, ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 12..15
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 26
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 83
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 88..89
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 112..114
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 114
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250, ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 151
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 166
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 181
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 239
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250, ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 239
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 344
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 362
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 377
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 388
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 391
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 397..398
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250, ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 416
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250, ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 434
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250, ECO:0000255|HAMAP-Rule:MF_01631"
FT STRAND 7..13
FT /evidence="ECO:0007829|PDB:3DK5"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:3DK5"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:3DK5"
FT HELIX 36..47
FT /evidence="ECO:0007829|PDB:3DK5"
FT STRAND 50..58
FT /evidence="ECO:0007829|PDB:3DK5"
FT HELIX 60..63
FT /evidence="ECO:0007829|PDB:3DK5"
FT TURN 64..69
FT /evidence="ECO:0007829|PDB:3DK5"
FT HELIX 70..73
FT /evidence="ECO:0007829|PDB:3DK5"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:3DK5"
FT HELIX 89..97
FT /evidence="ECO:0007829|PDB:3DK5"
FT STRAND 106..114
FT /evidence="ECO:0007829|PDB:3DK5"
FT HELIX 120..132
FT /evidence="ECO:0007829|PDB:3DK5"
FT STRAND 136..142
FT /evidence="ECO:0007829|PDB:3DK5"
FT STRAND 180..187
FT /evidence="ECO:0007829|PDB:3DK5"
FT HELIX 189..197
FT /evidence="ECO:0007829|PDB:3DK5"
FT HELIX 212..219
FT /evidence="ECO:0007829|PDB:3DK5"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:3DK5"
FT HELIX 232..235
FT /evidence="ECO:0007829|PDB:3DK5"
FT HELIX 241..261
FT /evidence="ECO:0007829|PDB:3DK5"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:3DK5"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:3DK5"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:3DK5"
FT STRAND 288..293
FT /evidence="ECO:0007829|PDB:3DK5"
FT STRAND 309..315
FT /evidence="ECO:0007829|PDB:3DK5"
FT STRAND 323..331
FT /evidence="ECO:0007829|PDB:3DK5"
FT STRAND 339..343
FT /evidence="ECO:0007829|PDB:3DK5"
FT STRAND 347..349
FT /evidence="ECO:0007829|PDB:3DK5"
FT STRAND 354..357
FT /evidence="ECO:0007829|PDB:3DK5"
FT STRAND 359..363
FT /evidence="ECO:0007829|PDB:3DK5"
FT STRAND 371..375
FT /evidence="ECO:0007829|PDB:3DK5"
FT STRAND 377..383
FT /evidence="ECO:0007829|PDB:3DK5"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:3DK5"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:3DK5"
FT STRAND 419..423
FT /evidence="ECO:0007829|PDB:3DK5"
FT HELIX 460..464
FT /evidence="ECO:0007829|PDB:3DK5"
FT TURN 466..469
FT /evidence="ECO:0007829|PDB:3DK5"
FT STRAND 470..472
FT /evidence="ECO:0007829|PDB:3DK5"
SQ SEQUENCE 495 AA; 51584 MW; C14DC76BD6E5EC86 CRC64;
MTFPGDTAVL VLAAGPGTRM RSDTPKVLHT LAGRSMLSHV LHAIAKLAPQ RLIVVLGHDH
QRIAPLVGEL ADTLGRTIDV ALQDRPLGTG HAVLCGLSAL PDDYAGNVVV TSGDTPLLDA
DTLADLIATH RAVSAAVTVL TTTLDDPFGY GRILRTQDHE VMAIVEQTDA TPSQREIREV
NAGVYAFDIA ALRSALSRLS SNNAQQELYL TDVIAILRSD GQTVHASHVD DSALVAGVNN
RVQLAELASE LNRRVVAAHQ LAGVTVVDPA TTWIDVDVTI GRDTVIHPGT QLLGRTQIGG
RCVVGPDTTL TDVAVGDGAS VVRTHGSSSS IGDGAAVGPF TYLRPGTALG ADGKLGAFVE
VKNSTIGTGT KVPHLTYVGD ADIGEYSNIG ASSVFVNYDG TSKRRTTVGS HVRTGSDTMF
VAPVTIGDGA YTGAGTVVRE DVPPGALAVS AGPQRNIENW VQRKRPGSPA AQASKRASEM
ACQQPTQPPD ADQTP
