GLMU_YERPE
ID GLMU_YERPE Reviewed; 456 AA.
AC Q8Z9S7; Q0W9R8; Q74PA2; Q8CZF5;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 129.
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};
GN OrderedLocusNames=YPO4119, y4133, YP_4026;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) IN COMPLEX WITH UDP-GLCNAC ANALOG.
RA Nocek B., Kuhn M., Gu M., Anderson W.F., Joachimiak A.;
RT "Crystal structure of yersinia pestis GlmU in complex with alp glucosamine
RT 1-phosphate (gp1).";
RL Submitted (MAY-2012) to the PDB data bank.
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: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, 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=AAM87675.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAS64165.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL590842; CAL22687.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM87675.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE017042; AAS64165.1; ALT_INIT; Genomic_DNA.
DR PIR; AC0500; AC0500.
DR RefSeq; WP_002215550.1; NZ_WUCM01000028.1.
DR RefSeq; YP_002348970.1; NC_003143.1.
DR PDB; 4FCE; X-ray; 1.96 A; A=1-456.
DR PDBsum; 4FCE; -.
DR AlphaFoldDB; Q8Z9S7; -.
DR SMR; Q8Z9S7; -.
DR IntAct; Q8Z9S7; 6.
DR STRING; 214092.YPO4119; -.
DR PaxDb; Q8Z9S7; -.
DR DNASU; 1149080; -.
DR EnsemblBacteria; AAM87675; AAM87675; y4133.
DR EnsemblBacteria; AAS64165; AAS64165; YP_4026.
DR GeneID; 66843619; -.
DR KEGG; ype:YPO4119; -.
DR KEGG; ypk:y4133; -.
DR KEGG; ypm:YP_4026; -.
DR PATRIC; fig|214092.21.peg.4663; -.
DR eggNOG; COG1207; Bacteria.
DR HOGENOM; CLU_029499_15_2_6; -.
DR UniPathway; UPA00113; UER00532.
DR UniPathway; UPA00113; UER00533.
DR UniPathway; UPA00973; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; 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; 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.
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..456
FT /note="Bifunctional protein GlmU"
FT /id="PRO_0000233888"
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..456
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT ACT_SITE 363
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 11..14
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 25
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 140
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="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: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:0000255|HAMAP-Rule:MF_01631"
FT BINDING 227
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="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:0000255|HAMAP-Rule:MF_01631"
FT BINDING 333
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|Ref.4"
FT BINDING 351
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|Ref.4"
FT BINDING 366
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|Ref.4"
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 ECO:0000269|Ref.4"
FT BINDING 380
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 386..387
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 405
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 423
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 440
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT STRAND 6..12
FT /evidence="ECO:0007829|PDB:4FCE"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:4FCE"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:4FCE"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:4FCE"
FT HELIX 35..46
FT /evidence="ECO:0007829|PDB:4FCE"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:4FCE"
FT HELIX 59..65
FT /evidence="ECO:0007829|PDB:4FCE"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:4FCE"
FT HELIX 82..89
FT /evidence="ECO:0007829|PDB:4FCE"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:4FCE"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:4FCE"
FT HELIX 111..120
FT /evidence="ECO:0007829|PDB:4FCE"
FT STRAND 125..132
FT /evidence="ECO:0007829|PDB:4FCE"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:4FCE"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:4FCE"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:4FCE"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:4FCE"
FT STRAND 167..176
FT /evidence="ECO:0007829|PDB:4FCE"
FT HELIX 177..185
FT /evidence="ECO:0007829|PDB:4FCE"
FT HELIX 200..207
FT /evidence="ECO:0007829|PDB:4FCE"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:4FCE"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:4FCE"
FT HELIX 229..250
FT /evidence="ECO:0007829|PDB:4FCE"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:4FCE"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:4FCE"
FT STRAND 260..268
FT /evidence="ECO:0007829|PDB:4FCE"
FT STRAND 278..286
FT /evidence="ECO:0007829|PDB:4FCE"
FT STRAND 297..300
FT /evidence="ECO:0007829|PDB:4FCE"
FT STRAND 314..317
FT /evidence="ECO:0007829|PDB:4FCE"
FT STRAND 328..332
FT /evidence="ECO:0007829|PDB:4FCE"
FT STRAND 343..355
FT /evidence="ECO:0007829|PDB:4FCE"
FT STRAND 360..372
FT /evidence="ECO:0007829|PDB:4FCE"
FT STRAND 383..385
FT /evidence="ECO:0007829|PDB:4FCE"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:4FCE"
FT STRAND 408..415
FT /evidence="ECO:0007829|PDB:4FCE"
SQ SEQUENCE 456 AA; 48840 MW; 30C8729567281E6A CRC64;
MSNSSMSVVI LAAGKGTRMY SDLPKVLHPL AGKPMVQHVI DAAMKLGAQH VHLVYGHGGE
LLKKTLADPS LNWVLQAEQL GTGHAMQQAA PHFADDEDIL MLYGDVPLIS VDTLQRLLAA
KPEGGIGLLT VKLDNPSGYG RIVRENGDVV GIVEHKDASD AQREINEINT GILVANGRDL
KRWLSLLDNN NAQGEFYITD IIALAHADGK KIATVHPTRL SEVEGVNNRL QLSALERVFQ
TEQAEKLLLA GVMLLDPSRF DLRGELTHGR DITIDTNVII EGHVILGDRV RIGTGCVLKN
CVIGDDSEIS PYTVLEDARL DANCTVGPFA RLRPGAELAE GAHVGNFVEI KKARLGKGSK
AGHLSYLGDA EIGAGVNIGA GTITCNYDGA NKFKTIIGDD VFVGSDTQLV APVTVANGAT
IGAGTTVTRD VAENELVISR VKQVHIQGWK RPVKKK
