GLMU_MYCTU
ID GLMU_MYCTU Reviewed; 495 AA.
AC P9WMN3; L0T872; P96382; Q7D8Z8;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 54.
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, ECO:0000269|PubMed:19121323, ECO:0000269|PubMed:19237750};
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, ECO:0000269|PubMed:19121323, ECO:0000269|PubMed:19237750};
GN Name=glmU {ECO:0000255|HAMAP-Rule:MF_01631}; OrderedLocusNames=Rv1018c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP PUPYLATION AT LYS-362, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20066036; DOI=10.1371/journal.pone.0008589;
RA Festa R.A., McAllister F., Pearce M.J., Mintseris J., Burns K.E.,
RA Gygi S.P., Darwin K.H.;
RT "Prokaryotic ubiquitin-like protein (Pup) proteome of Mycobacterium
RT tuberculosis.";
RL PLoS ONE 5:E8589-E8589(2010).
RN [3]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS,
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND SUBUNIT.
RX PubMed=19237750; DOI=10.1107/s0907444909001036;
RA Zhang Z., Bulloch E.M., Bunker R.D., Baker E.N., Squire C.J.;
RT "Structure and function of GlmU from Mycobacterium tuberculosis.";
RL Acta Crystallogr. D 65:275-283(2009).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.41 ANGSTROMS), AND SUBUNIT.
RX PubMed=19407371; DOI=10.1107/s1744309109010252;
RA Verma S.K., Jaiswal M., Kumar N., Parikh A., Nandicoori V.K., Prakash B.;
RT "Structure of N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) from
RT Mycobacterium tuberculosis in a cubic space group.";
RL Acta Crystallogr. F 65:435-439(2009).
RN [6] {ECO:0007744|PDB:3DJ4}
RP X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS
RP AND MAGNESIUM IONS, FUNCTION, CATALYTIC ACTIVITY, PHOSPHORYLATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND SUBUNIT.
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).
RN [7] {ECO:0007744|PDB:3SPT}
RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) IN COMPLEX WITH UDP-GLCNAC;
RP ACETYL-COA AND MAGNESIUM IONS, COFACTOR, AND SUBUNIT.
RA Jagtap P.A., Prakash B.;
RT "Structure of Mycobacterium tuberculosis GlmU in complex with Acetyl CoA.";
RL Submitted (JUL-2011) to the PDB data bank.
RN [8] {ECO:0007744|PDB:4G3P, ECO:0007744|PDB:4G3Q, ECO:0007744|PDB:4G3S}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH UDP-GLCNAC;
RP MAGNESIUM AND COBALT IONS, AND COFACTOR.
RA Jagtap P.A., Verma S.K., Prakash B.;
RT "Structural snapshots of Glmu from Mycobacterium tuberculosis.";
RL Submitted (JUL-2012) to the PDB data bank.
RN [9] {ECO:0007744|PDB:4G87, ECO:0007744|PDB:4HCQ}
RP X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) IN COMPLEX WITH UDP-GLCNAC;
RP MAGNESIUM AND COBALT IONS, COFACTOR, AND REACTION MECHANISM.
RX PubMed=23485416; DOI=10.1016/j.jmb.2013.02.019;
RA Jagtap P.K., Verma S.K., Vithani N., Bais V.S., Prakash B.;
RT "Crystal structures identify an atypical two-metal-ion mechanism for
RT uridyltransfer in GlmU: its significance to sugar nucleotidyl
RT transferases.";
RL J. Mol. Biol. 425:1745-1759(2013).
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, ECO:0000269|PubMed:19121323,
CC ECO:0000269|PubMed:19237750}.
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 ECO:0000269|PubMed:19121323, ECO:0000269|PubMed:19237750};
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 ECO:0000269|PubMed:19121323, ECO:0000269|PubMed:19237750};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:19121323, ECO:0000269|PubMed:19237750,
CC ECO:0000269|PubMed:23485416, ECO:0000269|Ref.7, ECO:0000269|Ref.8};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:23485416, ECO:0000269|Ref.8};
CC Note=Binds 1 Mg(2+) ion per subunit (PubMed:19237750, PubMed:19121323,
CC Ref.7, Ref.8, PubMed:23485416). Can also use Co(2+) ion to a lesser
CC extent (Ref.8) (PubMed:23485416). {ECO:0000269|PubMed:19121323,
CC ECO:0000269|PubMed:19237750, ECO:0000269|PubMed:23485416,
CC ECO:0000269|Ref.7, ECO:0000269|Ref.8};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=106.75 uM for GlcNAc-1-P (at pH 7.6)
CC {ECO:0000269|PubMed:19121323};
CC KM=61.86 uM for UTP (at pH 7.6) {ECO:0000269|PubMed:19121323};
CC KM=240 uM for GlcN-1-P (at pH 7.6) {ECO:0000269|PubMed:19121323};
CC KM=304 uM for acetyl-CoA (at pH 7.6) {ECO:0000269|PubMed:19121323};
CC Vmax=1.869 umol/min/mg enzyme (Uridyltransferase activity) (at pH
CC 7.6) {ECO:0000269|PubMed:19121323};
CC Vmax=4.489 umol/min/mg enzyme (Acetyltransferase activity) (at pH
CC 7.6) {ECO:0000269|PubMed:19121323};
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:19121323, ECO:0000269|PubMed:19237750,
CC ECO:0000269|PubMed:19407371, ECO:0000269|Ref.7}.
CC -!- INTERACTION:
CC P9WMN3; P10145: CXCL8; Xeno; NbExp=3; IntAct=EBI-11740532, EBI-3917999;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01631}.
CC -!- PTM: Phosphorylated at the C-terminal domain by PknB. The
CC phosphorylation is required for acetyltransferase activity, but does
CC not affect uridyltransferase activity. {ECO:0000269|PubMed:19121323}.
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; AL123456; CCP43768.1; -; Genomic_DNA.
DR PIR; E70622; E70622.
DR RefSeq; NP_215534.1; NC_000962.3.
DR RefSeq; WP_003405267.1; NZ_NVQJ01000018.1.
DR PDB; 2QKX; X-ray; 2.75 A; A=1-389.
DR PDB; 3D8V; X-ray; 2.55 A; A=1-495.
DR PDB; 3D98; X-ray; 2.50 A; A=1-495.
DR PDB; 3DJ4; X-ray; 2.38 A; A=1-495.
DR PDB; 3FOQ; X-ray; 3.41 A; A=1-495.
DR PDB; 3SPT; X-ray; 2.33 A; A=1-495.
DR PDB; 3ST8; X-ray; 1.98 A; A=1-495.
DR PDB; 4G3P; X-ray; 2.47 A; A=1-495.
DR PDB; 4G3Q; X-ray; 1.90 A; A=1-495.
DR PDB; 4G3S; X-ray; 2.04 A; A=1-495.
DR PDB; 4G87; X-ray; 2.03 A; A=1-495.
DR PDB; 4HCQ; X-ray; 2.60 A; A=1-495.
DR PDBsum; 2QKX; -.
DR PDBsum; 3D8V; -.
DR PDBsum; 3D98; -.
DR PDBsum; 3DJ4; -.
DR PDBsum; 3FOQ; -.
DR PDBsum; 3SPT; -.
DR PDBsum; 3ST8; -.
DR PDBsum; 4G3P; -.
DR PDBsum; 4G3Q; -.
DR PDBsum; 4G3S; -.
DR PDBsum; 4G87; -.
DR PDBsum; 4HCQ; -.
DR AlphaFoldDB; P9WMN3; -.
DR SMR; P9WMN3; -.
DR IntAct; P9WMN3; 1.
DR STRING; 83332.Rv1018c; -.
DR ChEMBL; CHEMBL1293297; -.
DR DrugCentral; P9WMN3; -.
DR iPTMnet; P9WMN3; -.
DR PaxDb; P9WMN3; -.
DR DNASU; 886069; -.
DR GeneID; 886069; -.
DR KEGG; mtu:Rv1018c; -.
DR TubercuList; Rv1018c; -.
DR eggNOG; COG1207; Bacteria.
DR OMA; TAIVEHK; -.
DR PhylomeDB; P9WMN3; -.
DR BRENDA; 2.3.1.157; 3445.
DR BRENDA; 2.7.7.23; 3445.
DR SABIO-RK; P9WMN3; -.
DR UniPathway; UPA00113; UER00532.
DR UniPathway; UPA00113; UER00533.
DR UniPathway; UPA00973; -.
DR PRO; PR:P9WMN3; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019134; F:glucosamine-1-phosphate N-acetyltransferase activity; IDA:MTBBASE.
DR GO; GO:0000287; F:magnesium ion binding; IDA:MTBBASE.
DR GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IDA:MTBBASE.
DR GO; GO:0070569; F:uridylyltransferase activity; IDA:MTBBASE.
DR GO; GO:0044650; P:adhesion of symbiont to host cell; IMP:AgBase.
DR GO; GO:0000902; P:cell morphogenesis; IEA:UniProtKB-UniRule.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0035635; P:entry of bacterium into host cell; IMP:AgBase.
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; IDA:UniProtKB.
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; Acetylation; Acyltransferase; Cell shape;
KW Cell wall biogenesis/degradation; Cytoplasm; Isopeptide bond; Magnesium;
KW Metal-binding; Multifunctional enzyme; Nucleotidyltransferase;
KW Peptidoglycan synthesis; Reference proteome; Repeat; Transferase;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:21969609"
FT CHAIN 2..495
FT /note="Bifunctional protein GlmU"
FT /id="PRO_0000233802"
FT REGION 2..241
FT /note="Pyrophosphorylase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT REGION 242..262
FT /note="Linker"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT REGION 263..495
FT /note="N-acetyltransferase"
FT /evidence="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:0000255|HAMAP-Rule:MF_01631,
FT ECO:0000305|Ref.7"
FT BINDING 12..15
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:19237750, ECO:0000269|PubMed:23485416,
FT ECO:0000269|Ref.7, ECO:0000269|Ref.8"
FT BINDING 26
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.8"
FT BINDING 83
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:19237750, ECO:0000269|Ref.7"
FT BINDING 88..89
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:19237750, ECO:0000269|PubMed:23485416,
FT ECO:0000269|Ref.7, ECO:0000269|Ref.8"
FT BINDING 112..114
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:19237750, ECO:0000269|PubMed:23485416,
FT ECO:0000269|Ref.8"
FT BINDING 114
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000269|PubMed:23485416, ECO:0000269|Ref.8,
FT ECO:0007744|PDB:4G87"
FT BINDING 114
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:19121323,
FT ECO:0000269|PubMed:23485416, ECO:0000269|Ref.7,
FT ECO:0007744|PDB:3SPT, ECO:0007744|PDB:4HCQ"
FT BINDING 151
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:19237750, ECO:0000269|PubMed:23485416,
FT ECO:0000269|Ref.7, ECO:0000269|Ref.8"
FT BINDING 166
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:19237750, ECO:0000269|PubMed:23485416,
FT ECO:0000269|Ref.7, ECO:0000269|Ref.8"
FT BINDING 181
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:19237750, ECO:0000269|PubMed:23485416,
FT ECO:0000269|Ref.7, ECO:0000269|Ref.8"
FT BINDING 239
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000269|PubMed:23485416, ECO:0000269|Ref.8,
FT ECO:0007744|PDB:4G87"
FT BINDING 239
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:19121323,
FT ECO:0000269|PubMed:23485416, ECO:0000269|Ref.7,
FT ECO:0007744|PDB:3SPT, ECO:0007744|PDB:4HCQ"
FT BINDING 239
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:19237750, ECO:0000269|PubMed:23485416,
FT ECO:0000269|Ref.7, ECO:0000269|Ref.8"
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 ECO:0000269|PubMed:23485416, ECO:0000269|Ref.8"
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 ECO:0000269|PubMed:23485416, ECO:0000269|Ref.8"
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|PubMed:23485416, ECO:0000269|Ref.8"
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 ECO:0000269|Ref.7"
FT BINDING 391
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631,
FT ECO:0000269|Ref.7"
FT BINDING 397..398
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 416
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631,
FT ECO:0000269|Ref.7"
FT BINDING 434
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|Ref.7"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:21969609"
FT CROSSLNK 362
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-Cter in protein Pup)"
FT /evidence="ECO:0000269|PubMed:20066036"
FT STRAND 7..13
FT /evidence="ECO:0007829|PDB:4G3Q"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:4G3Q"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:3D98"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:4G3Q"
FT HELIX 36..47
FT /evidence="ECO:0007829|PDB:4G3Q"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:4G3Q"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:4G3Q"
FT HELIX 64..74
FT /evidence="ECO:0007829|PDB:4G3Q"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:4G3Q"
FT HELIX 89..97
FT /evidence="ECO:0007829|PDB:4G3Q"
FT STRAND 106..112
FT /evidence="ECO:0007829|PDB:4G3Q"
FT HELIX 120..132
FT /evidence="ECO:0007829|PDB:4G3Q"
FT STRAND 136..143
FT /evidence="ECO:0007829|PDB:4G3Q"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:4G3Q"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:3FOQ"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:4G3Q"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:4G3Q"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:4G3Q"
FT STRAND 179..187
FT /evidence="ECO:0007829|PDB:4G3Q"
FT HELIX 189..196
FT /evidence="ECO:0007829|PDB:4G3Q"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:3D98"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:4G3Q"
FT HELIX 213..219
FT /evidence="ECO:0007829|PDB:4G3Q"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:4G3Q"
FT HELIX 232..235
FT /evidence="ECO:0007829|PDB:4G3Q"
FT HELIX 241..261
FT /evidence="ECO:0007829|PDB:4G3Q"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:4G3Q"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:4G3Q"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:4G3Q"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:4G87"
FT STRAND 288..293
FT /evidence="ECO:0007829|PDB:4G3Q"
FT STRAND 309..315
FT /evidence="ECO:0007829|PDB:4G3Q"
FT STRAND 323..331
FT /evidence="ECO:0007829|PDB:4G3Q"
FT STRAND 339..343
FT /evidence="ECO:0007829|PDB:4G3Q"
FT STRAND 347..349
FT /evidence="ECO:0007829|PDB:4G87"
FT STRAND 354..363
FT /evidence="ECO:0007829|PDB:4G3Q"
FT STRAND 371..383
FT /evidence="ECO:0007829|PDB:4G3Q"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:4G3Q"
FT STRAND 400..403
FT /evidence="ECO:0007829|PDB:3ST8"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:4G3Q"
FT STRAND 419..423
FT /evidence="ECO:0007829|PDB:4G3Q"
FT HELIX 460..464
FT /evidence="ECO:0007829|PDB:4G3Q"
FT HELIX 469..479
FT /evidence="ECO:0007829|PDB:4G3Q"
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
