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Database: UniProt
Entry: E1VTR4_GLUAR
LinkDB: E1VTR4_GLUAR
Original site: E1VTR4_GLUAR 
ID   E1VTR4_GLUAR            Unreviewed;       483 AA.
AC   E1VTR4;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 88.
DE   RecName: Full=Bifunctional protein GlmU {ECO:0000256|HAMAP-Rule:MF_01631};
DE   Includes:
DE     RecName: Full=UDP-N-acetylglucosamine pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_01631};
DE              EC=2.7.7.23 {ECO:0000256|HAMAP-Rule:MF_01631};
DE     AltName: Full=N-acetylglucosamine-1-phosphate uridyltransferase {ECO:0000256|HAMAP-Rule:MF_01631};
DE   Includes:
DE     RecName: Full=Glucosamine-1-phosphate N-acetyltransferase {ECO:0000256|HAMAP-Rule:MF_01631};
DE              EC=2.3.1.157 {ECO:0000256|HAMAP-Rule:MF_01631};
GN   Name=glmU {ECO:0000256|HAMAP-Rule:MF_01631,
GN   ECO:0000313|EMBL:CBT75017.1};
GN   OrderedLocusNames=AARI_07960 {ECO:0000313|EMBL:CBT75017.1};
OS   Glutamicibacter arilaitensis (strain DSM 16368 / CIP 108037 / IAM 15318 /
OS   JCM 13566 / NCIMB 14258 / Re117) (Arthrobacter arilaitensis).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Glutamicibacter.
OX   NCBI_TaxID=861360 {ECO:0000313|Proteomes:UP000006878};
RN   [1] {ECO:0000313|EMBL:CBT75017.1, ECO:0000313|Proteomes:UP000006878}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 16368 / CIP 108037 / IAM 15318 / JCM 13566 / Re117
RC   {ECO:0000313|Proteomes:UP000006878};
RX   PubMed=21124797; DOI=10.1371/journal.pone.0015489;
RA   Monnet C., Loux V., Gibrat J.F., Spinnler E., Barbe V., Vacherie B.,
RA   Gavory F., Gourbeyre E., Siguier P., Chandler M., Elleuch R., Irlinger F.,
RA   Vallaeys T.;
RT   "The Arthrobacter arilaitensis Re117 genome sequence reveals its genetic
RT   adaptation to the surface of cheese.";
RL   PLoS ONE 5:E15489-E15489(2010).
RN   [2] {ECO:0000313|Proteomes:UP000006878}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16368 / CIP 108037 / IAM 15318 / JCM 13566 / Re117
RC   {ECO:0000313|Proteomes:UP000006878};
RA   Genoscope.;
RT   "Complete genome sequence of Arthrobacter arilaitensis (strain DSM 16368 /
RT   CIP 108037 / JCM 13566 / Re117).";
RL   Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|ARBA:ARBA00001851, ECO:0000256|HAMAP-
CC         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:0000256|ARBA:ARBA00000731, ECO:0000256|HAMAP-
CC         Rule:MF_01631};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01631};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01631};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
CC       {ECO:0000256|HAMAP-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:0000256|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:0000256|HAMAP-
CC       Rule:MF_01631}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_01631}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_01631}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the transferase
CC       hexapeptide repeat family. {ECO:0000256|ARBA:ARBA00007707,
CC       ECO:0000256|HAMAP-Rule:MF_01631}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the N-
CC       acetylglucosamine-1-phosphate uridyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00007947, ECO:0000256|HAMAP-Rule:MF_01631}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01631}.
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DR   EMBL; FQ311875; CBT75017.1; -; Genomic_DNA.
DR   AlphaFoldDB; E1VTR4; -.
DR   STRING; 861360.AARI_07960; -.
DR   KEGG; aai:AARI_07960; -.
DR   eggNOG; COG1207; Bacteria.
DR   HOGENOM; CLU_029499_15_2_11; -.
DR   OMA; TAIVEHK; -.
DR   UniPathway; UPA00113; UER00532.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000006878; 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; cd02540; GT2_GlmU_N_bac; 1.
DR   CDD; cd03353; LbH_GlmU_C; 1.
DR   Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 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   NCBIfam; TIGR01173; glmU; 1.
DR   PANTHER; PTHR43584:SF3; BIFUNCTIONAL PROTEIN GLMU; 1.
DR   PANTHER; PTHR43584; NUCLEOTIDYL TRANSFERASE; 1.
DR   Pfam; PF00132; Hexapep; 1.
DR   Pfam; PF12804; NTP_transf_3; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW   Rule:MF_01631};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW   Rule:MF_01631};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW   ECO:0000256|HAMAP-Rule:MF_01631};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01631};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01631};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01631};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW   Rule:MF_01631};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_01631};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW   Rule:MF_01631}; Reference proteome {ECO:0000313|Proteomes:UP000006878};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_01631};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01631}.
FT   DOMAIN          11..141
FT                   /note="MobA-like NTP transferase"
FT                   /evidence="ECO:0000259|Pfam:PF12804"
FT   REGION          1..239
FT                   /note="Pyrophosphorylase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   REGION          240..260
FT                   /note="Linker"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   REGION          261..483
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   REGION          454..483
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        469..483
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        372
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         14..17
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         28
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         81
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         86..87
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         110..112
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         112
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         149
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         164
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         179
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         237
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         237
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         342
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         360
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         375
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         386
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         395..396
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         414
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         432
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
SQ   SEQUENCE   483 AA;  51161 MW;  C901F4855FB4ED20 CRC64;
     MSDQVNAPVA VIVLAAGAGT RMKSAKPKIM HEIAGRSMIG HALHAASALQ PQNLVAVVRH
     QRDLVAEHIL SQFPSITIAD QDEIPGTGRA VQQGLEVVDP ALEGTVVVTY GDVPLLTSEV
     LQDLVATHES NGNSVTVLTT ELDDPNGYGR ILRDDKGEVA GIREQKDASA DELLIKEINS
     GIYAFDAKIL RSALTEVTTE NAQGEMYLTD VLAIARERGG RVASSQIADR WQIEGANDRV
     QVSNLARIYN ERKTEFWMRQ GVTIVDPATT WIDADVMIGQ DATIKPGTQL HGETIIGANA
     TVGPDTTLTN VVVGQRATVK RTDATDSRIA EGASVGPFAY LRPGTDLGVD GKIGAFYETK
     NVTIGRGSKL SHLGYAGDAE IGEFTNIGCG NITANYDGEK KHRTKIGSHV RTSSNTVFVA
     PVEIGDGAYT GAGAIVRKNV PAGALALSVA PQRNSEGWTL EKRPGTSSAD AAFKSSLNSS
     ASE
//
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