ID   A0A0H3H5X9_KLEOK        Unreviewed;       456 AA.
AC   A0A0H3H5X9;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   28-MAR-2018, entry version 22.
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:AEX03067.1};
GN   OrderedLocusNames=KOX_06685 {ECO:0000313|EMBL:AEX03067.1};
OS   Klebsiella oxytoca (strain ATCC 8724 / DSM 4798 / JCM 20051 / NBRC
OS   3318 / NRRL B-199 / KCTC 1686).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella.
OX   NCBI_TaxID=1006551 {ECO:0000313|EMBL:AEX03067.1, ECO:0000313|Proteomes:UP000007843};
RN   [1] {ECO:0000313|Proteomes:UP000007843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8724 / DSM 4798 / JCM 20051 / NBRC 3318 / NRRL B-199 /
RC   KCTC 1686 {ECO:0000313|Proteomes:UP000007843};
RA   Shin S.H., Kim S., Kim J.Y., Yang K.-S., Seo J.-S.;
RT   "Complete genome sequence of Klebsiella oxytoca strain KCTC 1686.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the last two sequential reactions in the de
CC       novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-
CC       GlcNAc). The C-terminal domain catalyzes the transfer of acetyl
CC       group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P)
CC       to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is
CC       converted into UDP-GlcNAc by the transfer of uridine 5-
CC       monophosphate (from uridine 5-triphosphate), a reaction catalyzed
CC       by the N-terminal domain. {ECO:0000256|HAMAP-Rule:MF_01631,
CC       ECO:0000256|SAAS:SAAS00650355}.
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + alpha-D-glucosamine 1-phosphate =
CC       CoA + N-acetyl-alpha-D-glucosamine 1-phosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00650344}.
CC   -!- CATALYTIC ACTIVITY: UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
CC       = diphosphate + UDP-N-acetyl-alpha-D-glucosamine.
CC       {ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00650293}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01631};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01631};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A
CC       biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01631,
CC       ECO:0000256|SAAS:SAAS00650347}.
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
CC       glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate
CC       from alpha-D-glucosamine 6-phosphate (route II): step 2/2.
CC       {ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00650354}.
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.
CC       {ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00650342}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_01631,
CC       ECO:0000256|SAAS:SAAS00650301}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01631,
CC       ECO:0000256|SAAS:SAAS00650327}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the transferase
CC       hexapeptide repeat family. {ECO:0000256|HAMAP-Rule:MF_01631,
CC       ECO:0000256|SAAS:SAAS00650305}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the N-
CC       acetylglucosamine-1-phosphate uridyltransferase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00650312}.
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DR   EMBL; CP003218; AEX03067.1; -; Genomic_DNA.
DR   RefSeq; WP_014227347.1; NC_016612.1.
DR   STRING; 1006551.KOX_06685; -.
DR   EnsemblBacteria; AEX03067; AEX03067; KOX_06685.
DR   KEGG; kox:KOX_06685; -.
DR   PATRIC; fig|1006551.4.peg.1339; -.
DR   KO; K04042; -.
DR   OMA; IEPQTHL; -.
DR   UniPathway; UPA00113; UER00532.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000007843; 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:0009103; P:lipopolysaccharide biosynthetic process; IEA:InterPro.
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; 4.
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   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00650319, ECO:0000313|EMBL:AEX03067.1};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00650332};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00650295};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007843};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00650352};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00650323};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00650321};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00650297};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00650324};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00650358};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007843};
KW   Repeat {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00650299};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00650328, ECO:0000313|EMBL:AEX03067.1}.
FT   DOMAIN        8    123       NTP_transf_3. {ECO:0000259|Pfam:PF12804}.
FT   REGION        1    229       Pyrophosphorylase. {ECO:0000256|HAMAP-
FT                                Rule:MF_01631}.
FT   REGION       11     14       UDP-GlcNAc binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01631}.
FT   REGION       81     82       UDP-GlcNAc binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01631}.
FT   REGION      103    105       UDP-GlcNAc binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01631}.
FT   REGION      230    250       Linker. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   REGION      251    456       N-acetyltransferase. {ECO:0000256|HAMAP-
FT                                Rule:MF_01631}.
FT   REGION      386    387       Acetyl-CoA binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01631}.
FT   ACT_SITE    363    363       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   METAL       105    105       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   METAL       227    227       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING      25     25       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING      76     76       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING     140    140       UDP-GlcNAc; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01631}.
FT   BINDING     154    154       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING     169    169       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING     227    227       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING     333    333       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING     351    351       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING     366    366       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING     377    377       UDP-GlcNAc. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING     380    380       Acetyl-CoA; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01631}.
FT   BINDING     405    405       Acetyl-CoA. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
FT   BINDING     423    423       Acetyl-CoA; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01631}.
FT   BINDING     440    440       Acetyl-CoA. {ECO:0000256|HAMAP-Rule:
FT                                MF_01631}.
SQ   SEQUENCE   456 AA;  49359 MW;  4DB13E6473D38D34 CRC64;
     MSNSPMSVVI LAAGKGTRMY SDLPKVLHSL AGKPMVQHVI DAAKELGASA VHLVYGHGGD
     LLRQTLHEDN LNWVLQAEQL GTGHAMQQAA PFFSDDEDIL MLYGDVPLIS VETLKRLREA
     KPQGGIGLLT VKLDDPTGYG RITRDNGAVT GIVEHKDASD EQRRIQEINT GILVANGADL
     KRWLAKLTNN NVQGEYYITD IIAMAYEEGR EIAAVHPQRL SEVEGVNNRL QLSRLERVWQ
     SEKAEELLLA GVMLRDPARF DLRGVLKHGR DVEIDTNVIF EGDVVLGDRV KIGTGCVIKN
     STIGDDCEIS PYTVVEDAHL EAACTIGPFA RLRPGAELLE GAHVGNFVEI KKARLGKGTK
     AGHLSYLGDA EIGDNVNIGA GTITCNYDGA NKHKTVIGDD VFVGSDSQLV APVTVGKGVT
     IAAGTTVTRN VADNELVLSR VPQVHKQGWQ RPVKKK
//