ID   A0A0H3H5X9_KLEOK        Unreviewed;       456 AA.
AC   A0A0H3H5X9;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   22-APR-2020, entry version 33.
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 3318 /
OS   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.
RN   [2] {ECO:0000313|EMBL:AEX03067.1, 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};
RX   PubMed=22493189; DOI=10.1128/JB.00026-12;
RA   Shin S.H., Kim S., Kim J.Y., Lee S., Um Y., Oh M.K., Kim Y.R., Lee J.,
RA   Yang K.S.;
RT   "Complete genome sequence of Klebsiella oxytoca KCTC 1686, used in
RT   production of 2,3-butanediol.";
RL   J. Bacteriol. 194:2371-2372(2012).
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, ECO:0000256|SAAS:SAAS00381483}.
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|HAMAP-Rule:MF_01631,
CC         ECO:0000256|SAAS:SAAS01124206};
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|HAMAP-Rule:MF_01631,
CC         ECO:0000256|SAAS:SAAS01124218};
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, ECO:0000256|SAAS:SAAS00083707}.
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, ECO:0000256|SAAS:SAAS00083565}.
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, ECO:0000256|SAAS:SAAS00083673}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_01631,
CC       ECO:0000256|SAAS:SAAS00569615}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01631,
CC       ECO:0000256|SAAS:SAAS00083712}.
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:SAAS00569628}.
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:SAAS00569629}.
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DR   EMBL; CP003218; AEX03067.1; -; Genomic_DNA.
DR   RefSeq; WP_014227347.1; NC_016612.1.
DR   EnsemblBacteria; AEX03067; AEX03067; KOX_06685.
DR   KEGG; kox:KOX_06685; -.
DR   PATRIC; fig|1006551.4.peg.1339; -.
DR   HOGENOM; CLU_029499_15_2_6; -.
DR   KO; K04042; -.
DR   OMA; QNAQKEY; -.
DR   BioCyc; KOXY1006551:G1H2C-1375-MONOMER; -.
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:SAAS00458646, ECO:0000313|EMBL:AEX03067.1};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00083584};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00458644};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00458650};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00458735};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00458606};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00083642};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00458661};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00458685};
KW   Repeat {ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00458660};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01631,
KW   ECO:0000256|SAAS:SAAS00458747, ECO:0000313|EMBL:AEX03067.1}.
FT   DOMAIN          8..123
FT                   /note="NTP_transf_3"
FT                   /evidence="ECO:0000259|Pfam:PF12804"
FT   REGION          1..229
FT                   /note="Pyrophosphorylase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   REGION          11..14
FT                   /note="UDP-GlcNAc binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   REGION          81..82
FT                   /note="UDP-GlcNAc binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   REGION          103..105
FT                   /note="UDP-GlcNAc binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   REGION          230..250
FT                   /note="Linker"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   REGION          251..456
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   REGION          386..387
FT                   /note="Acetyl-CoA binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   ACT_SITE        363
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   METAL           105
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   METAL           227
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         25
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         76
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         140
FT                   /note="UDP-GlcNAc; via amide nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         154
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         169
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         227
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         333
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         351
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         366
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         377
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         380
FT                   /note="Acetyl-CoA; via amide nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         405
FT                   /note="Acetyl-CoA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         423
FT                   /note="Acetyl-CoA; via amide nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01631"
FT   BINDING         440
FT                   /note="Acetyl-CoA"
FT                   /evidence="ECO:0000256|HAMAP-Rule: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
//