ID V5YM27_CITFR Unreviewed; 456 AA.
AC V5YM27;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Uridyltransferase/glucosamine-1-phosphate acetyltransferase {ECO:0000313|EMBL:BAO18595.1};
DE Flags: Fragment;
GN Name=glmU {ECO:0000313|EMBL:BAO18595.1};
OS Citrobacter freundii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter; Citrobacter freundii complex.
OX NCBI_TaxID=546 {ECO:0000313|EMBL:BAO18595.1};
RN [1] {ECO:0000313|EMBL:BAO18595.1}
RP NUCLEOTIDE SEQUENCE.
RA Takeo M., Kimura K., Inoue T., Kato D., Negoro S., Tada S., Shanmugam M.,
RA Ike M.;
RT "Chitin/Chitosan-Like Bioflocculant Synthetic Pathway and Genes in
RT Citrobacter freundii.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
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};
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};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the transferase
CC hexapeptide repeat family. {ECO:0000256|ARBA:ARBA00007707}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the N-
CC acetylglucosamine-1-phosphate uridyltransferase family.
CC {ECO:0000256|ARBA:ARBA00007947}.
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DR EMBL; AB823570; BAO18595.1; -; Genomic_DNA.
DR AlphaFoldDB; V5YM27; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019134; F:glucosamine-1-phosphate N-acetyltransferase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IEA:InterPro.
DR GO; GO:0000902; P:cell morphogenesis; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:InterPro.
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; 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 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.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:BAO18595.1}.
FT DOMAIN 8..121
FT /note="MobA-like NTP transferase"
FT /evidence="ECO:0000259|Pfam:PF12804"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAO18595.1"
SQ SEQUENCE 456 AA; 49319 MW; 421AC49E5FF3543E CRC64;
MLNNAMSVVI LAAGKGTRMY SDLPKVLHTL AGKPMVQHVI DAANELGATH VHLVYGHGGD
LLKQTLKDGN LNWVLQAEQL GTGHAMQQAA PFFGDDEDIL MLYGDVPLIS TDTLRRLREA
KPQGGIGLLT VKLDDPTGYG RITRDNGNVT GIVEHKDATD EQRQIQEINT GILIANGADM
KRWLSKLTNN NVQGEYYITD IIAMAYKEGR EIAAVHPARI SETEGVNNRL QLSRLERVYQ
SEQAEKLLLA GVMLRDPARF DLRGTLIHGR DVEIDTNVII EGNVTVEDRV KIGAGCIIKN
SVIGEGCELS PYSVVEDAHL EAACTIGPFA RLRPGAELQE GAHVGNFVEM KKARLGKGSK
AGHLTYLGDA EIGDNVNIGA GTITCNYDGA NKFKTIIGDD VFVGSDTQLV APVTVGKGAT
IAAGTTVTRN VADNELVLSR VPQVHKQGWQ RPVKKK
//
