ID A0A1H1KVW0_9ACTO Unreviewed; 349 AA.
AC A0A1H1KVW0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Bifunctional UDP-N-acetylglucosamine pyrophosphorylase / Glucosamine-1-phosphate N-acetyltransferase {ECO:0000313|EMBL:SDR66511.1};
GN ORFNames=SAMN04489715_0655 {ECO:0000313|EMBL:SDR66511.1};
OS Schaalia meyeri.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Schaalia.
OX NCBI_TaxID=52773 {ECO:0000313|EMBL:SDR66511.1, ECO:0000313|Proteomes:UP000181914};
RN [1] {ECO:0000313|Proteomes:UP000181914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20733 {ECO:0000313|Proteomes:UP000181914};
RA Varghese N.;
RL Submitted (OCT-2016) 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};
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DR EMBL; FNLK01000006; SDR66511.1; -; Genomic_DNA.
DR RefSeq; WP_050695136.1; NZ_FNLK01000006.1.
DR AlphaFoldDB; A0A1H1KVW0; -.
DR STRING; 52773.ADJ76_05530; -.
DR KEGG; amy:ADJ76_05530; -.
DR OrthoDB; 9775031at2; -.
DR Proteomes; UP000181914; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR CDD; cd02540; GT2_GlmU_N_bac; 1.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR InterPro; IPR025877; MobA-like_NTP_Trfase.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR PANTHER; PTHR43584:SF3; BIFUNCTIONAL PROTEIN GLMU; 1.
DR PANTHER; PTHR43584; NUCLEOTIDYL TRANSFERASE; 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 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SDR66511.1}.
FT DOMAIN 7..151
FT /note="MobA-like NTP transferase"
FT /evidence="ECO:0000259|Pfam:PF12804"
SQ SEQUENCE 349 AA; 36408 MW; C648C3162CBB1650 CRC64;
MSRPAAVIVL AAGQGTRMKS ALPKVVHPLA GLSMIGHALR AAQGLDPLNL VAVVRHQRDV
VAAEIERVSP RAIIADQDDI PGTGRAVQCG LEALDAAVTP ASGTIIVTYG DVPLLSSATL
ADLVDTHERD GHAVTVLTSR VEDPTGYGRI IRDESGTVTA IVEQRDATEA QARINEINAG
IYAFDAEFLR ASLATLGSNN DQGEVYLTDV LAAAAPAGRS AGALDLADHW QSAGANDRVQ
LAELGAELNR RICREHMRSG VTIVDPASTW IDVDARVGAD TTIYPGTSLR GQTVVGAACE
IGPNATLIDA EVGDRCVVPS AWVGKGCVAA DTMVKPYTTI GTLITARRA
//
