ID G0EHA7_PYRF1 Unreviewed; 461 AA.
AC G0EHA7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Nucleotidyl transferase {ECO:0000313|EMBL:AEM39331.1};
GN OrderedLocusNames=Pyrfu_1473 {ECO:0000313|EMBL:AEM39331.1};
OS Pyrolobus fumarii (strain DSM 11204 / 1A).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC Pyrolobus.
OX NCBI_TaxID=694429 {ECO:0000313|EMBL:AEM39331.1, ECO:0000313|Proteomes:UP000001037};
RN [1] {ECO:0000313|EMBL:AEM39331.1, ECO:0000313|Proteomes:UP000001037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11204 / 1A {ECO:0000313|Proteomes:UP000001037};
RX PubMed=21886865;
RA Anderson I., Goker M., Nolan M., Lucas S., Hammon N., Deshpande S.,
RA Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Huntemann M.,
RA Liolios K., Ivanova N., Pagani I., Mavromatis K., Ovchinikova G., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Brambilla E.M., Huber H.,
RA Yasawong M., Rohde M., Spring S., Abt B., Sikorski J., Wirth R.,
RA Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Complete genome sequence of the hyperthermophilic chemolithoautotroph
RT Pyrolobus fumarii type strain (1A).";
RL Stand. Genomic Sci. 4:381-392(2011).
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 -!- 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|ARBA:ARBA00005166}.
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|ARBA:ARBA00005208}.
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; CP002838; AEM39331.1; -; Genomic_DNA.
DR RefSeq; WP_014027008.1; NC_015931.1.
DR AlphaFoldDB; G0EHA7; -.
DR STRING; 694429.Pyrfu_1473; -.
DR GeneID; 11138660; -.
DR KEGG; pfm:Pyrfu_1473; -.
DR eggNOG; arCOG00666; Archaea.
DR HOGENOM; CLU_029499_0_1_2; -.
DR InParanoid; G0EHA7; -.
DR OrthoDB; 15372at2157; -.
DR UniPathway; UPA00113; UER00532.
DR Proteomes; UP000001037; Chromosome.
DR GO; GO:0019134; F:glucosamine-1-phosphate N-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR InterPro; IPR023915; Bifunctiontional_GlmU_arc-type.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR NCBIfam; TIGR03992; Arch_glmU; 1.
DR PANTHER; PTHR43584:SF3; BIFUNCTIONAL PROTEIN GLMU; 1.
DR PANTHER; PTHR43584; NUCLEOTIDYL TRANSFERASE; 1.
DR Pfam; PF00483; NTP_transferase; 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};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000001037};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AEM39331.1}.
FT DOMAIN 10..222
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 461 AA; 50235 MW; 44715DB74C9F215C CRC64;
MGGIALVDAA LVLAGGRGER AWPLTATIYK PLLQLPGNES ILSRLVRQVS RLAKRVYVLV
PPGATEEFKK HLDSYGFTNV VVVEQQPYEN GGYGSGAAVR QLLEVVPDID SVLIVHGDTV
IHDSVIDDLV KLAENREWGL VGFRTNRNGK RYGVIVADGS RVKRIVEKPG WSGEVVANAA
IYLLPARLVR EAVMNIGISE RGEIEFPDAV NLVAKRLEDE GKWLRLLLIR EEHRIDVGPW
WEYLLASRMV LDWLVESGCR AEGNIAYNVI VKGVVCGEGF EVEGPSVLEG PIWLGRNARV
GPFTHLRKYT ILYDDVQVGA FVEIKGSVLM ERTVARHHAY IGDSVVGPRS NIAAGTVFAN
LRHDNATVRS CAGGRVRNTG LRKLGAVLGE GVKTGVNSSI MPGARIGPCS WIEPGAVVRG
DVPSCSFYRR DGEIVDIREA VANCCRGVRG GRGYGLCTKP E
//
