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Database: UniProt
Entry: D3TC06_ACIB4
LinkDB: D3TC06_ACIB4
Original site: D3TC06_ACIB4 
ID   D3TC06_ACIB4            Unreviewed;       400 AA.
AC   D3TC06;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=Nucleotidyl transferase {ECO:0000313|EMBL:ADD08091.1};
GN   OrderedLocusNames=Aboo_0280 {ECO:0000313|EMBL:ADD08091.1};
OS   Aciduliprofundum boonei (strain DSM 19572 / T469).
OC   Archaea; Candidatus Thermoplasmatota; DHVE2 group; Aciduliprofundum.
OX   NCBI_TaxID=439481 {ECO:0000313|EMBL:ADD08091.1, ECO:0000313|Proteomes:UP000001400};
RN   [1] {ECO:0000313|Proteomes:UP000001400}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19572 / T469 {ECO:0000313|Proteomes:UP000001400};
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Saunders E., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Flores G., Reysenbach A.-L., Woyke T.;
RT   "Complete sequence of Aciduliprofundum boonei T469.";
RL   Submitted (FEB-2010) 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   -!- 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; CP001941; ADD08091.1; -; Genomic_DNA.
DR   RefSeq; WP_012997090.1; NC_013926.1.
DR   AlphaFoldDB; D3TC06; -.
DR   GeneID; 8827222; -.
DR   KEGG; abi:Aboo_0280; -.
DR   HOGENOM; CLU_029499_0_1_2; -.
DR   OrthoDB; 15372at2157; -.
DR   UniPathway; UPA00113; UER00532.
DR   Proteomes; UP000001400; 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   CDD; cd05636; LbH_G1P_TT_C_like; 1.
DR   CDD; cd04181; NTP_transferase; 1.
DR   Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR   InterPro; IPR023915; Bifunctiontional_GlmU_arc-type.
DR   InterPro; IPR001451; Hexapep.
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; PF00132; Hexapep; 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:UP000001400};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADD08091.1}.
FT   DOMAIN          3..225
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
SQ   SEQUENCE   400 AA;  44164 MW;  9C2E579C28F31634 CRC64;
     MRAFILAAGE GTRMWPLTDT RPKPLIPLAN KPIIEHILDA LVEAGIEKIS ILIGYEGRQI
     AERYGYSYKG AKIDYVYQNE RRGTGDAVLY ASKYNDEKFL ILNGDLYFEK SAISDILGHD
     NAVLGVYKDN AESYGLLIGD ENLEEIREKV PSSSGLVNAG VYVFHREIFE YIKRVELSPR
     GEIEFTDAIN MFVKEHDVKI VKYNGLWLDI GYPWHLLDAT KAYLEKMKCE IGGEVEENVV
     LKGKVCIGEG TKIMSGTYIE GPVLIGKNCK IGPNAYIRPY TVIGDDCHIG NSSEVKASII
     MNGSKVPHFN YVGDSVIGEN CNLGAGTKVA NLRLDEKNIR VVVKDKIVDT GRRKLGVIMG
     DYVHTGINVS IDVGTMIGSY AAIAPGAKIK GIVSTRSRVF
//
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