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Entry: A0A135VQ91_9ARCH
LinkDB: A0A135VQ91_9ARCH
Original site: A0A135VQ91_9ARCH 
ID   A0A135VQ91_9ARCH        Unreviewed;       425 AA.
AC   A0A135VQ91;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Nucleotidyl transferase domain-containing protein {ECO:0000259|Pfam:PF00483};
GN   ORFNames=AM326_09450 {ECO:0000313|EMBL:KXH74867.1};
OS   Candidatus Thorarchaeota archaeon SMTZ-45.
OC   Archaea; Asgard group; Candidatus Thorarchaeota.
OX   NCBI_TaxID=1706443 {ECO:0000313|EMBL:KXH74867.1, ECO:0000313|Proteomes:UP000070599};
RN   [1] {ECO:0000313|EMBL:KXH74867.1, ECO:0000313|Proteomes:UP000070599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMTZ-45 {ECO:0000313|EMBL:KXH74867.1};
RX   PubMed=26824177;
RA   Seitz K.W., Lazar C.S., Hinrichs K.U., Teske A.P., Baker B.J.;
RT   "Genomic reconstruction of a novel, deeply branched sediment archaeal
RT   phylum with pathways for acetogenesis and sulfur reduction.";
RL   ISME J. 0:0-0(2016).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXH74867.1}.
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DR   EMBL; LRSM01000096; KXH74867.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135VQ91; -.
DR   UniPathway; UPA00113; UER00532.
DR   Proteomes; UP000070599; Unassembled WGS sequence.
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   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   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          3..235
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
SQ   SEQUENCE   425 AA;  46516 MW;  E495D9DC6521227D CRC64;
     MKKAVILAAG DSTRLLPLSA NQPKHVLPIA GKPLIFHTLE ALEKAGIRET LVVYGYQASK
     LREAVETRAW KMKISFVNQK ERKGTAHAAG YAKKFVGKSN AILMYGDVMV GPNTFEGLIE
     RHKKRKFDLT LSVKPIENPS AYGVVKVQRG KAKALIEKPE PEQMVSDLVN AGIYAISYPI
     WEAIEKTELS PRGEYEITDS ISMLIEKGNV GAYSLPSWWL DIGKPWDLLE ANRLCLEQLE
     RRVEGTVEDG ATVKGKVIVE EGTLMKSGAY IEGPVFIDGE SVIGPNCYIR PHTSLGKRVK
     IGNAVEIKNS IIMNDTNVGH LSYVGDSIIG QRSNFGAGTI TANLRHDNET IFATVKGERI
     NSGRRKLGAI IGDDVKTGIG TSISPGVVLH QGSQTGVGVI VKRDIAPYKL VTVKQDQSIM
     DVERR
//
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