ID D7DAB1_STAHD Unreviewed; 429 AA.
AC D7DAB1;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Nucleotidyl transferase {ECO:0000313|EMBL:ADI32707.1};
GN OrderedLocusNames=Shell_1620 {ECO:0000313|EMBL:ADI32707.1};
OS Staphylothermus hellenicus (strain DSM 12710 / JCM 10830 / BK20S6-10-b1 /
OS P8).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Staphylothermus.
OX NCBI_TaxID=591019 {ECO:0000313|EMBL:ADI32707.1, ECO:0000313|Proteomes:UP000002573};
RN [1] {ECO:0000313|Proteomes:UP000002573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12710 / JCM 10830 / BK20S6-10-b1 / P8
RC {ECO:0000313|Proteomes:UP000002573};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Mikhailova N., Anderson I.J., Woyke T.;
RT "Complete sequence of Staphylothermus hellenicus DSM 12710.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADI32707.1, ECO:0000313|Proteomes:UP000002573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12710 / JCM 10830 / BK20S6-10-b1 / P8
RC {ECO:0000313|Proteomes:UP000002573};
RX PubMed=22180806; DOI=10.4056/sigs.2054696;
RA Anderson I., Wirth R., Lucas S., Copeland A., Lapidus A., Cheng J.F.,
RA Goodwin L., Pitluck S., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Pati A., Mikhailova N., Woyke T., Klenk H.P.,
RA Kyrpides N., Ivanova N.;
RT "Complete genome sequence of Staphylothermus hellenicus P8.";
RL Stand. Genomic Sci. 5:12-20(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; CP002051; ADI32707.1; -; Genomic_DNA.
DR RefSeq; WP_013143904.1; NC_014205.1.
DR AlphaFoldDB; D7DAB1; -.
DR STRING; 591019.Shell_1620; -.
DR GeneID; 9234913; -.
DR KEGG; shc:Shell_1620; -.
DR eggNOG; arCOG00666; Archaea.
DR HOGENOM; CLU_029499_0_1_2; -.
DR OrthoDB; 15372at2157; -.
DR UniPathway; UPA00113; UER00532.
DR Proteomes; UP000002573; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADI32707.1}.
FT DOMAIN 2..233
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 429 AA; 47782 MW; 423DE20977D4108B CRC64;
MKAIILAAGK GLRLRPITET RPKPLIPILC KPLLQWQLEA LAGIDEIDEV IIVVSYLKEK
VEQFIRKVNV PFKITLLDQG EELGTGDAVL KAIRKKGIDE KTLIIYGDIF LKDWNKLKQL
FLTRKNSIVG VEVDNPSDYG VIIVDENNSF KGIIEKPAIP PSSLINAGIY FLDARDILKH
SDIEPSPRGE LEFTDILTSM ARNGIEIKVY QLNKGEWIDI GKPWHLLDAN RMALENISTK
IMGSIEPGAH VHGRVFVGED TIIKSGTYID GPVYIGKNTV IGPNAYLRPY SVICDGSKIG
FSVEVKSSLI MENVHISHLS YVGDSIICEH VNFGAGTITA NLRFDDKPVK MYIRGKKESS
GRRKLGAIIG AYVKTGINVS FMPGVKIGSH SWIAPGAIVY KDIPPRSFYR WMGIGYIENL
KENQKIRDK
//
