ID   E8T248_THEA1            Unreviewed;       830 AA.
AC   E8T248;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Nucleotidyl transferase {ECO:0000313|EMBL:ADU96943.1};
GN   OrderedLocusNames=Theam_0976 {ECO:0000313|EMBL:ADU96943.1};
OS   Thermovibrio ammonificans (strain DSM 15698 / JCM 12110 / HB-1).
OC   Bacteria; Aquificota; Aquificae; Desulfurobacteriales;
OC   Desulfurobacteriaceae; Thermovibrio.
OX   NCBI_TaxID=648996 {ECO:0000313|EMBL:ADU96943.1, ECO:0000313|Proteomes:UP000006362};
RN   [1] {ECO:0000313|EMBL:ADU96943.1, ECO:0000313|Proteomes:UP000006362}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15698 / JCM 12110 / HB-1
RC   {ECO:0000313|Proteomes:UP000006362};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Vetriani C., Woyke T.;
RT   "Complete sequence of chromosome of Thermovibrio ammonificans HB-1.";
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC       {ECO:0000256|ARBA:ARBA00010231}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002444; ADU96943.1; -; Genomic_DNA.
DR   RefSeq; WP_013537729.1; NC_014926.1.
DR   AlphaFoldDB; E8T248; -.
DR   STRING; 648996.Theam_0976; -.
DR   KEGG; tam:Theam_0976; -.
DR   eggNOG; COG1109; Bacteria.
DR   eggNOG; COG1208; Bacteria.
DR   HOGENOM; CLU_017652_1_0_0; -.
DR   OrthoDB; 9801899at2; -.
DR   Proteomes; UP000006362; Chromosome.
DR   GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd04181; NTP_transferase; 1.
DR   Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 3.
DR   Gene3D; 3.30.310.50; Alpha-D-phosphohexomutase, C-terminal domain; 1.
DR   Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR   InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR   InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR   InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
DR   InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR   InterPro; IPR005835; NTP_transferase_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   PANTHER; PTHR22572:SF15; MANNOSE-1-PHOSPHATE GUANYLTRANSFERASE BETA; 1.
DR   PANTHER; PTHR22572; SUGAR-1-PHOSPHATE GUANYL TRANSFERASE; 1.
DR   Pfam; PF00483; NTP_transferase; 1.
DR   Pfam; PF02878; PGM_PMM_I; 1.
DR   Pfam; PF02879; PGM_PMM_II; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR   SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
DR   SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADU96943.1}.
FT   DOMAIN          2..233
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
FT   DOMAIN          385..515
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          534..632
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
SQ   SEQUENCE   830 AA;  93247 MW;  C89693ADD84488F6 CRC64;
     MKAVVMAGGF GTRIQPLTNS LPKPMLPVVN LPMMEHTMKK LVALGVEEFV ILLYYKPEVI
     KEYFGDGSRL GVKVNYVLPE ADYGTAGAVK KAQQFLNETF IVVSGDVITD FDFREIAGFH
     EFKKSPVTIT LTSVSNPLQF GIVITDKEGK ILKFLEKPGW GEVFSDTINT GIYIMEPEVL
     DFIPENVPFD FSKDLFPLLM EKGIELFGFK AQGYWKDVGN PDAYREVHRD ILQGKVKLQI
     PGKLVKHREG VLFLQGDAEI PKSVKIRGTV VVGKGVEVGE GTLLENTVIG PETEVGKRCQ
     LRECILWDRV KVGDDSKLRN TVICSFTELG SGVTALKGAI IAEKVKIEDN VQIAKDVVIW
     PEKFVESGSI VSSNLVWGER WKRSLFEGGR ISGRINVELS PELAAKLGAA FGSTLPEGSW
     VYTSRDYHRA SRMIKRAFVS GLLSTGVNVL DLRQFPHPAM RFLLENTKKV AGVHFEASVG
     SPGHTDILFF DENGLPIDTN REKAIERIFF RERFRRVGPS EVGLIKESSY AADRYQRAIE
     ESIDHKIKQP SYRVVADLMN GVYSALYPEL LAHFKVESVV LNSYFSEEKI THLPILKEKA
     LWSVPRIVKA TEADIGFIIY PNGERLKVIS DTGEFVPNYK LLLLFLLALD RAVEQQVKVL
     VPVSCPSVLD GKLKNVIVER GKLRGIKANL LRQFALVGDL NGRFIFPEFS LSPDAVYASI
     KLLELMSFSN ASVSELLSAI PPFFFKHVIV SCPSSKKAKL MRKISEEAME KRASFIDGVK
     IFFNGDWILL IPDQFTDNLH IFVQTEKEER GRELLNQFNR KIEKWIEEKE
//