ID   A0A2K2FDR2_9FIRM        Unreviewed;       820 AA.
AC   A0A2K2FDR2;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Nucleotidyltransferase {ECO:0000313|EMBL:PNT96894.1};
GN   ORFNames=CDQ84_14365 {ECO:0000313|EMBL:PNT96894.1};
OS   Pseudoclostridium thermosuccinogenes.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Pseudoclostridium.
OX   NCBI_TaxID=84032 {ECO:0000313|EMBL:PNT96894.1, ECO:0000313|Proteomes:UP000236151};
RN   [1] {ECO:0000313|EMBL:PNT96894.1, ECO:0000313|Proteomes:UP000236151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5806 {ECO:0000313|EMBL:PNT96894.1,
RC   ECO:0000313|Proteomes:UP000236151};
RA   Koendjbiharie J.G., van Kranenburg R.;
RT   "Investigating the central metabolism of Clostridium thermosuccinogenes.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC       {ECO:0000256|ARBA:ARBA00010231}.
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:PNT96894.1}.
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DR   EMBL; NIOJ01000043; PNT96894.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K2FDR2; -.
DR   KEGG; cthd:CDO33_07985; -.
DR   OrthoDB; 9803871at2; -.
DR   Proteomes; UP000236151; Unassembled WGS sequence.
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; cd05805; MPG1_transferase; 1.
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; 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   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR   SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 2.
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   Reference proteome {ECO:0000313|Proteomes:UP000236151};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PNT96894.1}.
FT   DOMAIN          2..232
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
FT   DOMAIN          382..512
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
SQ   SEQUENCE   820 AA;  91897 MW;  E6D829612A14AA16 CRC64;
     MKAVIMAGGE GTRLRPLTCS RPKPMVPVAN KPVMEHIIEL LKKHNLTEIA VTLQYMPDII
     KEYFNDGKEL GVDMRYYVEN TPLGTAGSVK NAEDFLDDTF IVISGDALTD IDLSEVIDFH
     NKKGSMATLV LKKVDIPLEY GVVVTDDDGR IVRFLEKPSW GEVFSDTANT GIYVLSPEVL
     SYFKKNEMFD FSKDLFPILL KENKPMYGFI ADGYWCDIGD LAAYRQANFD VLDGKVKVNI
     SGKQISKGIW VDEGAEIDET ATIEAPCIIG KNSKIKKNVH IGSYSVIGES NIVEDRAGLK
     RSIIWKNCIL ESNAQLRGSI LCNKVHFREN TSAYENAVIG DDTTVRENAV IKPNIKVWPN
     KLIDESVEVN SNLVWGSKFT RTIFGNRGVA GEINVDITPE YASKLGAAYG AVFKGKAKVG
     ISCDRSNSAN MLKISFISGL LSSGLEVYDL GNLLLPMTRS AVRFYKFDGG IHISTSSEDM
     ARLFVDFLDK NGSNIDRGLE RKIENVFIRE DFSRCEGDLI KRVEVIPDYS KYYLHSIINN
     VKSQKMNFRV ALFSNSDFIT NTMSTLLKEL GCEVGIIRQK LINTRTIKQS TLAADVRYFS
     NYIKTRKFDL GVSIEDNSEK MMLVDNKGRI VTEDMFIALV SLILLKMMNG GMVVVPVSAS
     QVVEKIAEQH NGKVLRAKTS LQDLMAKMLC SEVKEGMLEQ FTMHFDAMAG LVRILDFMAS
     NDCKLSDLVE MIPDFHINRK EVECPWNAKG KVIRQIMQEA GKDRVETLEG VKIHQDRGWV
     LVLPDAERPV CKVISESYSA EFAEELSDLY VNKVREISRS
//