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Database: UniProt
Entry: A0A101GT27_9FIRM
LinkDB: A0A101GT27_9FIRM
Original site: A0A101GT27_9FIRM 
ID   A0A101GT27_9FIRM        Unreviewed;       824 AA.
AC   A0A101GT27;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Mannose-1-phosphate guanylyltransferase {ECO:0000313|EMBL:KUK64126.1};
GN   ORFNames=XD84_1727 {ECO:0000313|EMBL:KUK64126.1};
OS   Desulfotomaculum sp. 46_80.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC   Desulfotomaculum.
OX   NCBI_TaxID=1641375 {ECO:0000313|EMBL:KUK64126.1, ECO:0000313|Proteomes:UP000053828};
RN   [1] {ECO:0000313|Proteomes:UP000053828}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA   Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA   Andersen G.L., Banfield J.F.;
RT   "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT   Other Microbial Community Members in Biogeochemical Transformations in Oil
RT   Reservoirs.";
RL   MBio 7:e01669-15(2015).
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:KUK64126.1}.
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DR   EMBL; LGGF01000041; KUK64126.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101GT27; -.
DR   PATRIC; fig|1641375.3.peg.2169; -.
DR   Proteomes; UP000053828; Unassembled WGS sequence.
DR   GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0016779; F:nucleotidyltransferase 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; IPR036900; A-D-PHexomutase_C_sf.
DR   InterPro; IPR001451; Hexapep.
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; PF00132; Hexapep; 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; 1.
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   Nucleotidyltransferase {ECO:0000313|EMBL:KUK64126.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KUK64126.1}.
FT   DOMAIN          2..232
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
FT   DOMAIN          381..512
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
SQ   SEQUENCE   824 AA;  90380 MW;  E9B74BD3D92EB950 CRC64;
     MKTIIMAGGE GSRLRPITCG RPKPMAPVVN RPVMFHIVEL LKKHGFYNIG VTLQYKPEFI
     RSFFGNGSEQ GVSMQYFIEE VPLGTAGSVK NAQTFLDETF LVISGDALTD LDLSAAVDFH
     RKRGAIATLV LTRVGCPLEY GVVITKQDGT ITRFLEKPAW GEVFSDTVNT GIYILEPEVL
     DYIPDNRSFD FSQDLFPALL RDKKPLFGVV SPGYWCDIGN IQQYIQAHYD VLAGKVNTGI
     SARQVKPGIW IGEGVDLHAE CHLEGPILIG NGCCIGAGVK ISPYTTIGDG CLIQENASLK
     QSVLWNNVYL GPGTALRGAV LCSRVQVRSN SEVYEGAVVG SDSVLQERSI VRPEVKIWPN
     KQTEAGSIVN NSLIWGACWS RKLFGLEGVT GMFNIEVTAE LACRLGAAFC TVLGAESRVA
     VSADNYPPAQ MLKEALASGM QSTGAVVYDL GTVITPLHRF AVSNLGLAGG VHIKISQRNP
     EHVSILFFNA KGGNISRGIE RKIENILFRD DFPRVDMAHV RLRRYVRKIT DLYLQELLKG
     VDVELIRKSG LTLILACDQN NLQKYITALG KSLNLTFKNL NLSGTDGAML SWEKCIEKLP
     AVSSMVCNER AWAGVLIDPD ADHLVLVDER GRLIQDNMLV VLTALIILKS QRGPVFVPVT
     APQVVENLAM QYNGRVIRTK TAVQDLIEKV LGQDQGCIEY SGLSQFLLNF DALGALLGIL
     GFAVQQGFSL GELIDEIPSF FVSKKEISVP WEAKGRVIRV LTETEQEMQL LDGVKVFHND
     GWALVLPDPE EPVCRVFSEG ASMEIAESLA DLYIKKISEI IDKS
//
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