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
//