ID A0A124FPP2_9FIRM Unreviewed; 828 AA.
AC A0A124FPP2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Mannose-1-phosphate guanylyltransferase {ECO:0000313|EMBL:KUK53437.1};
GN ORFNames=XD78_1216 {ECO:0000313|EMBL:KUK53437.1};
OS Desulfotomaculum sp. 46_296.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC Desulfotomaculum.
OX NCBI_TaxID=1635262 {ECO:0000313|EMBL:KUK53437.1, ECO:0000313|Proteomes:UP000053813};
RN [1] {ECO:0000313|Proteomes:UP000053813}
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:KUK53437.1}.
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DR EMBL; LGFZ01000031; KUK53437.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A124FPP2; -.
DR STRING; 1635262.XD78_1216; -.
DR PATRIC; fig|1635262.3.peg.1992; -.
DR Proteomes; UP000053813; 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; 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; 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:KUK53437.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KUK53437.1}.
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 828 AA; 90823 MW; 78DB0F5F138BDEE6 CRC64;
MKTIIMAGGE GSRLRPITCG RPKPMAPVAN RPIMLHIVEL LKKHGLYNIG VTLQYKPEFI
RSYFGNGSEQ GVNLQYFIEE IPLGTAGSVK NARAFLDETF LVISGDALTD LDLSEAVAFH
RKRGAIATLV LTRVGCPLEY GVVITKQDGI IIRFLEKPAW GEVFSDTVNT GIYILEPEVL
DYIPDDRSFD FSQDLFPLLL RDKKPLFGVV LPGYWCDIGN IQQYVQAHHD VLAGKVNTSI
SAREVSPGIW LGEGVDLHAE CDLEGPILIG NGCCIGAKAK ISPYTTIGAG CLIQEKASVK
QSVLWNNVYL GPGTAIRGAV LCSRVQARSN SEVYEGAVIG SDSILQERSI VRPEVKIWPN
KQAEAGSIVN NSLIWGACWS RKLFGLEGVT GMFNIEVTAE LACRLGAAFC TVLGGESRVA
ISADNYPPAQ MLKEALASGM QSTGANVYDL GTVITPLHRF AVTNLTLAGG VHVKVSQRNP
EHVSILFFNA KGGNISRGIE RKIENILFRD DFPRVDMTHV RFRKHVREIS DLYVQELTKG
IDVDLIKKSC LNLILAYDQN NLQKYITPLG KSLNITFKNV NLSGPAGGLL SWEKCIEKLP
VISSMVCDEG AWGGVMIDPD ADHLVLVDER GRLIQDNMLV VLVALIILKS QRGPVFVPVT
APRVVENLAM QYNSKVIRTK TAVQDLTEKV LGQDQVGINY SSGLSQFLLN FDALGAFLGI
INFTVQQGLS LGELVDEIPS FFVSKKEISV PWEAKGRVLR VLTNTDQETQ LLDGVKVFHD
DGWALVLPDP EEPVCRVFSE GASMEIAESL ADMYVKKINE IVNRHPCC
//
