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Database: UniProt
Entry: A0A369BDZ2_9FIRM
LinkDB: A0A369BDZ2_9FIRM
Original site: A0A369BDZ2_9FIRM 
ID   A0A369BDZ2_9FIRM        Unreviewed;       855 AA.
AC   A0A369BDZ2;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Nucleotidyltransferase {ECO:0000313|EMBL:RCX18806.1};
GN   ORFNames=DFR58_10475 {ECO:0000313|EMBL:RCX18806.1};
OS   Anaerobacterium chartisolvens.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Anaerobacterium.
OX   NCBI_TaxID=1297424 {ECO:0000313|EMBL:RCX18806.1, ECO:0000313|Proteomes:UP000253034};
RN   [1] {ECO:0000313|EMBL:RCX18806.1, ECO:0000313|Proteomes:UP000253034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27016 {ECO:0000313|EMBL:RCX18806.1,
RC   ECO:0000313|Proteomes:UP000253034};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (JUL-2018) 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:RCX18806.1}.
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DR   EMBL; QPJT01000004; RCX18806.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A369BDZ2; -.
DR   Proteomes; UP000253034; 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; 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; 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:UP000253034};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RCX18806.1}.
FT   DOMAIN          43..271
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
FT   DOMAIN          423..554
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
SQ   SEQUENCE   855 AA;  95484 MW;  729F783F7431B4E7 CRC64;
     MEYNYYILLL THGLLYFLQF KALKQSICST GLKYQRKGDD LMKAIIMAGG EGSRLRPLTC
     DLPKPMVPVM NRPIMQHIIE LLKSYGIIDI GVTLMYLPDK IKNYFGNGSS LGVNLHYFIE
     DFPLGTAGSV KNAQHFLDET FIVISGDSLT DLDLLKALEY HNRKYSKATL VLSKVERPLE
     YGVVLTDEDD AVIGFLEKPS WGEVFSDTIN TGTYILEPEV LDYFEKGKKF DFSQELFPLL
     LENKIPMYGY ISYGYWCDIG DPTSYLQAHY DAFEGKIKLP FEGEEIKKGV WAGSGTVIEP
     NAELNGPCLI GSNCHIGNGT VIDNFSVIGS GNIIEDEVSI KRGVLWDNTS IQFGSEIRGA
     ILCNKVTLKH YVSVFENSII GDRCIINERA IIKPNIKIWP QKTIDPLAIV DRNVIWSSRQ
     SRTIFGENGL SGIINVDISP EFATRLGAAY GSIFKKGSKV VVSSTNSNSA RMFKHAFVSG
     ILSIGVEVFN LSSLLTPISR HAINFLSVEG GIHIKVSDDN PNKLRVDFMD SKGGSISRGT
     ERKIENAYFR EDFKRCSGEE ISRLNNITDF KDYYIRSILN QTDVHKIMDI SPKICVISPS
     DFVISIVLSM LADSGCKVVS FSSCNPEAVD LIIYEINKTN ADFAAFIDSN GETLILIDKN
     GNIIKDDLFL SLSSLIAFKS SPNISVVVPV TAPSVIESLA SKYGGRVVRT KTSSQAVMEQ
     ILSRNPYKSR EDMGQFLLNF DALAGLVKII EYLCINNITL TEAINEIPSF YMSKRNIFCP
     WELKGKVMRT LITDKNNERI ELIDGVKFIM DNGWALVLPD ADMPLCRVYS EGKSPEIAET
     ISEYYLEKIN HIVNE
//
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