ID A0A101VFG7_9FIRM Unreviewed; 823 AA.
AC A0A101VFG7;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Nucleotidyl transferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=APF76_12340 {ECO:0000313|EMBL:KUO53590.1};
OS Desulfitibacter sp. BRH_c19.
OC Bacteria; Bacillota; Clostridia; Moorellales; Desulfitibacteraceae;
OC Desulfitibacter.
OX NCBI_TaxID=1734395 {ECO:0000313|EMBL:KUO53590.1, ECO:0000313|Proteomes:UP000053015};
RN [1] {ECO:0000313|EMBL:KUO53590.1, ECO:0000313|Proteomes:UP000053015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c19 {ECO:0000313|EMBL:KUO53590.1};
RA Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (OCT-2015) 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:KUO53590.1}.
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DR EMBL; LOER01000003; KUO53590.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101VFG7; -.
DR STRING; 1734395.APF76_12340; -.
DR Proteomes; UP000053015; Unassembled WGS sequence.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
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; IPR005845; A-D-PHexomutase_a/b/a-II.
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 Pfam; PF02879; PGM_PMM_II; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 2..232
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
FT DOMAIN 382..513
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 532..629
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
SQ SEQUENCE 823 AA; 91847 MW; F4D421975E56BBCB CRC64;
MKAIIMAGGE GSRLRPLTCD RPKPMVPVGN RPVMEYAIEL LKKLNITEIG VTLQYLPQHI
TDYFGDGKQW GVNLHYFIED VPLGTAGSVK NAGSFLDETF LVVSGDALTD LNLQEAIVFH
RQKKSLATIV LTAVTNPLEY GVVITNPDGS IERFLEKPGW GEVFSDWVNT GIYVLEPEAL
DYFEMGQKFD FSKDLFPLLL KNKESMFGCL LEGYWCDIGN LEQYLQSHKD ILAGKVDVNP
KGTLIKGTLN GEVAANKANS VRINGPVLIG DNCRLGAGVR LEPFTILGDN VIIEDEVTIK
RTVIWNNVYI GKKTSLSGAL IGNRVTIKDN VTILQDAAIG DGTNINSRST IKPGVKIWPF
KTVNTGAIVS ESLVWGEKAN RNLFGIEGIP GLTNWDITPE LAAKLGASYG SVLKKEHQVA
VSCDGKLVTK MLKGSFVSGL MSTGVKVSDL GDLTMPIHRF AVRGIGAQGG VHIKIDHNSL
DKCWLQFVDC KGININRDVE RKIEGTYIRE DFRRVQEGEI GETVLMQHSI SSYLDNLMNS
IDFDKIGQRD LKLLVNTRGA VMKNLFQELS SRLKCDFQYV NNDHLEDKSF KKQILMSDEM
SKEITDTGMD FGIILDANGE RIILIDNHGR RIDEHLFTVL MALVLFKANK GGTVVVPVTA
SETIEKIGEE YNGKVIRTKT APWAVMSELL REEIAKLQKP YSQFFMQNDS LYAAVMLMDF
IVKENISLAD LINEIPDFHL EVKTANCPWE QKGRIMRALI SEVTEYPVEL IDGVKIRHEK
GWALVLPHCE EPQYNIYTEG LSQEIAEELG VFYQDKIQRM LQT
//
