ID A0A0J0UT21_9ACTN Unreviewed; 857 AA.
AC A0A0J0UT21;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Nucleoside-diphosphate-sugar pyrophosphorylase family protein {ECO:0000313|EMBL:KLR60025.1};
DE EC=2.7.7.13 {ECO:0000313|EMBL:KLR60025.1};
DE EC=5.4.2.8 {ECO:0000313|EMBL:KLR60025.1};
GN ORFNames=IMCC26207_110269 {ECO:0000313|EMBL:KLR60025.1};
OS Actinobacteria bacterium IMCC26207.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1641811 {ECO:0000313|EMBL:KLR60025.1, ECO:0000313|Proteomes:UP000036180};
RN [1] {ECO:0000313|EMBL:KLR60025.1, ECO:0000313|Proteomes:UP000036180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC26207 {ECO:0000313|EMBL:KLR60025.1,
RC ECO:0000313|Proteomes:UP000036180};
RA Kim S., Cho J.-C.;
RT "Genome sequence of freshwater Actinobacteria.";
RL Submitted (MAY-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:KLR60025.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LCZK01000010; KLR60025.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J0UT21; -.
DR STRING; 1641811.IMCC26207_110269; -.
DR PATRIC; fig|1641811.3.peg.2583; -.
DR Proteomes; UP000036180; Unassembled WGS sequence.
DR GO; GO:0004475; F:mannose-1-phosphate guanylyltransferase (GTP) activity; IEA:UniProtKB-EC.
DR GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
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; IPR005845; A-D-PHexomutase_a/b/a-II.
DR InterPro; IPR005846; A-D-PHexomutase_a/b/a-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 Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 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 Isomerase {ECO:0000313|EMBL:KLR60025.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000313|EMBL:KLR60025.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000036180};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KLR60025.1}.
FT DOMAIN 31..261
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
FT DOMAIN 411..542
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 561..659
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 665..769
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 857 AA; 92612 MW; DAB399ED5C74CF3E CRC64;
MTDLPRRHRQ LSPDEDDLSP ANSSKDVPIV KAVIMAGGEG TRLRPLTSNA PKPMLPLVNR
PMMEHIIDLL KAHGINEIVV TVAFMPNAIR NHFGDGSEFG VKMTYASEEH PLGTAGSVRN
AMTELTETFL VISGDVLTDI DLSALVQSHV DRQALATIGL VRVEDPLEYG IVISNEDGSI
ERFLEKPTWG QVFSDTINSG IYVLEPEIFD WIAADVPVDF SSDVFPALLE AGKPVFGSVA
EGYWEDVGTL SAYLRAHKDI LDAKVSVRIP GFEVSTGVFI GEGVEINHGV VINGPAVIGD
NCFLESGAEL GEYSVLGDGV RMRRDGHIER SVIHENAYIG ESVMIRGTLV GRASDLRRGV
RCEEGVVLGD EVFVGENAVL SSEIKVYPFK TVEAGAVVNS SVIWESRGAR SLFGNGGVTG
LANVDMTPEL AAKVALAFAT SLKKDATVVV SRDSSRAARM LKRAMIAGLN AGGVNVLDLE
TASVPLTRFH CRATLVSGAI TLRLSADDPD SVIIRFFDRG GSDILEEQQR KIERLFTRED
FRRVRPADIG DIDLVPRSLE QYALALEQTI DVKAVAARRF KVVIDYSYGS TSFVMPNVLA
KLGAEVLVVN PFASTKGTLG FDRDEHAAQV AALVKASGAD LGALIDPSGE QLLLVDDHGT
VLSFDQLLFV FLDLVCDNLL GDTVALPVTV SRAAAEIVES RGYKVLWTKT SAAALMEEAD
SPAVGFAANL EGGIILPGFL PAFDAAAGLL KMLDLLAGRD VKLSELVAHA PSVHLLHEQV
ITPWEQKGTV MRTLVEQTHG REVDLIDGIK VHHDSGWVLV LPDPEEPITH IWAEGDTAGD
ARTLSQEYAR RIRQMLK
//
