ID V6JSS3_9ACTN Unreviewed; 831 AA.
AC V6JSS3;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Mannose-1-phosphate guanyltransferase {ECO:0000313|EMBL:EST22892.1};
GN ORFNames=N566_26215 {ECO:0000313|EMBL:EST22892.1};
OS Streptomycetaceae bacterium MP113-05.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae.
OX NCBI_TaxID=1380770 {ECO:0000313|EMBL:EST22892.1, ECO:0000313|Proteomes:UP000017915};
RN [1] {ECO:0000313|EMBL:EST22892.1, ECO:0000313|Proteomes:UP000017915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP113-05 {ECO:0000313|EMBL:EST22892.1,
RC ECO:0000313|Proteomes:UP000017915};
RA Valde M., Degnes K.F., Sletta H., Ruckert C., Kalinowski J., Zotchev S.B.;
RT "Streptomyces bacterium from a marine sponge: physiological
RT characterization and genome-based analysis of secondary metabolite
RT biosynthesis potential.";
RL Submitted (SEP-2013) 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:EST22892.1}.
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DR EMBL; AWQV01000854; EST22892.1; -; Genomic_DNA.
DR AlphaFoldDB; V6JSS3; -.
DR STRING; 1380770.N566_26215; -.
DR PATRIC; fig|1380770.3.peg.4571; -.
DR HOGENOM; CLU_017652_1_0_11; -.
DR OrthoDB; 9801810at2; -.
DR Proteomes; UP000017915; 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; 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; 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 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; 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:UP000017915};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EST22892.1}.
FT DOMAIN 2..233
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
FT DOMAIN 384..511
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 532..632
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 638..740
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 831 AA; 89991 MW; E6E823EDC17AA6C8 CRC64;
MKAVVMAGGE GTRLRPMTAS MPKPLLPVAN RPIMEHVLRL LKRHGLSETV VTVQFLASLV
RNYFGDGEEL GMELTYANEE KPLGTAGSVK NAEEALKDDS FLVISGDALT DFDLTDLVRF
HRERGALVTV CLTRVPNPLE FGITIVDEDG KVERFLEKPT WGQVFSDTVN TGIYVMEPEV
FDYVDPDVSV DWSGDVFPQL MKEGKPIYGY VAEGYWEDVG THESYVKAQA DVLEGKVQVD
IDGFELSPGV WVAEGAEVHP EAVLRGPLYI GDYAKIEAGV EIREHSVIGS NVVVKSGAFL
HRAVVHDNVY IGQQANLRGC VVGRNTDVMR AARIEDGAVI GDECLVGEES IIQGNVRVYP
FKTVEAGAFV NTSVIWESRG QAHLFGARGV SGILNVEITP ELAVRLAGAY ATTLKKGSTV
TTARDHSRGA RALKRAIISA LQTSAIDVRD LENVPLPVAR QQTARGSAGG IMIRTTQGMP
DNVDIMFFDE RGADLSQGAQ RKLDRVYTRQ EYRRAFPGEI GDLRFPASVF DSYTGSLLRA
VNTEGIPESG LKVVVDASNG SSGLVLPSLL GRLGVDALTI NPGLAEARPT ETADSRRSGL
VRLGEIVASA RAAFGVRFDP VGERLSLVDE RGKIVEDHRA LLVMLDLVAA ERRSGRVALP
VTTTRIAEQV AAYHGTQVEW TTTSPDDLTR VGREDDTIFG GDGQGGFIVP ESSSVFDGTA
AFVRLLGLVA RTQLTLSQID ARIPQAHVLR RSLTTPWAVK GSVMRRVVEA AGDRDVDTTD
GVRIVESDGR WVMVLPDPAE AVTHLWAEGP DDTSAQVLLD EWTAVVDGAG R
//
