ID A0A1A5NW68_9ACTN Unreviewed; 831 AA.
AC A0A1A5NW68;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Mannose-1-phosphate guanyltransferase {ECO:0000313|EMBL:OBQ47189.1};
GN ORFNames=A4U61_17735 {ECO:0000313|EMBL:OBQ47189.1};
OS Streptomyces sp. H-KF8.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1727216 {ECO:0000313|EMBL:OBQ47189.1, ECO:0000313|Proteomes:UP000093719};
RN [1] {ECO:0000313|Proteomes:UP000093719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H-KF8 {ECO:0000313|Proteomes:UP000093719};
RA Undabarrena A., Ugalde J.A., Seeger M., Camara B.;
RL Submitted (APR-2016) 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:OBQ47189.1}.
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; LWAB01000011; OBQ47189.1; -; Genomic_DNA.
DR RefSeq; WP_065002704.1; NZ_LWAB01000011.1.
DR AlphaFoldDB; A0A1A5NW68; -.
DR OrthoDB; 9801810at2; -.
DR Proteomes; UP000093719; 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:UP000093719};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OBQ47189.1}.
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 639..740
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 831 AA; 89568 MW; 789D921F045EE8F3 CRC64;
MKAVVMAGGE GTRLRPMTSS MPKPLLPVAN QPIMEHVLRL LKRHGLNETV VTVQFLASLV
KNYFGDGEEL GMELTYANEE KPLGTAGSVK NAEEALKDDT FLVISGDALT DFDLTELINF
HKEKGALVTV CLTRVPNPLE FGITIVDEEG KVERFLEKPT WGQVFSDTVN TGIYVMEPEV
FDYVEPDVPV DWSGDVFPQL MKEGKPVYGF IAEGYWEDVG THESYVKAQA DVLEGKVDVD
IDGFEISPGV WVAEGAEVHP DAVLRGPLYI GDYAKVEAGA EIREHTVVGS NVVVKSGAFL
HKAVVHDNVY VGPHSNLRGC VLGRNTDVMR AARIEDGAVI GDECLIGEES IVQGNVRVYP
FKTIEAGAFV NTSVIWESRG QAHLFGARGV SGILNVEITP ELAVRLAGAY ATTLKKGSTV
TTARDHSRGA RALKRAVISA LQASAIDVRD LENVPLPVAR QQTARGSAGG IMIRTTPGVP
DSVDIMFFDG QGADLSQGGQ RKLDRVFARQ EYRRAFPGEI GDLHFPASVF DSYTGSLLRN
VDITGIAESG LKVVVDASNG SAGLVLPSLL GKLGVDSLTI NPGLDESRPT ETADVRRAGL
VRLGEMVASS GAAFGVRFDP VGERLSLVDE KGRIIEDDRA LLVMLDLIAA ERRSGRVALP
VTTTRIAEQV AAYHGTQVEW TTTSPDDLTR VGGEEGTIFG GDGKGGFIVP EFNRVYDGTA
AFVRLIGLVA RTQLTLSQID ARIPRAHVLK RDLATPWAVK GLVMRRVVEE AGDRFVDTTD
GVRVVEADGR WVMVLPDPAE AVTHLWAEGP DDASAQALLD EWAAVVDSAG R
//