ID A0A0M8QHS9_9ACTN Unreviewed; 831 AA.
AC A0A0M8QHS9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Mannose-1-phosphate guanyltransferase {ECO:0000313|EMBL:KOT37052.1};
GN ORFNames=ADK41_20840 {ECO:0000313|EMBL:KOT37052.1};
OS Streptomyces caelestis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=36816 {ECO:0000313|EMBL:KOT37052.1, ECO:0000313|Proteomes:UP000037773};
RN [1] {ECO:0000313|EMBL:KOT37052.1, ECO:0000313|Proteomes:UP000037773}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-24567 {ECO:0000313|EMBL:KOT37052.1,
RC ECO:0000313|Proteomes:UP000037773};
RA Noorani M.;
RL Submitted (JUL-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:KOT37052.1}.
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DR EMBL; LGCN01000200; KOT37052.1; -; Genomic_DNA.
DR RefSeq; WP_030833762.1; NZ_LGCN01000200.1.
DR AlphaFoldDB; A0A0M8QHS9; -.
DR PATRIC; fig|36816.3.peg.4511; -.
DR OrthoDB; 9801810at2; -.
DR Proteomes; UP000037773; 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:UP000037773};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KOT37052.1}.
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; 89467 MW; D4401398123D9BA6 CRC64;
MKAVVMAGGE GTRLRPMTSS MPKPLLPVAN RPIMEHVLRL LKKHGLNETV VTVQFLASLV
KNYFGDGEEL GMELTYANEE KPLGTAGSVK NAEEALKDDA FLVISGDALT DFDLTELINF
HKEKGALVTV CLTRVPNPLE FGITIVDEEG KVERFLEKPT WGQVFSDTVN TGIYVMEPEV
FDYVDPDVPV DWSGDVFPQL MKEGKPVYGY VAEGYWEDVG THESYVKAQA DVLEGKVDVD
IDGFEISPGV WVAEGAEVHP DAVLRGPLYI GDYAKVEAGA EIREHTVVGS NVVVKSGAFL
HKAVVHDNVY VGPHSNLRGC VVGKNTDIMR AARIEDGAVI GDECLVGEES IVQGNVRVYP
FKTIEAGAFV NTSVIWESRG QAHLFGARGV SGILNVEITP ELAVRLAGAY ATTLKKGSTV
TTARDHSRGA RALKRAVISA LQASAIDVRD LENVPLPVAR QQTARGSAGG IMIRTTPGVP
DSVDIMFFDG QGADLSQGSQ RKLDRVFARQ EYRRAFPGEI GDLHFPASVF DSYTGSLLRN
VDITGIAESG LKVVVDASNG SAGLVLPSLL GKLGVDSLTI NPGLDESRPT ETADMRRSGL
VRLGEIVASS GAAFGVRFDP VGERLSLVDE KGRIIEDDRS LLVMLDLIAS ERRSGRVALP
VTTTRIAEQV AAYHGTQVEW TTTSPDDLTR VGGEEGTIFG GDGKGGFIVP EFSSVYDGTA
AFVRLIGLVA RTQLTLSQID ARIPRAHVLK RDLATPWAVK GLVMRRVVEA AGDRFVDTTD
GVRVVETDGR WVMVLPDPAE AVTHLWAEGP DDASAQALLD EWSAVVDSAG R
//
