ID A0A3R9SYL2_9ACTN Unreviewed; 831 AA.
AC A0A3R9SYL2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Mannose-1-phosphate guanyltransferase {ECO:0000313|EMBL:RSR96661.1};
GN ORFNames=EF917_23255 {ECO:0000313|EMBL:RSR96661.1};
OS Streptomyces sp. WAC00469.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2487415 {ECO:0000313|EMBL:RSR96661.1, ECO:0000313|Proteomes:UP000269080};
RN [1] {ECO:0000313|EMBL:RSR96661.1, ECO:0000313|Proteomes:UP000269080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WAC00469 {ECO:0000313|EMBL:RSR96661.1,
RC ECO:0000313|Proteomes:UP000269080};
RA Culp E., Yim G., Waglechner N., Wang W., Pawlowski A.C., Wright G.D.;
RT "Unmasking the antibiotic production potential of Actinomycetes through
RT CRISPR/Cas9 inactivation of ubiquitous gene clusters.";
RL Submitted (NOV-2018) 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:RSR96661.1}.
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DR EMBL; RPRX01000100; RSR96661.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R9SYL2; -.
DR OrthoDB; 9801810at2; -.
DR Proteomes; UP000269080; 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:UP000269080};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RSR96661.1}.
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 640..740
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 831 AA; 89687 MW; 6FE2B88BE8D594CB CRC64;
MKAVVMAGGE GTRLRPMTSS MPKPLLPVAN RPIMEHVLRL LKRHGLNETV VTVQFLASLV
KNYFGDGEEL GMELTYANEE KPLGTAGSVK NAEEALKDDA FLVISGDALT DFDLTDLIRF
HKEKGAMVTV CLTRVPNPLE FGITIVDEEG KVERFLEKPT WGQVFSDTVN TGIYVMEPEI
FDYVEPDVPV DWSGDVFPKL MKEGKPIYGY VAEGYWEDVG THESYVKAQA DVLEGKVDVQ
LDGFEISPGV WVAEGAEVHP DAVLRGPVYI GDYAKVEAGA EIREHTVIGS NVVVKSGAFL
HKAVVHDNVY IGQHSNLRGC VVGKNTDIMR AARIEDGAVI GDECLIGEES IVQGNVRVYP
FKTIEAGAFV NTSVIWESRG QAHLFGARGV SGILNVEITP ELAVRLAGAY ATTLKKGATV
TTARDHSRGA RALKRAVISA LQASAIDVRD LENVPLPVAR EQTARGSAGG IMIRTTPGVP
DSVDIMFFDG QGADLSQAGQ RKLDRVFARQ EYRRAFPGEI GDLHFPSSVF DSYTGSLLRN
VDTTGIAESG LKVVVDASNG SAGLVLPSLL GKLGVDSLTI NPGLDESRPT ETEEMRRKGL
VRLGEIVASS GAAFGVRFDP VGERLSLVDE KGRIIEDDRA LLVMLDLVAA ERRSGRVALP
VTTTRIAEQV AAYHGTQVEW TTTSPDDLTR VGRQEGTIFG GDGKGGFIVP EFSSVYDGTA
AFVRLIGLVA RTQLTLSQID ARIPRAHVLK KDLATPWAVK GLVMRTVVEA AGDRHVDTTD
GVRVVESDGR WVMVLPDPAE AVTHLWAEGP DDASAQALLD EWSAVVDSAG R
//
