ID A0A0N0TSJ5_9ACTN Unreviewed; 831 AA.
AC A0A0N0TSJ5;
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:KOX26253.1};
GN ORFNames=ADL06_15910 {ECO:0000313|EMBL:KOX26253.1};
OS Streptomyces sp. NRRL F-6491.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519495 {ECO:0000313|EMBL:KOX26253.1, ECO:0000313|Proteomes:UP000037743};
RN [1] {ECO:0000313|EMBL:KOX26253.1, ECO:0000313|Proteomes:UP000037743}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL F-6491 {ECO:0000313|EMBL:KOX26253.1,
RC ECO:0000313|Proteomes:UP000037743};
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:KOX26253.1}.
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DR EMBL; LGEE01000210; KOX26253.1; -; Genomic_DNA.
DR RefSeq; WP_053648910.1; NZ_LGEE01000210.1.
DR AlphaFoldDB; A0A0N0TSJ5; -.
DR PATRIC; fig|1519495.3.peg.3390; -.
DR OrthoDB; 9801810at2; -.
DR Proteomes; UP000037743; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KOX26253.1}.
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; 89574 MW; 866CEB8680F4ACC5 CRC64;
MKAVVMAGGE GTRLRPMTSS MPKPLLPVVN RPIMEHVLRL LKRHGLNETV VTVQFLASLV
RNYFGDGEEL GMELTYANEE KPLGTAGSVK NAEEALKDDA FLVISGDALT DFDLTDLIAF
HKEKGALVTV CLTRVPNPLE FGITIVDEEG KVERFLEKPT WGQVFSDTVN TGIYVMEPEV
FDYVEADTSV DWSGDVFPQL MKEGKPIYGY VAEGYWEDVG THESYVKAQA DVLEGKVQVD
IDGFEISPGV WVSEGAEVHP DAVLRGPLYI GDYAKVEAGA EIREHTVVGS NVVVKSGAFL
HKAVVHDNVY IGQQSNLRGC VIGKNTDVMR AARIEDGAVI GDECLVGEES IVQGNVRVYP
FKTIEAGAFV NTSVIWESRG QAHLFGARGV SGILNVEITP ELAVRLAGAY ATTLKKGSTV
TTARDHSRGA RALKRAVISA LQASAIDVRD LENVPLPVAR QQTARGSAGG IMIRTSPGVP
DSVDIMFFDE RGADLSQGGQ RKLDRVFARQ EYRRAFPGEI GDLSFPASVF DSYTGSLLRN
VDTSGIAEAG LKVVVDASNG SAGLVLPSLL GRLQVDSLTI NPGLDESRPT ESAESRRAGL
VRLGEIVASA RAAFGVRFDP VGERLSLVDE RGRIIEDDRA LLVMLDLVAA ERRSGRVALP
VTTTRIAEQV AAYHGTQVDW TTTSPDDLTR VGREESTIFG GDGRGGFIVP EFSSVFDGTA
AFVRLLGLVA RTQLTLSQID ARIPRAHVLK RDIATPWAVK GLVMRKVVEA AGSRSVDTTD
GVRVVEADGR WVMVLPDPAE AVTHLWAEGP DDTSAQALLD EWAAVVDSAG N
//
