ID A0A0X3XHQ8_9ACTN Unreviewed; 831 AA.
AC A0A0X3XHQ8;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Mannose-1-phosphate guanyltransferase {ECO:0000313|EMBL:KUL68818.1};
GN ORFNames=ADL34_32205 {ECO:0000313|EMBL:KUL68818.1};
OS Streptomyces sp. NRRL WC-3605.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609103 {ECO:0000313|EMBL:KUL68818.1, ECO:0000313|Proteomes:UP000052945};
RN [1] {ECO:0000313|EMBL:KUL68818.1, ECO:0000313|Proteomes:UP000052945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL WC-3605 {ECO:0000313|EMBL:KUL68818.1,
RC ECO:0000313|Proteomes:UP000052945};
RA Gilbert D.G.;
RL Submitted (OCT-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:KUL68818.1}.
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; LLZN01000104; KUL68818.1; -; Genomic_DNA.
DR RefSeq; WP_062674486.1; NZ_LLZN01000104.1.
DR AlphaFoldDB; A0A0X3XHQ8; -.
DR OrthoDB; 9801810at2; -.
DR Proteomes; UP000052945; 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:UP000052945};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KUL68818.1}.
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; 89634 MW; 84D14CCD94F50C4C CRC64;
MKAVVMAGGE GTRLRPMTSS MPKPLLPVAN RPIMEHVLRL LKRHGLNETV VTVQFLASLV
KNYFGDGEEL GMELTYANEE KPLGTAGSVK NAEEALKDDA FLVISGDALT DFDLTELINF
HKEKGSMVTV CLTRVPNPLE FGITIVDEEG RVERFLEKPT WGQVFSDTVN TGIYVMEPEV
FDYVEADVPV DWSGDVFPQL MKEGKPIYGY VAEGYWEDVG THESYVKAQA DVLEGKVDVE
LDGFEISPGV WVAEGAEVHP DAVLRGPAYI GDYAKVEAGA EIREHTVVGS NVVVKSGAFL
HRAVVHDNVY VGPHSNLRGC VVGKNTDIMR AARIEDGAVI GDECLIGEES IVQGNVRVYP
FKTIEAGAFV NNSVIWESRG QAHLFGARGV SGILNVEITP ELAVRLAGAY ATTLKKGATV
TTARDHSRGA RALKRAVISA LQASAIDVRD LENVPLPVAR QQTARGSAGG IMIRTTPGVP
DSVDIMFFDG QGADLSQASQ RKLDRVFARQ EYRRAFPGEI GDLHFPASVF DSYTGSLLRN
VDTTGIAESG LKVVVDASNG SAGLVLPSLL GKLGVDSLTI NPGLDESRPT ESADTRRSGL
VRLGEIVASA RAAFGVRFDP VGERLSLVDE KGRIVEDDRA LLVMLDLVAA ERRSGRVALP
VTTTRIAEQV AAYHGTQVEW TTTSPDDLTR VGADEATIFG GDGRGGFIIP EFSSVFDGTA
AFVRLIGLVA RTQLTLSQID ARIPRAHVLK RDLATPWAVK GLVMRRVVEE AGDRFVDTTD
GVRVVETDGR WVMVLPDPAE AVTHLWAEGP DDASAQALLD EWAAVVDSAG R
//
