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Database: UniProt
Entry: A0A239E2I9_9ACTN
LinkDB: A0A239E2I9_9ACTN
Original site: A0A239E2I9_9ACTN 
ID   A0A239E2I9_9ACTN        Unreviewed;       832 AA.
AC   A0A239E2I9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Mannose-1-phosphate guanylyltransferase / phosphomannomutase {ECO:0000313|EMBL:SNS38837.1};
GN   ORFNames=SAMN06265355_11663 {ECO:0000313|EMBL:SNS38837.1};
OS   Actinomadura mexicana.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Thermomonosporaceae; Actinomadura.
OX   NCBI_TaxID=134959 {ECO:0000313|EMBL:SNS38837.1, ECO:0000313|Proteomes:UP000198420};
RN   [1] {ECO:0000313|EMBL:SNS38837.1, ECO:0000313|Proteomes:UP000198420}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44485 {ECO:0000313|EMBL:SNS38837.1,
RC   ECO:0000313|Proteomes:UP000198420};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC       {ECO:0000256|ARBA:ARBA00010231}.
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DR   EMBL; FZNP01000016; SNS38837.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239E2I9; -.
DR   OrthoDB; 9801810at2; -.
DR   Proteomes; UP000198420; Unassembled WGS sequence.
DR   GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0016779; F:nucleotidyltransferase 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   Nucleotidyltransferase {ECO:0000313|EMBL:SNS38837.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SNS38837.1}.
FT   DOMAIN          2..233
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
FT   DOMAIN          383..512
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          533..633
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          641..740
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
SQ   SEQUENCE   832 AA;  89778 MW;  E07A2C0B23E55054 CRC64;
     MKAVVMAGGE GTRLRPMTAN QPKPLLPLVN RPIMEHVLRL LKKHGFGETV VTVQFLAALI
     RNYFGDGEEL GMSLSYATEE VPLGTAGSVK NAEEALRDDR FLVISGDALT DIDLTDMVRF
     HEENDALVTI GLKRVPNPLE FGIIIVDDVG RVQRFLEKPT WGQVFSDTVN TGIYVMEPEV
     LEHVAEGEPV DWSADVFPKL LAEGARLFGY VADCYWEDVG THESYLKAQA DMLSGQVGID
     LDGFEMSPGV WVAEGAEVDA EAILKGPLYI GDYAKVEAGV ELREFTVLGS NVVVKEGAFL
     HRAVVHDNVF VAPSTNLRGC VVGKNTDIMA GARVEEGAVI GDECVIEAEA YVSSGVKVYP
     FKTIEAGAVV NTSVIWESRG QRNLFGPRGV SGLVNVEITP ELAVRLASAY ATTLKKGTTV
     VTGRDVSRAA RTLKRAVNSA LTASAINVQD LEATPLTVAR FETGREDSVG GIYIRTTLGD
     PQGVDILFLD ADGADLSQGA QRKLERVFGR QEYRRAFPGE IAELTYPPRV VETYTRDLLR
     RVDIRGVREA GLKIVLDCAG GVASLVLPNL LGKVGVEVLT RNAGLDEANP TETLAERMRD
     LERLGELVSS SRAAFGVRFD PVGERISLVD ENGELVGDDR ALLVMLDLVA AERRGGKVAL
     PVTTTRVAEQ VCRFHGVQVE WTSTSQDVLT KAAAQPSVVF AGDGRGGFLM PEFSGTVDGI
     AAFVRLVGLV ARTRLTLSQI DRRIPDAHLL RRSVPTPWAA KGSVMRHVVE AAGNRTLDTT
     DGVRVVEGDG RWVLVLPDPA EAVTHLWAEG PDADAAQALL AEWAAVVERA GS
//
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