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Database: UniProt
Entry: A0A345SSA8_9ACTN
LinkDB: A0A345SSA8_9ACTN
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ID   A0A345SSA8_9ACTN        Unreviewed;       831 AA.
AC   A0A345SSA8;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Mannose-1-phosphate guanyltransferase {ECO:0000313|EMBL:AXI76613.1};
GN   ORFNames=C7M71_003140 {ECO:0000313|EMBL:AXI76613.1};
OS   Peterkaempfera bronchialis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Peterkaempfera.
OX   NCBI_TaxID=2126346 {ECO:0000313|EMBL:AXI76613.1, ECO:0000313|Proteomes:UP000249340};
RN   [1] {ECO:0000313|Proteomes:UP000249340}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 106435 {ECO:0000313|Proteomes:UP000249340};
RA   Batra D., Gulvik C.A.;
RT   "Streptacidiphilus bronchialis DSM 106435 chromosome.";
RL   Submitted (JUL-2018) 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; CP031264; AXI76613.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A345SSA8; -.
DR   KEGG; stri:C7M71_003140; -.
DR   OrthoDB; 9801810at2; -.
DR   Proteomes; UP000249340; Chromosome.
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:UP000249340};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AXI76613.1}.
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;  89721 MW;  1B45EC1757F63680 CRC64;
     MKAVVMAGGE GTRLRPMTSS MPKPLLPVVN RPIMEHVLRL LKRHGLNETV VTVQFLASLV
     KNFFGDGEEL GMSLTYANEE VPLGTAGSVK NAEDALKDDS FLVISGDALT DFDLTDLIRF
     HREKGALVTV CLTRVPNPLE FGITIVDDEG KVERFLEKPT WGQVFSDTVN TGIYVMEPEV
     FDYVAADESV DWSSDVFPQL LKEGKPIYGY IAEGYWEDVG THESYVKAQA DVLEGKVDVD
     IDGFEISPGV WVAEGAEVDR EAVLRGPLYI GDYAKVEAGV ELREHTVLGS NVVVKRGAFL
     HKAVVHDNVY IGPQSNLRGC VIGKNTDVMR AARIDDGAVI GDECLIEEES IIAGNVRVYP
     FKTIEAGAFV NTSVIWESRG QEHLFGARGV SGILNVEITP ELAVRLAGAY ATTLKKGATV
     TIARDHSRGA RALKRAMISA LQTSAIDVRD LENVPMPVAR QQTARGSAGG IMLRTTPGVP
     DSVDILFFDE RGADLSQAGQ RKLDRVYARQ EYRRAFPGEI GDLTSSSRVF DSYAGTLLKA
     VDISGVAESG LKVVVDTAHG SASLVLPSLL GRLGVEALTV NGGLDETHPT ETAEERRIGL
     VRLGELVASS RAAFGVRFDP VGERISFVDE RGRIIEDDRA LLVLLDLVAA ERRSGRVALP
     VTTTRIAEQV AAYHGTQVLW TTTSPDDLTR ASAAEGTVFG GDGRGGFVVP EFSGVFDGPA
     AFVRLMGLVA RTQLTLSQID ARIPTAHVHR RDLATPWSAK GMVMRSVVEA AGDRQVDTTD
     GVRVVEPDGR WTMVLPDPAE AVTHLWAEGP DEAATQALLD EWAGVVEGAG R
//
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