ID D9VJR6_9ACTN Unreviewed; 832 AA.
AC D9VJR6;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Mannose-1-phosphate guanyltransferase {ECO:0000313|EMBL:EFL13947.1};
GN ORFNames=SSNG_01199 {ECO:0000313|EMBL:EFL13947.1};
OS Streptomyces sp. C.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=253839 {ECO:0000313|EMBL:EFL13947.1, ECO:0000313|Proteomes:UP000005763};
RN [1] {ECO:0000313|EMBL:EFL13947.1, ECO:0000313|Proteomes:UP000005763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C {ECO:0000313|EMBL:EFL13947.1,
RC ECO:0000313|Proteomes:UP000005763};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces sp. strain C.";
RL Submitted (FEB-2009) 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; GG657750; EFL13947.1; -; Genomic_DNA.
DR RefSeq; WP_007262896.1; NZ_GG657750.1.
DR AlphaFoldDB; D9VJR6; -.
DR STRING; 253839.SSNG_01199; -.
DR eggNOG; COG1109; Bacteria.
DR eggNOG; COG1208; Bacteria.
DR HOGENOM; CLU_017652_1_0_11; -.
DR Proteomes; UP000005763; 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:EFL13947.1}.
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 639..740
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 832 AA; 89741 MW; C921EFB391F2454D CRC64;
MKAVVMAGGE GTRLRPMTSS MPKPLLPVVN RPIMEHVLRL LKRHGLSETV VTVQFLASLV
KNYFGDGEEL GMELTYANEE KPLGTAGSVK NAEEALKDDT FLVISGDALT DFDLTDLINF
HKEKGALVTV CLTRVPNPLE FGITIVDEEG KVERFLEKPT WGQVFSDTIN TGIYVMEPEI
FDYVDPDVSV DWSGDVFPQL MKEGRPIFGY VAEGYWEDVG THASYVKAQA DVLEGKVQVD
MDGFEISPGV WIAEGAEVSP DAVLRGPLYV GDYAKVEAGV ELREHTVVGS NVVVKSGAFL
HKAVVHDNVY IGPHSNLRGC VIGKNTDIMR AARIEDGAVI GDECLVGEES IIQGNVRVYP
FKTIEAGAFV NTSVIWESRG QAHLFGARGV SGILNVEITP ELVVKLAGAY ATMLKKGAIV
TTARDHSRGA RALKRAVISA LQASAIDVRD LENVPLPVAR QQTARGAAGG IMIRTSPGVP
DSVDIMFLDE RGADLSQAQQ RKLDRVYARQ EYRRAFPGEI GDLQFPSSVF DSYTGSLLRR
VDTTGIADAG LKVVVDASNG SAGLVLPSLL GRLGVDALTI NPGLDESRPT ETRESRRAGL
VRLGEIVASA RAAFGVRFDP VGERISLVDE RGRIIEDDRA LLVLLDLVAA EKRSGKVALP
VTTTRVAEQV AAYHGTQVEW TTTSPDDLTR VGREETTIFG GDGRGGFIVP EFSSVFDGSA
AFVQLIGLVA RTQLTLSQID ARIPRAHVLK RDVPTPWAAK GLVMRRVVEA AGDRQVDTTD
GVRVVEADGR WALVLPDPAE AVTHLWAEGP DDASAQALLD EWGAAVDGAG QH
//
