ID F2RBD1_STRVP Unreviewed; 831 AA.
AC F2RBD1;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Mannose-1-phosphate guanylyltransferase or Phosphomannomutase {ECO:0000313|EMBL:CCA54259.1};
DE EC=2.7.7.13 {ECO:0000313|EMBL:CCA54259.1};
GN OrderedLocusNames=SVEN_0972 {ECO:0000313|EMBL:CCA54259.1};
OS Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM
OS 4526 / NBRC 13096 / PD 04745).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=953739 {ECO:0000313|EMBL:CCA54259.1, ECO:0000313|Proteomes:UP000006854};
RN [1] {ECO:0000313|EMBL:CCA54259.1, ECO:0000313|Proteomes:UP000006854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 /
RC PD 04745 {ECO:0000313|Proteomes:UP000006854};
RX PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA Pullan S.T., Bibb M.J., Merrick M.;
RT "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT provides new insights into global nitrogen regulation in actinomycetes.";
RL BMC Genomics 12:175-175(2011).
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231}.
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DR EMBL; FR845719; CCA54259.1; -; Genomic_DNA.
DR RefSeq; WP_015032178.1; NZ_JABVZO010000242.1.
DR AlphaFoldDB; F2RBD1; -.
DR SMR; F2RBD1; -.
DR STRING; 953739.SVEN_0972; -.
DR GeneID; 69863159; -.
DR KEGG; sve:SVEN_0972; -.
DR PATRIC; fig|953739.5.peg.3018; -.
DR eggNOG; COG1109; Bacteria.
DR eggNOG; COG1208; Bacteria.
DR HOGENOM; CLU_017652_1_0_11; -.
DR OrthoDB; 9801810at2; -.
DR Proteomes; UP000006854; Chromosome.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0004475; F:mannose-1-phosphate guanylyltransferase (GTP) activity; IEA:UniProtKB-EC.
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:CCA54259.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006854};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CCA54259.1}.
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; 89647 MW; BBAF0E5B42D98555 CRC64;
MKAVVMAGGE GTRLRPMTSS MPKPLLPVVN RPIMEHVLRL LKRHGLNETV VTVQFLASLV
RNYFGDGEEL GMELTYANEE KPLGTAGSVK NAEEALKDDA FLVISGDALT DFDLTDLIAF
HKEKGALVTV CLTRVPNPLE FGITIVDEEG KVERFLEKPT WGQVFSDTVN TGIYVMEPEV
FDYVQADVPV DWSGDVFPQL MKEGKPIYGY VAEGYWEDVG THESYVKAQA DVLEGKVQVD
IDGFEISPGV WVAEGAEVHH DAVLRGPLYI GDYAKVEADA EIREHTVVGS NVVVKSGAFL
HKAVVHDNVY IGQQSNLRGC VIGKNTDIMR AARIEDGAVI GDECLVGEES IVQGNVRVYP
FKTIEAGAFV NTSVIWESRG QAHLFGARGV SGILNVEITP ELAVRLAGAY ATTLKKGSTV
TTARDHSRGA RALKRAVISA LQASAIDVRD LENVPLPVAR QQTARGSAGG IMVRTSPGVP
DSVDIMFFDE RGADLSQGGQ RKLDRVFARQ EYRRAFPGEI GDLSFPASVF DSYTGSLLRN
VDTTGIAEAG LKVVVDASNG SAGLVLPSLL GRLQVDSLTI NPGLDESRPT ESAESRRAGL
VRLGEIVASA RAAFGVRFDP VGERLSLVDE RGRIIEDDRA LLVMLDLVAA ERRSGRVALP
VTTTRIAEQV AAYHGTQVEW TTTSPDDLTR VGREESTIFG GDGRGGFIVP EFSSVFDGAA
AFVRLIGLVA RTQLTLSQID ARIPRAHVLK RDIATPWAVK GLVMRRVVEA AGSRSVDTTD
GVRVVEADGR WVMVLPDPAE AVTHLWAEGP DDASAQALLD EWAEVVASAG S
//
