ID A0A2S6CXU7_9CYAN Unreviewed; 842 AA.
AC A0A2S6CXU7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Mannose-1-phosphate guanylyltransferase {ECO:0000313|EMBL:PPJ64576.1};
GN ORFNames=CUN59_04115 {ECO:0000313|EMBL:PPJ64576.1};
OS Cuspidothrix issatschenkoi CHARLIE-1.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Aphanizomenonaceae;
OC Cuspidothrix.
OX NCBI_TaxID=2052836 {ECO:0000313|EMBL:PPJ64576.1, ECO:0000313|Proteomes:UP000239589};
RN [1] {ECO:0000313|EMBL:PPJ64576.1, ECO:0000313|Proteomes:UP000239589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHARLIE-1 {ECO:0000313|EMBL:PPJ64576.1,
RC ECO:0000313|Proteomes:UP000239589};
RA Kust A., Mares J., Jokela J., Urajova P., Hajek J., Saurav K., Voracova K.,
RA Fewer D.P., Haapaniemi E., Permi P., Rehakova K., Sivonen K., Hrouzek P.;
RT "Discovery of a pederin family compound in a non-symbiotic bloom-forming
RT cyanobacterium.";
RL Submitted (FEB-2018) 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:PPJ64576.1}.
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DR EMBL; PGEM01000025; PPJ64576.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S6CXU7; -.
DR OrthoDB; 9803871at2; -.
DR Proteomes; UP000239589; Unassembled WGS sequence.
DR GO; GO:0031470; C:carboxysome; IEA:UniProt.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0043886; F:structural constituent of carboxysome shell; IEA:UniProt.
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; IPR001451; Hexapep.
DR InterPro; IPR018357; Hexapep_transf_CS.
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; PF00132; Hexapep; 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; 3.
DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 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:PPJ64576.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000239589};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PPJ64576.1}.
FT DOMAIN 3..233
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
FT DOMAIN 383..513
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 534..631
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 636..743
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 842 AA; 93268 MW; EBC67DDC1BF87778 CRC64;
MRAVLMAGGS GTRLRPLTCD LPKPMVPILN RPIAEHIINL LKRHQIYEVI ATLHYLPDVL
RDYFQDGGDF GVQMTYAIEE DQPLGTAGCV KNIAELLDET FLVISGDSIT DFDLSAAIEF
HKQKQSKATL ILTRVPNPIE FGVVITDTEG RINRFLEKPS TSEIFSDTVN TGTYILEPEV
LDYLPEHTEC DFSKDLFPLL LAKNEPIYGY VAEGYWCDVG HLDAYREAQY DALERKVRLK
VAYPEIAPGL WIGQNTYIDP SAKIATPAVI GNNCRIGARV KIEDGTVIGD NVTIGADAHL
KRPIIWNGAI IGDEAQLSAC VISRGTRVDR RAHVLEAAVV GSLSTVGEEA QISPGVRVWP
SKKIESGAVL NINLIWGNIA QRNLFGQRGV QGLANIDITP EFAVKLGAAY GSTLKPGSMV
TVSRDQRNVS RMVTRSLIAG LMSVGVDVQN LDTTAIPIAR TVIPTMQVTG GIHVRVHPER
RDYILIEFMD MKGINISKAQ EKKIEGAYFK EDMRRSQSHE IGDVVYSSQL MDCYGKAFEK
LLNVDTLRHS RAKVVIDYVY AVSGAVLPQM LDKFGADAVV LNASLNKTAI SNADRELLLT
QLGHVVEAVN ANFGVQVSAN GEQLILVDES GFPIRGEMLT ALMVDMMLTA NPRSSVVVPV
HASSAVELVA HRHDGNVIRT KANPTALMEA CQKNPNVVLG GSGETGFIFP QLHPGFDSMF
CIAKLIEMLT IQERSLATVR SELPRVIHRT YTVRCPWTAK GALMRYLVET HPAQNLELID
GVKIRQPYDD NWVLLLPDAS EPLVHLYVNS SDRDWVDETL RDYRARVQYF VEREQENYRL
DI
//
