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Database: UniProt
Entry: K9YL76_CYASC
LinkDB: K9YL76_CYASC
Original site: K9YL76_CYASC 
ID   K9YL76_CYASC            Unreviewed;       503 AA.
AC   K9YL76;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=Phosphoglucomutase/phosphomannomutase alpha/beta/alpha domain I {ECO:0000313|EMBL:AFZ47207.1};
GN   OrderedLocusNames=Cyast_1242 {ECO:0000313|EMBL:AFZ47207.1};
OS   Cyanobacterium stanieri (strain ATCC 29140 / PCC 7202).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Geminocystaceae; Cyanobacterium.
OX   NCBI_TaxID=292563 {ECO:0000313|EMBL:AFZ47207.1, ECO:0000313|Proteomes:UP000010483};
RN   [1] {ECO:0000313|Proteomes:UP000010483}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29140 / PCC 7202 {ECO:0000313|Proteomes:UP000010483};
RX   PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA   Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA   Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA   Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA   Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT   "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT   genome sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC       {ECO:0000256|ARBA:ARBA00010231}.
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DR   EMBL; CP003940; AFZ47207.1; -; Genomic_DNA.
DR   AlphaFoldDB; K9YL76; -.
DR   STRING; 292563.Cyast_1242; -.
DR   KEGG; csn:Cyast_1242; -.
DR   PATRIC; fig|292563.3.peg.1302; -.
DR   eggNOG; COG1109; Bacteria.
DR   HOGENOM; CLU_016950_6_0_3; -.
DR   OMA; NCDGAIM; -.
DR   BioCyc; CSTA292563:G1353-1248-MONOMER; -.
DR   Proteomes; UP000010483; Chromosome.
DR   GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd03089; PMM_PGM; 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   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; IPR005841; Alpha-D-phosphohexomutase_SF.
DR   PANTHER; PTHR42946:SF1; PHOSPHOGLUCOSAMINE MUTASE FAMILY PROTEIN; 1.
DR   PANTHER; PTHR42946; PHOSPHOHEXOSE MUTASE; 1.
DR   Pfam; PF02878; PGM_PMM_I; 1.
DR   Pfam; PF02879; PGM_PMM_II; 1.
DR   Pfam; PF02880; PGM_PMM_III; 1.
DR   PRINTS; PR00509; PGMPMM.
DR   SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000010483}.
FT   DOMAIN          9..151
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          175..279
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          284..399
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
SQ   SEQUENCE   503 AA;  56253 MW;  8D86C9282D4119CA CRC64;
     MLKENWKKLQ NGSDIRGVAL EGIEGEKVNL TPEIIKILGK SFAQWLSEKL SKSPSQLIIS
     LGRDSRLSGE NLLGTIATAI SELGVTVYNF EMASTPAMFM STIDTDLNCD GAIMLTASHL
     PFNRNGLKFF TKQGGLEKQD ITNILEKAQE NSFNYTKEKG NIINKNFMAK YADLFVKQIR
     QAVNHPRHFE EPLKELKIIV DAGNGAGGFF ADKVLKPLGA DITGSQFLEP DGTFPNHIPN
     PENPEAMASI CEAVIKHKAD FGIIFDTDVD RSAAVDSTGK ELNRNRLIAL ISAIILQEHP
     QSTIVTDSIT SEGLTKFIEQ NLGGKHHRFK RGYKNVINEA LRLNNEGIES WLAIETSGHA
     ALKENYFLDD GAYLITKLLI ELAKLKLMDK RLTELINSLE EPLESKEIRL TIKADNFKEY
     GNNIIEELTI FTNNQSDWQI VPNNYEGVRV SCPSEEEKGW FLLRLSLHDP VIPINIESNV
     QGGVEKIMAR LFRFLESFSA LEK
//
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