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
//