ID B1WR63_CROS5 Unreviewed; 488 AA.
AC B1WR63;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Phosphoglucomutase/phosphomannomutase {ECO:0000313|EMBL:ACB50121.1};
GN OrderedLocusNames=cce_0770 {ECO:0000313|EMBL:ACB50121.1};
OS Crocosphaera subtropica (strain ATCC 51142 / BH68) (Cyanothece sp. (strain
OS ATCC 51142)).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Crocosphaera; Crocosphaera subtropica.
OX NCBI_TaxID=43989 {ECO:0000313|EMBL:ACB50121.1, ECO:0000313|Proteomes:UP000001203};
RN [1] {ECO:0000313|EMBL:ACB50121.1, ECO:0000313|Proteomes:UP000001203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51142 / BH68 {ECO:0000313|Proteomes:UP000001203};
RX PubMed=18812508; DOI=10.1073/pnas.0805418105;
RA Welsh E.A., Liberton M., Stoeckel J., Loh T., Elvitigala T., Wang C.,
RA Wollam A., Fulton R.S., Clifton S.W., Jacobs J.M., Aurora R., Ghosh B.K.,
RA Sherman L.A., Smith R.D., Wilson R.K., Pakrasi H.B.;
RT "The genome of Cyanothece 51142, a unicellular diazotrophic cyanobacterium
RT important in the marine nitrogen cycle.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:15094-15099(2008).
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, ECO:0000256|RuleBase:RU004326}.
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DR EMBL; CP000806; ACB50121.1; -; Genomic_DNA.
DR RefSeq; WP_009546009.1; NC_010546.1.
DR AlphaFoldDB; B1WR63; -.
DR STRING; 43989.cce_0770; -.
DR KEGG; cyt:cce_0770; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_7_1_3; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000001203; Chromosome circular.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProt.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd05800; PGM_like2; 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; IPR005843; A-D-PHexomutase_C.
DR InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR PANTHER; PTHR45745:SF1; PHOSPHOGLUCOMUTASE 2A-RELATED; 1.
DR PANTHER; PTHR45745; PHOSPHOMANNOMUTASE 45A; 1.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 1.
DR Pfam; PF00408; PGM_PMM_IV; 1.
DR PRINTS; PR00509; PGMPMM.
DR SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004326};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001203}.
FT DOMAIN 8..149
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 170..277
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 285..391
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 421..476
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 488 AA; 53416 MW; 8FDF45C1CA64B540 CRC64;
MAFTQNPIKF GTDGWRGVIA ADFTFERVAM LAPLAAKILE ENYRVSASAP QSGSLRDRTI
IVGYDRRFLA EEFAQVATDA IIEAGYNVML SDSYAPTPAF SWAAKAQNAL GAIVLTASHN
PGKYLGLKVK GAFGGSVSPA VTQQIEELLP NPPQFSASPG TISHFDPWES YCQGLQEKVD
INAIREAIAT GKLRVFADVM HGAAATGLER LLGCSIEEIN GDRDPLFEGG APEPLPRYLS
KLFTSIKTAA SQGNNSLRVG LVFDGDSDRI AAVDGQGNFL SSQILIPILI DHLANRKGFT
GEIIKTLSGS DLIPRLAHLY NLSVYETPIG YKYIADRMLN AEVLIGGEES GGIGYGTHIP
ERDALLSALY VLEAVVESGQ DLGEYYRQLQ EKTDFYNAYD RIDLPLANME VRAKLLQRLE
TEPLREVAGQ SVTSCDTKDG YKYRLTDGSW LLIRFSGTEP VLRLYCESLT MKQVHQTLNW
AKNWANSV
//
