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Database: UniProt
Entry: A0A2T1CCG7_9CYAN
LinkDB: A0A2T1CCG7_9CYAN
Original site: A0A2T1CCG7_9CYAN 
ID   A0A2T1CCG7_9CYAN        Unreviewed;       542 AA.
AC   A0A2T1CCG7;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent) {ECO:0000256|ARBA:ARBA00012728};
DE            EC=5.4.2.2 {ECO:0000256|ARBA:ARBA00012728};
GN   ORFNames=C7B62_24035 {ECO:0000313|EMBL:PSB05956.1};
OS   Pleurocapsa sp. CCALA 161.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Hyellaceae;
OC   Pleurocapsa.
OX   NCBI_TaxID=2107688 {ECO:0000313|EMBL:PSB05956.1, ECO:0000313|Proteomes:UP000239836};
RN   [1] {ECO:0000313|EMBL:PSB05956.1, ECO:0000313|Proteomes:UP000239836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCALA 161 {ECO:0000313|EMBL:PSB05956.1,
RC   ECO:0000313|Proteomes:UP000239836};
RA   Cohen D.B., Kent A.D.;
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PSB05956.1, ECO:0000313|Proteomes:UP000239836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCALA 161 {ECO:0000313|EMBL:PSB05956.1,
RC   ECO:0000313|Proteomes:UP000239836};
RA   Moore K.R., Magnabosco C., Momper L., Gold D.A., Bosak T., Fournier G.P.;
RT   "The ancient ancestry and fast evolution of plastids.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate;
CC         Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601;
CC         EC=5.4.2.2; Evidence={ECO:0000256|ARBA:ARBA00000443};
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}.
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:PSB05956.1}.
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DR   EMBL; PVWF01000192; PSB05956.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T1CCG7; -.
DR   InParanoid; A0A2T1CCG7; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000239836; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004614; F:phosphoglucomutase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd03085; PGM1; 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; IPR036900; A-D-PHexomutase_C_sf.
DR   InterPro; IPR016066; A-D-PHexomutase_CS.
DR   InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR   InterPro; IPR045244; PGM.
DR   PANTHER; PTHR22573:SF2; PHOSPHOGLUCOMUTASE; 1.
DR   PANTHER; PTHR22573; PHOSPHOHEXOMUTASE FAMILY MEMBER; 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; 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   Magnesium {ECO:0000256|RuleBase:RU004326};
KW   Metal-binding {ECO:0000256|RuleBase:RU004326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000239836}.
FT   DOMAIN          14..149
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          184..285
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          294..406
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   542 AA;  59426 MW;  E0400CBAECC64C7F CRC64;
     MNIRTVSTTP FSDQKPGTSG LRKSVTVFQT PHYLENFVQS IFDSLDGCEG QTIVLGGDGR
     YYNRQAIQII LKMAAANGIG RILVGKGGIM STPAASAIIR QYKAYGGIIL SASHNPGGPQ
     GDFGIKYNIT SGGPAPEKVT EAIFERSKVI NRYKILEADD LNLDKLTVTR LGEMSVEVID
     PVEPYARLME SLFDFERIRQ LIKHDFKLCV DSMHAVTGPY AKDIFEKRLG AAGSVLNGEP
     LEDFGGGHPD PNLVYAHDLV EIMFANDAPD FGAASDGDGD RNMVLGNNFF VTPSDSLAVL
     TANATLVPGY KTGLSGVARS MPTSEAVDRV AEKLGITCYE TPTGWKFFGN LLDANKATLC
     GEESFGTGSN HVREKDGLWA VLFWLNILAV KGESVEAIVK DHWKTYGRNY YSRHDYEEVD
     KERATELMDR LGGMLDGMAG KKFANYEVKY ADDFSYSDPV DHSVSKNQGI RIGFTDGSRI
     VFRLSGTGTK GATLRLYVES YEPDANKHNL ETQAALKPLI DLAQEIAQIK EYTQRDEPTV
     IT
//
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