ID A3Z9M5_9SYNE Unreviewed; 552 AA.
AC A3Z9M5;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 80.
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=RS9917_07625 {ECO:0000313|EMBL:EAQ68299.1};
OS Synechococcus sp. RS9917.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=221360 {ECO:0000313|EMBL:EAQ68299.1, ECO:0000313|Proteomes:UP000005593};
RN [1] {ECO:0000313|EMBL:EAQ68299.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS9917 {ECO:0000313|EMBL:EAQ68299.1};
RA Scanlan D., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (JAN-2006) 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:EAQ68299.1}.
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DR EMBL; AANP01000006; EAQ68299.1; -; Genomic_DNA.
DR RefSeq; WP_007101497.1; NZ_CH724158.1.
DR AlphaFoldDB; A3Z9M5; -.
DR STRING; 221360.RS9917_07625; -.
DR eggNOG; COG0033; Bacteria.
DR HOGENOM; CLU_009330_0_1_3; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000005593; 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 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; 2.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|RuleBase:RU004326}.
FT DOMAIN 23..162
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 194..295
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 304..416
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 552 AA; 58989 MW; BCB4F7218AE4D024 CRC64;
MTTSAPAEPT QRQVRLDAPF TDQKPGTSGL RKSSQQFEQP HYLESFVEAV FRTLPGVQGG
TLVVGGDGRY GNRRAIDVIL RMGAAHGLSQ VILTTGGILS TPAASNLIRQ RQAIGGIILS
ASHNPGGPNG DFGVKVNGAN GGPTPAAFTD AVFACTTTLE QYSIVDAAPI PLEAPGRHTI
GTMTVEVIDG VEDFVALMQQ LFDFDRIRDL IRSDFPLAFD AMHAVTGPYA TRLFEELLGA
PAGSVRNGVP LEDFGGGHPD PNLTYAHELA DLLLNGEAYR FGAACDGDGD RNMILGQHCF
VNPSDSLAVL TANATVAPAY AAGLAGVARS MPTSAAVDVV AKDLGIDCYE TPTGWKFFGN
LLDAGRITLC GEESFGTGSN HVREKDGLWA VLFWLQILAE RRCSVAEIMA AHWARFGRHY
YSRHDYEAVP SDAAHGLYER LEAMLPALRG QDFAGRRIQA ADNFSYTDPV DGSVTTGQGL
RILLDDGSRV VVRLSGTGTK GATIRVYLES YVPSSGDLHQ DPQVALADMI EAINQLAEIQ
VRTGMDRPTV IT
//
