ID K9SEV5_9CYAN Unreviewed; 501 AA.
AC K9SEV5;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE SubName: Full=Phosphoglucomutase/phosphomannomutase alpha/beta/alpha domain I {ECO:0000313|EMBL:AFY69162.1};
GN ORFNames=Pse7367_0862 {ECO:0000313|EMBL:AFY69162.1};
OS Pseudanabaena sp. PCC 7367.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pseudanabaenales;
OC Pseudanabaenaceae; Pseudanabaena.
OX NCBI_TaxID=82654 {ECO:0000313|EMBL:AFY69162.1, ECO:0000313|Proteomes:UP000010386};
RN [1] {ECO:0000313|EMBL:AFY69162.1, ECO:0000313|Proteomes:UP000010386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7367 {ECO:0000313|EMBL:AFY69162.1,
RC ECO:0000313|Proteomes:UP000010386};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished chromosome of genome of Pseudanabaena sp. PCC 7367.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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; CP003592; AFY69162.1; -; Genomic_DNA.
DR RefSeq; WP_015164136.1; NC_019701.1.
DR AlphaFoldDB; K9SEV5; -.
DR STRING; 82654.Pse7367_0862; -.
DR KEGG; pseu:Pse7367_0862; -.
DR PATRIC; fig|82654.3.peg.997; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_7_1_3; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000010386; Chromosome.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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:UP000010386}.
FT DOMAIN 12..148
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 170..285
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 294..402
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 437..489
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 501 AA; 54828 MW; A0DDE9F3A32FE872 CRC64;
MPEEQTLTPP IRFGTDGWRG VIAAEFTFDR LALVAPVAAQ VMAETFGDQS AQPNLIIVGY
DRRFLSPEFA QSVADAVSQA GFDVLLANGY APTPAFSWAA FEQKALGALV ITASHNPAIY
SGLKIKGAFG GSVAPELTKQ VEARVNNPAK FPQPEQRSPG KITSFDPWQS YCAALRTKVD
IDLIREQIRS GELTVFADVM HGAAATGLER ILQVGEKSGA SGSIHELNTI ADPLFGGGAP
EPLPRYMERL LAQIKEFHRQ NPEKLSVGLV FDGDADRIAA VDSAGNFLST QILIPILISH
LAQNRGFSGE LIKTISGADL MPRVAALYDL PTYETPVGYK YIAERMLELK AQGNPPMIGG
EESGGVGYGN HIPERDALLS ALYVLEAIAT AKQDLSDLYQ NLRDKTDYHS EYDRIDKRLS
SLEIKDKLMA YLSANPLDEV AGRKVVAIDS RDGFKFRLAD QSWLLVRFSG TEPVLRLYCE
AATMELVQET LSWISDWVEK F
//
