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Database: UniProt
Entry: A9G2L2_SORC5
LinkDB: A9G2L2_SORC5
Original site: A9G2L2_SORC5 
ID   A9G2L2_SORC5            Unreviewed;       563 AA.
AC   A9G2L2;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   SubName: Full=Pgm3 protein {ECO:0000313|EMBL:CAN95661.1};
DE            EC=5.4.2.2 {ECO:0000313|EMBL:CAN95661.1};
GN   Name=pgm3 {ECO:0000313|EMBL:CAN95661.1};
GN   OrderedLocusNames=sce5498 {ECO:0000313|EMBL:CAN95661.1};
OS   Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So
OS   ce56)).
OC   Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae; Sorangium.
OX   NCBI_TaxID=448385 {ECO:0000313|EMBL:CAN95661.1, ECO:0000313|Proteomes:UP000002139};
RN   [1] {ECO:0000313|EMBL:CAN95661.1, ECO:0000313|Proteomes:UP000002139}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=So ce56 {ECO:0000313|Proteomes:UP000002139};
RX   PubMed=17965706; DOI=10.1038/nbt1354;
RA   Schneiker S., Perlova O., Kaiser O., Gerth K., Alici A., Altmeyer M.O.,
RA   Bartels D., Bekel T., Beyer S., Bode E., Bode H.B., Bolten C.J.,
RA   Choudhuri J.V., Doss S., Elnakady Y.A., Frank B., Gaigalat L., Goesmann A.,
RA   Groeger C., Gross F., Jelsbak L., Jelsbak L., Kalinowski J., Kegler C.,
RA   Knauber T., Konietzny S., Kopp M., Krause L., Krug D., Linke B., Mahmud T.,
RA   Martinez-Arias R., McHardy A.C., Merai M., Meyer F., Mormann S.,
RA   Munoz-Dorado J., Perez J., Pradella S., Rachid S., Raddatz G., Rosenau F.,
RA   Rueckert C., Sasse F., Scharfe M., Schuster S.C., Suen G.,
RA   Treuner-Lange A., Velicer G.J., Vorholter F.-J., Weissman K.J., Welch R.D.,
RA   Wenzel S.C., Whitworth D.E., Wilhelm S., Wittmann C., Bloecker H.,
RA   Puehler A., Mueller R.;
RT   "Complete genome sequence of the myxobacterium Sorangium cellulosum.";
RL   Nat. Biotechnol. 25:1281-1289(2007).
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; AM746676; CAN95661.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9G2L2; -.
DR   STRING; 448385.sce5498; -.
DR   KEGG; scl:sce5498; -.
DR   eggNOG; COG0033; Bacteria.
DR   HOGENOM; CLU_016950_8_1_7; -.
DR   OrthoDB; 9806956at2; -.
DR   BioCyc; SCEL448385:SCE_RS28210-MONOMER; -.
DR   Proteomes; UP000002139; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd05801; PGM_like3; 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; IPR005852; PGM_a-D-Glc-sp.
DR   NCBIfam; TIGR01132; pgm; 1.
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   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, ECO:0000313|EMBL:CAN95661.1};
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:UP000002139}.
FT   DOMAIN          55..195
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          226..330
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          337..456
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          505..555
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
FT   REGION          45..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   563 AA;  60512 MW;  3B24F8094D754B11 CRC64;
     MEGLARPARS TMRRLMPLHP LAGRKAPPDV LIDPDKLRAQ YYSERPDMGD PQQRVAFGTS
     GHRGSAARRS FNEAHVLAVA QAICDYRAKE GTTGSLYLGM DTHALSEPAQ RSVIEVFAAN
     GVDVLIAERN GVTPTPAISH AILTANRGRT SGLADGVVIT PSHNPPDDGG IKYNPPNGGP
     ADTAVTGWIE ERANELLRAD NAGVKRTPYE AALRAPTTHP YDFIGPYVAD LGNVVDLEAV
     RGAKLRIGVD PLGGSNIAYW APIAEKFGLD ITVVNQAVDP TFSFMPLDHD GKIRMDCSSP
     HAMANLIALK DDYDLAFGND ADSDRHGIVT RSAGLMNPNH YLAVAVSYLF RNRPLWRPDA
     AVGKTLVSSS MIDRVAKDLG RPLREVPVGF KWFVDGLLDG SLGFGGEESA GASFLRKNGQ
     VWSTDKDGIL LDLLAAEILA RTGRDPAEHY RDLTARFGAP IYTRIDAPAT PSQKSVLKKL
     SPDAVRAETL AGEPITAKLT RAPGNGGEIG GLKVVAENGW FAARPSGTED VYKIYAESFK
     DQAHLDRVLD EARAMVTDAL SAK
//
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