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Database: UniProt
Entry: A9WL72_RENSM
LinkDB: A9WL72_RENSM
Original site: A9WL72_RENSM 
ID   A9WL72_RENSM            Unreviewed;       470 AA.
AC   A9WL72;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:ABY21786.1};
DE            EC=5.4.2.2 {ECO:0000313|EMBL:ABY21786.1};
DE            EC=5.4.2.8 {ECO:0000313|EMBL:ABY21786.1};
GN   OrderedLocusNames=RSal33209_0028 {ECO:0000313|EMBL:ABY21786.1};
OS   Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 /
OS   NBRC 15589 / NCIMB 2235).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Renibacterium.
OX   NCBI_TaxID=288705 {ECO:0000313|EMBL:ABY21786.1, ECO:0000313|Proteomes:UP000002007};
RN   [1] {ECO:0000313|Proteomes:UP000002007}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235
RC   {ECO:0000313|Proteomes:UP000002007};
RX   PubMed=18723615; DOI=10.1128/JB.00721-08;
RA   Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., Chen D.S.,
RA   Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H.,
RA   Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.;
RT   "Genome sequence of the fish pathogen Renibacterium salmoninarum suggests
RT   reductive evolution away from an environmental Arthrobacter ancestor.";
RL   J. Bacteriol. 190:6970-6982(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}.
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DR   EMBL; CP000910; ABY21786.1; -; Genomic_DNA.
DR   RefSeq; WP_012243494.1; NC_010168.1.
DR   AlphaFoldDB; A9WL72; -.
DR   STRING; 288705.RSal33209_0028; -.
DR   KEGG; rsa:RSal33209_0028; -.
DR   eggNOG; COG1109; Bacteria.
DR   HOGENOM; CLU_016950_9_2_11; -.
DR   Proteomes; UP000002007; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd03089; PMM_PGM; 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; IPR005841; Alpha-D-phosphohexomutase_SF.
DR   PANTHER; PTHR43771; PHOSPHOMANNOMUTASE; 1.
DR   PANTHER; PTHR43771:SF1; PHOSPHOMANNOMUTASE; 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.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:ABY21786.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002007}.
FT   DOMAIN          13..140
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          163..267
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          285..385
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          391..469
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   470 AA;  50283 MW;  0D789CD05FE3DB66 CRC64;
     MSSNETPLDL SASFKAYDVR GIVGESITAP MVEAIGAAFV DVLNLSGQTV LVGGDMRPSS
     PEFCQAFAHG ANLRGADVKL LDFISTDELY FASGHFSAAG AMFTASHNPA EYNGIKMTQP
     GAVPLSSESG LQEIQELTAK YLAEGIPAAE KPGQMGVRDV LEDYSRYLRS LVDLSGSRPL
     KVVVDAGNGM AGLTTPAVLG DQLLKALPLE IVPMYFELDG TFPNHEANPL EPANLVDLQA
     AVVKHGADIG LAFDGDADRC FVIDEKGDPV SPSAVTGLVA RREIARAKAA GEEHPAIIHN
     LITSRAVPEL VIADGGRPVR TRVGHSFIKA VMAEEGAVFG GEHSAHYYFR DFYNADTGML
     AAMHVLAALG EQSLPLSELG AEYEPYVSSG EINSKIEDKA AAVSRVHEIY AREDVTVDEL
     DGVTFSANSG DWWFNLRPSN TEPYLRFNGE AKDRATLEEL RDAVLALVRS
//
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