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Database: UniProt
Entry: A0A0A0BU16_9CELL
LinkDB: A0A0A0BU16_9CELL
Original site: A0A0A0BU16_9CELL 
ID   A0A0A0BU16_9CELL        Unreviewed;       558 AA.
AC   A0A0A0BU16;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:KGM11172.1};
DE            EC=5.4.2.2 {ECO:0000313|EMBL:KGM11172.1};
GN   ORFNames=N869_03595 {ECO:0000313|EMBL:KGM11172.1};
OS   Cellulomonas bogoriensis 69B4 = DSM 16987.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=1386082 {ECO:0000313|EMBL:KGM11172.1, ECO:0000313|Proteomes:UP000054314};
RN   [1] {ECO:0000313|EMBL:KGM11172.1, ECO:0000313|Proteomes:UP000054314}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=69B4 {ECO:0000313|EMBL:KGM11172.1,
RC   ECO:0000313|Proteomes:UP000054314};
RA   Chen F., Li Y., Wang G.;
RT   "Genome sequencing of Cellulomonas bogoriensis 69B4.";
RL   Submitted (AUG-2013) 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}.
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:KGM11172.1}.
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DR   EMBL; AXCZ01000122; KGM11172.1; -; Genomic_DNA.
DR   RefSeq; WP_035061400.1; NZ_AXCZ01000122.1.
DR   AlphaFoldDB; A0A0A0BU16; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000054314; Unassembled WGS sequence.
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:KGM11172.1};
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:UP000054314}.
FT   DOMAIN          38..189
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          219..327
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          333..452
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          504..552
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   558 AA;  58191 MW;  DFE653A57BCE2187 CRC64;
     MHPRAGTPAQ PEDLIDVDAL VGAYYDRTPD LDDPGQRVAF GTSGHRGSSL DGAFNEAHII
     ATTAAIVEYR RGQGTDGPLF IGRDTHALSE PAFRTALEVL AAAEVDVHVD ARDGYTPTPA
     VSHAILLHNG SATQEGVRTG AGGSGLADGI VVTPSHNPPR DGGFKYNPPH GGPAGSEATS
     WIAARANEIL RQGVGGVRRL QPDAAMAAPA THRHDYLSAY VADLPHVLDL DLVRATGVRI
     GADPLGGAAV DYWGEIAERH GLDLTVVNPQ VDPRWSFMTL DWDGKIRMDC SSPSAMASLV
     HAMSGDAPFD VATGNDADAD RHGIVTPDAG LMNPNHYLAV AIDYLYGGAR PGWPAGAAIG
     KTLVSSALID RVAAHLGRDL LEVPVGFKHF VPGLLDGTVG FGGEESAGAS FLRTDGTVWT
     TDKDGIILAL LAAEITARTG RSPSQLHAGL VERHGRSWYA RVDAPATREQ KAALGALDAG
     QVTASTLAGE PITGRLTSAP GNGAAIGGLK VTTDNAWFAA RPSGTEDVYK IYAESFVSAE
     HLTEVQAAAK DLVTQTLG
//
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