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Database: UniProt
Entry: D0LE45_GORB4
LinkDB: D0LE45_GORB4
Original site: D0LE45_GORB4 
ID   D0LE45_GORB4            Unreviewed;       547 AA.
AC   D0LE45;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=Phosphoglucomutase, alpha-D-glucose phosphate-specific {ECO:0000313|EMBL:ACY22637.1};
GN   OrderedLocusNames=Gbro_3442 {ECO:0000313|EMBL:ACY22637.1};
OS   Gordonia bronchialis (strain ATCC 25592 / DSM 43247 / BCRC 13721 / JCM 3198
OS   / KCTC 3076 / NBRC 16047 / NCTC 10667) (Rhodococcus bronchialis).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=526226 {ECO:0000313|EMBL:ACY22637.1, ECO:0000313|Proteomes:UP000001219};
RN   [1] {ECO:0000313|Proteomes:UP000001219}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25592 / DSM 43247 / BCRC 13721 / JCM 3198 / KCTC 3076 /
RC   NBRC 16047 / NCTC 10667 {ECO:0000313|Proteomes:UP000001219};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Ovchinnikova G., Saunders E., Brettin T., Detter J.C., Han C., Larimer F.,
RA   Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T.,
RA   Wu D., Jando M., Schneider S., Goeker M., Klenk H.-P., Eisen J.A.;
RT   "The complete chromosome of Gordonia bronchialis DSM 43247.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACY22637.1, ECO:0000313|Proteomes:UP000001219}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25592 / DSM 43247 / BCRC 13721 / JCM 3198 / KCTC 3076 /
RC   NBRC 16047 / NCTC 10667 {ECO:0000313|Proteomes:UP000001219};
RX   PubMed=21304674;
RA   Ivanova N., Sikorski J., Jando M., Lapidus A., Nolan M., Lucas S.,
RA   Del Rio T.G., Tice H., Copeland A., Cheng J.F., Chen F., Bruce D.,
RA   Goodwin L., Pitluck S., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P.,
RA   Saunders E., Han C., Detter J.C., Brettin T., Rohde M., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P.,
RA   Kyrpides N.C.;
RT   "Complete genome sequence of Gordonia bronchialis type strain (3410).";
RL   Stand. Genomic Sci. 2:19-28(2010).
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; CP001802; ACY22637.1; -; Genomic_DNA.
DR   RefSeq; WP_012835151.1; NC_013441.1.
DR   AlphaFoldDB; D0LE45; -.
DR   STRING; 526226.Gbro_3442; -.
DR   KEGG; gbr:Gbro_3442; -.
DR   eggNOG; COG0033; Bacteria.
DR   HOGENOM; CLU_016950_8_1_11; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000001219; Chromosome.
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   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};
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:UP000001219}.
FT   DOMAIN          39..180
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          211..318
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          322..442
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          490..538
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   547 AA;  58075 MW;  50EC84558FF4CF36 CRC64;
     MAHPRAGTPA LPEDLIDVAA IERAYYDNVP DPSDPLQQVL FGTSGHRGSS LDNAFNEAHI
     LATTQAIVEY RRGAGITGPL FIGFDTHALS IPAWRTALEV LAANEISTYT AEGDSFTPTP
     AVSRAILTFN RDNPGVLADG IVVTPSHNPP RDGGFKYNPP SGGPADTSIT SVVAARANEI
     LANKLADVRR IPFEQARSGD YVHDFSFMMN YCDGLGEVVD LNVIREAGIH IGADPLGGAS
     VGYWAGIGFR YNLENLTVVN PTVDPTFSFM TLDTDGKIRM DCSSPNAMAS LISAREHYDI
     ATGNDADSDR HGIVTPDGGL MNPNHYLAVA IDYLFTHRPG WAESAAVGKT LVSSSLIDRV
     VAGIGRRLLE VPVGFKWFVD GLLDGSIAFG GEESAGASFL MFDGSPWTTD KDGIILALLA
     SEILAVTGKT PSERYRELAE RYGESAYARV DAPASREQKA VLAKLSASQV SATELAGEPI
     TAIMTEAPGN GAPIGGLKVT TENAWFAARP SGTEDVYKIY AESFKGAEHL AQVQTEAQQV
     VDAALGG
//
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