ID A0A0N9N4W6_9ACTN Unreviewed; 546 AA.
AC A0A0N9N4W6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:ALG85502.1};
DE EC=5.4.2.2 {ECO:0000313|EMBL:ALG85502.1};
GN ORFNames=ACH46_14775 {ECO:0000313|EMBL:ALG85502.1};
OS Gordonia phthalatica.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1136941 {ECO:0000313|EMBL:ALG85502.1, ECO:0000313|Proteomes:UP000063789};
RN [1] {ECO:0000313|Proteomes:UP000063789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QH-11 {ECO:0000313|Proteomes:UP000063789};
RA Jin D., Kong X., Bai Z.;
RT "Complete genome sequence and metabolic analysis of phthalate degradation
RT pathway in Gordonia sp. QH-11.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ALG85502.1, ECO:0000313|Proteomes:UP000063789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QH-11 {ECO:0000313|EMBL:ALG85502.1,
RC ECO:0000313|Proteomes:UP000063789};
RX PubMed=29068282; DOI=10.1099/ijsem.0.002430;
RA Jin D., Kong X., Jia M., Yu X., Wang X., Zhuang X., Deng Y., Bai Z.;
RT "Gordonia phthalatica sp. nov., a di-n-butyl phthalate-degrading bacterium
RT isolated from activated sludge.";
RL Int. J. Syst. Evol. Microbiol. 67:5128-5133(2017).
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; CP011853; ALG85502.1; -; Genomic_DNA.
DR RefSeq; WP_062393590.1; NZ_CP011853.1.
DR AlphaFoldDB; A0A0N9N4W6; -.
DR STRING; 1136941.ACH46_14775; -.
DR KEGG; goq:ACH46_14775; -.
DR PATRIC; fig|1136941.3.peg.3018; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000063789; 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:ALG85502.1};
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}.
FT DOMAIN 39..180
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 210..316
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 491..540
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 546 AA; 57676 MW; A3B0B526C6E6690A CRC64;
MAHPRAGTPA TADDLIDVAA VENAYYEIKP DPANPDQRVV FGTSGHRGSS LDGAFNEAHV
LAMTQAIVEH REKAGIEGPL FIGFDTHALS IPAWRSALEV LVGNGVSVFT ADEDQFTPTP
AVSRAILRFN RENPGVQADG IVVTPSHNPP ADGGFKYNPP SGGPADSTIT SVVAARANEI
LEEGLLAVQR VPFERARISE LVIDYPFLGE YVTALGEVVN IDAIRAADVR IGADPLGGAS
VAYWGEIKDY YGLDSMTVVN PNTDPAFGFM TLDTDGKIRM DCSSPNAMAS LIAARESYDI
ATGNDADSDR HGIVTSDAGL MNPNHYLAVA IDYLFTHREG WSEAAAIGKT LVSSSLIDRV
AAGIGRPLVE VPVGFKFFVD GLLDGTIAFG GEESAGASFL TFDGRPWSTD KDGIIMNLLA
SEILAVTGET PSERYVDLAE KYGASAYSRI DAPADREQKA RLAKLSASQV SASELAGEPI
TAILTEAPGN GAAIGGLKVT TENAWFAARP SGTEDVYKIY AESFRGADHL AQVQAEAQAL
VDSVLG
//
