ID A0A147E6U3_9MICC Unreviewed; 544 AA.
AC A0A147E6U3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Alpha-D-glucose phosphate-specific phosphoglucomutase {ECO:0000313|EMBL:QPT54171.1};
DE EC=5.4.2.2 {ECO:0000313|EMBL:QPT54171.1};
DE SubName: Full=Phosphoglucomutase, alpha-D-glucose phosphate-specific {ECO:0000313|EMBL:OAX52063.1};
GN ORFNames=AN277_0205270 {ECO:0000313|EMBL:OAX52063.1}, I6G21_02990
GN {ECO:0000313|EMBL:QPT54171.1};
OS Rothia kristinae.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Rothia.
OX NCBI_TaxID=37923 {ECO:0000313|EMBL:QPT54171.1, ECO:0000313|Proteomes:UP000594975};
RN [1] {ECO:0000313|Proteomes:UP000053171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RuSp02-3 {ECO:0000313|Proteomes:UP000053171};
RA Waterworth S., Matcher G.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OAX52063.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RUTW2-3 {ECO:0000313|EMBL:OAX52063.1};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:OAX52063.1, ECO:0000313|Proteomes:UP000053171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RuSp02-3 {ECO:0000313|Proteomes:UP000053171}, and RUTW2-3
RC {ECO:0000313|EMBL:OAX52063.1};
RA Waterworth S.C., Walmsley T.A., Matongo T., Davies-Coleman M.T.,
RA Dorrington R.A.;
RT "Identification of putative biosynthetic pathways for the production of
RT bioactive secondary metabolites by the marine actinomycete Kocuria
RT kristinae RUTW2-3.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:QPT54171.1, ECO:0000313|Proteomes:UP000594975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FDAARGOS_864 {ECO:0000313|EMBL:QPT54171.1,
RC ECO:0000313|Proteomes:UP000594975};
RA Sproer C., Gronow S., Severitt S., Schroder I., Tallon L., Sadzewicz L.,
RA Zhao X., Boylan J., Ott S., Bowen H., Vavikolanu K., Mehta A.,
RA Aluvathingal J., Nadendla S., Lowell S., Myers T., Yan Y., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (DEC-2020) 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}.
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DR EMBL; LJBJ02000008; OAX52063.1; -; Genomic_DNA.
DR EMBL; CP065738; QPT54171.1; -; Genomic_DNA.
DR RefSeq; WP_058730394.1; NZ_NOIV01000002.1.
DR AlphaFoldDB; A0A147E6U3; -.
DR GeneID; 44526774; -.
DR KEGG; rkr:I6G21_02990; -.
DR PATRIC; fig|37923.10.peg.1282; -.
DR Proteomes; UP000053171; Unassembled WGS sequence.
DR Proteomes; UP000594975; 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:QPT54171.1};
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:UP000053171}.
FT DOMAIN 38..178
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 208..314
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 320..440
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 489..538
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 544 AA; 58370 MW; A9847B1428F0C3CC CRC64;
MSDRAGTPAQ PQDLVDIEEL LTAYRERVPD AEDPAQRVAF GTSGHRGSAL SGSFNEAHIA
AITQAIVEYR TEQGIDGPLF MGRDTHALSG PAQETALEVL AAHGVVVLLD ARDGYVPTPA
LSRAILVHNA RPGASQADGI VITPSHNPPT DGGFKYNPPH GGPAGAEATG WIQDRANELL
ADGNRGVRRV PYAQAKLAET TQTYDYLDAY VSELPEVVDL EAIRKAGVRI GADPMGSASV
EYWKEIGRRY GLELTVVNPD VDPQWGFMTL DWDGKIRMDC SSPHAMASLI ANRDSYDIAT
GNDADSDRHG IVTPDAGLMN PNHFLTVAID YLYRHRPDWP GDAGVGKTLV SSSMIDRVAE
DLGRTLVEVP VGFKHFVDGL LAGTLGFGGE ESAGASFLRR DGAVWTTDKD GIILALLASE
ILAVTGKTPS QRYAELTERF GDPAYERIDA PATRDQKARL KQLSAEDVTV EELAGEPITA
TLTVAPGNGE PLGGLKVVTE SAWFAARPSG TEDVYKIYAE SFRGPEHLRQ VQAEAKRLVD
GVIG
//
