ID A0A0P0NIX4_9SPHI Unreviewed; 577 AA.
AC A0A0P0NIX4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:ALL07125.1};
GN ORFNames=AQ505_17510 {ECO:0000313|EMBL:ALL07125.1};
OS Pedobacter sp. PACM 27299.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1727164 {ECO:0000313|EMBL:ALL07125.1, ECO:0000313|Proteomes:UP000062859};
RN [1] {ECO:0000313|EMBL:ALL07125.1, ECO:0000313|Proteomes:UP000062859}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC 27299 {ECO:0000313|EMBL:ALL07125.1,
RC ECO:0000313|Proteomes:UP000062859};
RA Gilbert D.G.;
RL Submitted (OCT-2015) 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; CP012996; ALL07125.1; -; Genomic_DNA.
DR RefSeq; WP_062549363.1; NZ_CP012996.1.
DR AlphaFoldDB; A0A0P0NIX4; -.
DR STRING; 1727164.AQ505_17510; -.
DR KEGG; pep:AQ505_17510; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000062859; Chromosome.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd05799; PGM2; 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; IPR005841; Alpha-D-phosphohexomutase_SF.
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 PRINTS; PR00509; PGMPMM.
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:UP000062859}.
FT DOMAIN 48..186
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 210..315
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 324..444
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 516..546
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 577 AA; 63706 MW; 79F15177D1398134 CRC64;
MQLEAATLST INQWLNGNYD SKTKEEIQQL LDKEAFTELT DSFYRSLEFG TGGLRGIMGA
GSNRINKYTI GTATQGLCNY LNNKYPNEKI KVAIAHDSRN NSDYFAGITA DVFTANGIHV
YFFKALRPTP ELSFAIRELG CKSGVMLTAS HNPKEYNGYK AYGADGGQFT SPDDTMVMDE
VAKIKNIDEV KFDRIDSNFE LIGEEIDQLY LDKITELSVS PEAIARQKDL KIVFSPIHGT
GITLVPQALA QFGFTNLTLV EEQSTPDGNF PTVVYPNPEE KEALTLALKK AEEIDADLVL
ATDPDADRVG IAVKNNDGQF VLLNGNQTGS LLINYLLSAW EEKGKLTGDQ YIVKTIVTTN
IIEEIAKKKN VTFYNTLTGF KFIGQLMTSL EGKKTFIGGG EESYGYLIGE LVRDKDAVVS
CAFIAEMTAF YKDKGSSLYN AMLDMYVEYG LYKEELVSIT KKGKTGAEEI KAMMEKFRSN
PPATLGGAKV VLLKDYELGF ETNLSTAEKT KLDFPKSDVL QFITEDGSIV SARPSGTEPK
IKFYCSVNTT LKDKASFKET DALLGDKIKA VMKDLEA
//