ID   A0A127VCY4_9SPHI        Unreviewed;       577 AA.
AC   A0A127VCY4;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:AMP99165.1};
GN   ORFNames=AY601_2271 {ECO:0000313|EMBL:AMP99165.1};
OS   Pedobacter cryoconitis.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=188932 {ECO:0000313|EMBL:AMP99165.1, ECO:0000313|Proteomes:UP000071561};
RN   [1] {ECO:0000313|EMBL:AMP99165.1, ECO:0000313|Proteomes:UP000071561}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC 27485 {ECO:0000313|EMBL:AMP99165.1,
RC   ECO:0000313|Proteomes:UP000071561};
RA   Lee J., Kim O.-S.;
RT   "Complete genome sequence of Pedobacter cryoconitis PAMC 27485.";
RL   Submitted (MAR-2016) 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; CP014504; AMP99165.1; -; Genomic_DNA.
DR   RefSeq; WP_068400734.1; NZ_CP014504.1.
DR   AlphaFoldDB; A0A127VCY4; -.
DR   KEGG; pcm:AY601_2271; -.
DR   PATRIC; fig|188932.3.peg.2379; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000071561; 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:UP000071561}.
FT   DOMAIN          48..186
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          210..312
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          509..545
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   577 AA;  63654 MW;  20FD639C05134A2E CRC64;
     MQLEAAIQNT INEWLNGNYD QQTKEEIQKL IDSEASTELV DSFYRSLEFG TGGLRGIMGA
     GSNRINKYTI GTATQGLSNY LLKKYPGEQI KVAIAHDSRN QSDFFAKITA DVFSANGIHV
     YFFKELRPTP ELSFAIRHLG CRSGVMLTAS HNPKEYNGYK AYGADGGQFT SPDDNMVMDE
     VANIKSIDEV KFERNDKLVE LIGEEIDTLY LDQITALSVS PEAIARQKDL KIVYSPIHGT
     GITLVPKALA QFGFTNLTLV KEQSTPDGNF PTVVYPNPEE KEAMTLALNK AKEIDADLVL
     ATDPDADRVG IAVKNSDGEF VLLNGNQTGS LLINYLLTAW QEKGKLDGNQ YIVKTIVTTN
     LVEEIAKAKN VEYFNTLTGF KHIGHLITSL QGKKTFIGGG EESYGYLIGE LVRDKDAIIS
     CAFIAEMTAF YKDKGSSLYD AMLDMYVEYG LYKEELVSLT KKGKTGAEEI KAMMEKFRNN
     PPLELGGSKV KTLKDYELGV ETNLDTKEKT KLDFPVSDVL QFITEDGSIV SARPSGTEPK
     IKFYCSVNAP LADKAQFKTV DAALGAKIKS LMDDLQA
//