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Database: UniProt
Entry: Z4WTU6_9PORP
LinkDB: Z4WTU6_9PORP
Original site: Z4WTU6_9PORP 
ID   Z4WTU6_9PORP            Unreviewed;       583 AA.
AC   Z4WTU6;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Putative phosphoglucomutase {ECO:0000313|EMBL:EWC92718.1};
GN   ORFNames=HMPREF0636_0650 {ECO:0000313|EMBL:EWC92718.1};
OS   Porphyromonas catoniae ATCC 51270.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=887901 {ECO:0000313|EMBL:EWC92718.1, ECO:0000313|Proteomes:UP000023482};
RN   [1] {ECO:0000313|EMBL:EWC92718.1, ECO:0000313|Proteomes:UP000023482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51270 {ECO:0000313|EMBL:EWC92718.1,
RC   ECO:0000313|Proteomes:UP000023482};
RA   Durkin A.S., McCorrison J., Torralba M., Gillis M., Haft D.H., Methe B.,
RA   Sutton G., Nelson K.E.;
RL   Submitted (JAN-2014) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EWC92718.1}.
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DR   EMBL; JDFF01000011; EWC92718.1; -; Genomic_DNA.
DR   RefSeq; WP_044168331.1; NZ_JDFF01000011.1.
DR   AlphaFoldDB; Z4WTU6; -.
DR   PATRIC; fig|887901.3.peg.551; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000023482; Unassembled WGS sequence.
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:UP000023482}.
FT   DOMAIN          51..180
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          216..320
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          329..451
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          474..557
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   583 AA;  64828 MW;  1B0A57055AB8ABE6 CRC64;
     MEQNEFLAQV RAKATGWLAP GYDAETRHEV QRMLDNPDTT ELVEAFYKDL EFGTGGLRGI
     MGVGSNRMNR YTVGAATQGL ANYLKREFAS LPQIAVAIGH DCRNNSDVFA RITAEVFSAN
     GIKVYLFDAL RPTPEVSFAI RELGCQSGVM ITASHNPKEY NGYKAYWNDG AQMIAPHDRN
     TIIEVNKVTK VEDIHFDARP ELIELIGEDF DRKFIERVAS LSLPQKESIA RHHDLKIVYT
     PIHGTGVRII PATLRAIGFT NIINVPEQDV VSGNFPTVHS PNPEEPVALE LAIARAEATG
     ADLVLASDPD ADRIGVAVRN NEGKMVLING NEICALLTYY AIASRRDSGR LQPEDYVVKT
     IVTTELIRTI AEQNKVTLFD CYTGFKWIAD VIRQNEGKRN YIGGGEESYG FLREDFIRDK
     SSVSACCMFS ELAAWAKDKG LSIYQLLQQV FLEYGLYKEQ GVSVVRKGKT GAEEIEAMMK
     NFRENPMKSL AGSPVIEILD YAKLEGRWLD KREVFSLDMP TTSNVLQYKT ADGTKVSIRP
     SGTEPKIKFY IGVRGKVSSI EELPSAETAC LNKIATIRQE LGI
//
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