ID A0A133Q6M4_9BACT Unreviewed; 582 AA.
AC A0A133Q6M4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Putative phosphoglucomutase {ECO:0000313|EMBL:KXA38514.1};
GN ORFNames=HMPREF3226_01607 {ECO:0000313|EMBL:KXA38514.1};
OS Prevotella corporis.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=28128 {ECO:0000313|EMBL:KXA38514.1, ECO:0000313|Proteomes:UP000070533};
RN [1] {ECO:0000313|Proteomes:UP000070533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJR7716 {ECO:0000313|Proteomes:UP000070533};
RA Mitreva M., Pepin K.H., Mihindukulasuriya K.A., Fulton R., Fronick C.,
RA O'Laughlin M., Miner T., Herter B., Rosa B.A., Cordes M., Tomlinson C.,
RA Wollam A., Palsikar V.B., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-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}.
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:KXA38514.1}.
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DR EMBL; LRQG01000113; KXA38514.1; -; Genomic_DNA.
DR RefSeq; WP_025875537.1; NZ_KQ957260.1.
DR AlphaFoldDB; A0A133Q6M4; -.
DR STRING; 28128.HMPREF3226_01607; -.
DR PATRIC; fig|28128.5.peg.1647; -.
DR eggNOG; COG1109; Bacteria.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000070533; 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:UP000070533}.
FT DOMAIN 52..189
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 213..319
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 328..450
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 520..557
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 582 AA; 65545 MW; 12EAC8191E4F4643 CRC64;
MQNNQELITQ CEQKAQQWLT PAFDETTRAA VKSMLDSEDK DTLIESFYKD LEFGTGGLRG
IMGVGSNRMN IYTVGMATQG FANYLKINFK DRKEISVVVC HDCRNNSRLF AETVAKIFSA
NGIKVYLFED LRPTPECSFA IRHFKAQAGV NLTASHNPRE YNGYKAYWED GAQVLSPHDK
GIIDEVNKVK VEDIKFEGND DLIQIIGEDV DKVYLEKVKT VCIDPEVIKR QHDLKIVYTP
LHGAGRVLIP KALRSWGFDN IHCVEEQMVV DGNFPTVDRP NPEIAEALTL GLRDAKKLDA
DILMASDPDA DRVGMACKDS NGEWILINGN QTCLLYLWYI ITNRKAVGKM KPTDFIVKTI
VTTEVITEIA KKQNIEMRDC YTGFKWIAHE IAISEGKQQF IGGGEESYGF MAEDFVRDKD
AVSACALLAE ICAYAKDKGK TLYDLLMDIY LEYGFSEEYT INVERPGKSG AEEIQQMMKN
YRENPPTDLG GSTICTWKDF LKLEEVDADG NKKALVMPAT SNVLQWFCTD GTKVSVRPSG
TEPKIKFYLE IKDTMKTAED YKICRARACE KISAIKKSLG LD
//
