ID E4MD36_9BACT Unreviewed; 580 AA.
AC E4MD36;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II {ECO:0000313|EMBL:EFR57194.1};
DE EC=5.4.2.2 {ECO:0000313|EMBL:EFR57194.1};
GN Name=pgcA {ECO:0000313|EMBL:EFR57194.1};
GN ORFNames=HMPREF9720_1273 {ECO:0000313|EMBL:EFR57194.1};
OS Alistipes sp. HGB5.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Alistipes.
OX NCBI_TaxID=908612 {ECO:0000313|EMBL:EFR57194.1, ECO:0000313|Proteomes:UP000002960};
RN [1] {ECO:0000313|EMBL:EFR57194.1, ECO:0000313|Proteomes:UP000002960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HGB5 {ECO:0000313|EMBL:EFR57194.1,
RC ECO:0000313|Proteomes:UP000002960};
RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (NOV-2010) 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:EFR57194.1}.
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DR EMBL; AENZ01000057; EFR57194.1; -; Genomic_DNA.
DR RefSeq; WP_009598259.1; NZ_AENZ01000057.1.
DR AlphaFoldDB; E4MD36; -.
DR PATRIC; fig|908612.3.peg.2077; -.
DR eggNOG; COG1109; Bacteria.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000002960; Unassembled WGS sequence.
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; 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, ECO:0000313|EMBL:EFR57194.1};
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}.
FT DOMAIN 49..186
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 211..316
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 325..451
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 518..559
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 580 AA; 64713 MW; 33295DB8B31AAF45 CRC64;
MANELEQSVL KKAQAWLDGH YDEATKKQVK YLMDNDMKEL VESFYKDLEF GTGGLRGIMG
VGSNRMNVYT VGAATQGLAN YLRKNFAGEQ IRVAVGHDSR NNSRMFAERV ADIFASNGFT
VFLFDALRPT PELSFAIREL KCHSGVVVTA SHNPKEYNGY KAYWTDGAQV TEPHDKNIIA
EVAKITDVNM IQLGKNPQNI TILDEKFDEI YLNKVHELSL SPESVKKHHD MKIIYTPLHG
SGVRLVPESL KKFGFTNVKL VPEQAVIDGN FPTVESPNPE ERKTMSMAID LAAKEGADLV
LATDPDSDRI GVALRNKKGE YVLLNGNQTL VLLLSYQLTR WAERGKLDGN QYVVKTIVTS
QMANAVADYF KVKCYDCLTG FKYIAKIIRE NEGKAKYIGG GEESFGYLAG DYVRDKDAVS
ACSLAAEAAA WAMDTMGLTL YEWLQELYVK YGFFREGLVS VVRKGKEGAE LIQKMMVEFR
ENPPKTIVGS PVVKINDFLS LETTDVKSGS KTPIEQDKSN VLQWFTEDGS IVSVRPSGTE
PKIKFYFGVK APLESVADFE RVQAELDAKI EAIKKDLKLE
//
