ID A0A096BW63_9BACT Unreviewed; 582 AA.
AC A0A096BW63;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:KGF37324.1};
GN ORFNames=HMPREF2137_00645 {ECO:0000313|EMBL:KGF37324.1};
OS Hoylesella buccalis DNF00853.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Hoylesella.
OX NCBI_TaxID=1401074 {ECO:0000313|EMBL:KGF37324.1, ECO:0000313|Proteomes:UP000029556};
RN [1] {ECO:0000313|EMBL:KGF37324.1, ECO:0000313|Proteomes:UP000029556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DNF00853 {ECO:0000313|EMBL:KGF37324.1,
RC ECO:0000313|Proteomes:UP000029556};
RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JUL-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:KGF37324.1}.
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DR EMBL; JRNN01000008; KGF37324.1; -; Genomic_DNA.
DR RefSeq; WP_036871383.1; NZ_JRNN01000008.1.
DR AlphaFoldDB; A0A096BW63; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000029556; 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; 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 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 Magnesium {ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|RuleBase:RU004326}.
FT DOMAIN 52..189
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 213..318
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"
SQ SEQUENCE 582 AA; 65325 MW; 3A539214865B54C3 CRC64;
MANNAELIAQ CEQKAKQWLA PAFDEETQKE VKAKIEAEDK TDLIDSFYKD LEFGTGGLRG
IMGAGSNRMN IYTVGMATQG FANYLKKNFQ DRTDISVVVC HDCRNNSRKF AESVADIFTA
NGIKVYLFDD MRPTPECSFA IRHLGCQAGV NITASHNPKE YNGYKAYWED GAQVLAPHDM
GIINEVNKVK VEDVKFEGNK QLLQIIGEDI DQAYLDAVKT VSIDPEVIKR QHDLKIVYTP
LHGTGMKMIP RSLKYWGFDN VHCVKEQMVK DGNFPTVVSP NPENGEALTL ALRDAKQLDA
DIVMASDPDA DRVGMACKND KGEWILVNGN QTCLIFLYYI ITNRKNMGML KPTDYIVKTI
VTTEVIRKVA EKNNIEMIDC YTGFKWIARE IRVADPGKKY IGGGEESYGF MAADFVRDKD
AVSAMCLLAE ICAYAKDQGK TLYDLLLDIY LEYGFSKEFT INVVRPGKTG ADEIKTMMEN
FRKNPPTELG GSKVVVRKDY QTLEQRDAKG NVSKLDMPDT SNVLQWFCDD GTKVSVRPSG
TEPKIKFYLE VKGTMKCAGC YERCDAEANE KINAIKKSLH LE
//
