ID A0A2S1LD65_9FLAO Unreviewed; 575 AA.
AC A0A2S1LD65;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:AWG21641.1};
GN ORFNames=FFWV33_08880 {ECO:0000313|EMBL:AWG21641.1};
OS Flavobacterium faecale.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1355330 {ECO:0000313|EMBL:AWG21641.1, ECO:0000313|Proteomes:UP000244527};
RN [1] {ECO:0000313|EMBL:AWG21641.1, ECO:0000313|Proteomes:UP000244527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WV33 {ECO:0000313|EMBL:AWG21641.1,
RC ECO:0000313|Proteomes:UP000244527};
RA Lee P.C.;
RT "Compelte genome sequence of WV33.";
RL Submitted (APR-2017) 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; CP020918; AWG21641.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S1LD65; -.
DR KEGG; ffa:FFWV33_08880; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000244527; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000244527}.
FT DOMAIN 47..184
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 209..313
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 322..443
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 575 AA; 63359 MW; 1E2175C21177FB21 CRC64;
MEIKQNILDA ANEWLSPVFD TKTQEEVQAL IANSPKELEE SFYKSLEFGT GGMRGTMGAG
DNRINKYTLG KSTQGLSDYL RTFFPNQPLK AVIAYDCRHN SDTLAKVVAD VFSANGIEVY
LFSSLRPTPE LSFAVKHLNC HCGIVLTASH NPPEYNGYKV YWQDGGQIVP PEDGAIINVI
ENLKYNQIKF EANESLIHYI GEEVDKAFID STIANASFDT PAAAKDDLNI VFTSLHGTSI
TVTPQTLAQA GYKNVNIVEE QAEPNGDFPT VKSPNPEEPE ALKMATELAN KINADIVIGT
DPDCDRLGVA VRNNDGQMTL LNGNQTMILM TAFLLEKWKL AGKLNGKQFI ASTIVSTPMV
MELATAYDVE YKSGLTGFKW IAKMVKDFPE SQFIGGGEES FGFMVGDAVR DKDAVASTLL
ICEVAAQAKA KGSSAYNELI QHYVDFGFYK EHLISLTKKG MDGLAEITQM MVDLRENPIK
EISGQRVVMV EDYKASTAKN LLTGEVETLT MPKADVLIYY TEDGSKICAR PSGTEPKIKF
YISVNTELES VEKFAETDAY LNEKIQNIIT GMQLN
//