ID   A0A1V9FX93_9BACT        Unreviewed;       459 AA.
AC   A0A1V9FX93;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Phosphoglucosamine mutase {ECO:0000313|EMBL:OQP62940.1};
GN   ORFNames=A4R26_17320 {ECO:0000313|EMBL:OQP62940.1};
OS   Niastella populi.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Niastella.
OX   NCBI_TaxID=550983 {ECO:0000313|EMBL:OQP62940.1, ECO:0000313|Proteomes:UP000192276};
RN   [1] {ECO:0000313|Proteomes:UP000192276}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=208 {ECO:0000313|Proteomes:UP000192276};
RA   Chen L., Zhuang W., Wang G.;
RL   Submitted (APR-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:OQP62940.1}.
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DR   EMBL; LWBP01000112; OQP62940.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V9FX93; -.
DR   STRING; 550983.A4R26_17320; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000192276; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0008966; F:phosphoglucosamine mutase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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   InterPro; IPR024086; GlmM_arc-type.
DR   NCBIfam; TIGR03990; Arch_GlmM; 1.
DR   PANTHER; PTHR42946:SF1; PHOSPHOGLUCOMUTASE (ALPHA-D-GLUCOSE-1,6-BISPHOSPHATE-DEPENDENT); 1.
DR   PANTHER; PTHR42946; PHOSPHOHEXOSE MUTASE; 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:UP000192276}.
FT   DOMAIN          8..140
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          161..262
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          269..364
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          400..451
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   459 AA;  49923 MW;  3ADEA69BCB42E8CC CRC64;
     MALIKSISGI RGTIGGKTGE NLTPLDVVKF SAAFGSWLLE KNSGNKIVIG RDGRISGAMV
     QQLVVNTLTG LGIDVVDIGL STTPTVEMAV VWENAAGGII ITASHNPKEW NALKLLNARG
     EFISGEDGAQ VLEKAGKEEF NFVSVDKLGA YTVNDTYLQK HIDTIVNYPL VDVESIRQKN
     YKVVVDVVNS TGALAIPPLL TALGIEEVIV LNEEITGKFA HNPEPLPENL TGLSGAVRKH
     KADLGIAVDP DVDRLCFVCE DGSMFGEEYT LVAVADYVLG KKVGNTVSNM SSTKALKEIT
     LKHGGEYYPS AVGEVNVVDK MKAVNAVIGG EGNGGIIVPD LHYGRDALIG IGLFLSSLAT
     HKNGIRSFRT RYPDYFISKN KIELQNGIDV KDIFEKIKTK YRNQPVNTED GLKIEFDSDW
     VHLRTSNTEP IIRIYAESSF ETTANNIALR LMHDIKEFM
//