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Database: UniProt
Entry: A0A0K9Y1P8_9FLAO
LinkDB: A0A0K9Y1P8_9FLAO
Original site: A0A0K9Y1P8_9FLAO 
ID   A0A0K9Y1P8_9FLAO        Unreviewed;       460 AA.
AC   A0A0K9Y1P8;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Phosphoglucosamine mutase {ECO:0000313|EMBL:KNB62145.1};
GN   ORFNames=AC804_04480 {ECO:0000313|EMBL:KNB62145.1};
OS   Chryseobacterium sp. Hurlbut01.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Chryseobacterium.
OX   NCBI_TaxID=1681828 {ECO:0000313|EMBL:KNB62145.1, ECO:0000313|Proteomes:UP000036769};
RN   [1] {ECO:0000313|Proteomes:UP000036769}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hurlbut01 {ECO:0000313|Proteomes:UP000036769};
RA   Couger M.B., Youseff N., Elshahed M., French D., Hoff W.;
RT   "Draft Genome Sequence of the Environmental Isolate Chryseobacterium sp.
RT   Hurlbut 01.";
RL   Submitted (JUL-2015) 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:KNB62145.1}.
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DR   EMBL; LGIP01000003; KNB62145.1; -; Genomic_DNA.
DR   RefSeq; WP_050377833.1; NZ_LGIP01000003.1.
DR   AlphaFoldDB; A0A0K9Y1P8; -.
DR   PATRIC; fig|1681828.3.peg.3097; -.
DR   Proteomes; UP000036769; 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}.
FT   DOMAIN          8..142
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          173..263
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          270..373
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          393..457
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   460 AA;  50665 MW;  2BE3AA43AC2D5D51 CRC64;
     MSLIKSISGI RGTIGGKVND NLTPLDVVKF ASAFGTWLQN NKNKKDLTLV IGRDARISGS
     MVNSLVCATL QGLGINVIDL GLSTTPTVEI MVPELKADGG IILTASHNPK QWNALKLLNE
     KGEFINRENG AEVLALAENE DFNYAEVDDL GKYETRDDAF DIHIQQILDL PMVDVEAIKA
     KKYKIVLDAV NSTGGIAIPM LLDKLGCETV KLYCEPNGQF PHNPEPLKEH LGDICELVIK
     EKADFGVVVD PDVDRLALVD EKGEMFGEEY TLVAVADYLL KNKNGVAISN LSSSRALRDV
     AQTHNSEYFA SAVGEVNVVN LMKEKNAVIG GEGNGGIIYP ELHYGRDSLV GVALFLTHLA
     KENKTVSELR AGYPSYFMGK KKIELTPEIN VDDLLTKMEK EYQNEEVSTV DGVKIDFENN
     WVHLRKSNTE PIIRIYTEAK SQEEADRLGD DMIAKIRSLI
//
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