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Database: UniProt
Entry: A0A2S5A0M3_9SPHI
LinkDB: A0A2S5A0M3_9SPHI
Original site: A0A2S5A0M3_9SPHI 
ID   A0A2S5A0M3_9SPHI        Unreviewed;       459 AA.
AC   A0A2S5A0M3;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Phosphoglucosamine mutase {ECO:0000313|EMBL:POY36105.1};
GN   Name=glmM {ECO:0000313|EMBL:POY36105.1};
GN   ORFNames=C3K47_12975 {ECO:0000313|EMBL:POY36105.1};
OS   Solitalea longa.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Solitalea.
OX   NCBI_TaxID=2079460 {ECO:0000313|EMBL:POY36105.1, ECO:0000313|Proteomes:UP000236893};
RN   [1] {ECO:0000313|EMBL:POY36105.1, ECO:0000313|Proteomes:UP000236893}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HR-AV {ECO:0000313|EMBL:POY36105.1,
RC   ECO:0000313|Proteomes:UP000236893};
RA   Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL   Submitted (JAN-2018) 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:POY36105.1}.
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DR   EMBL; PQVF01000008; POY36105.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S5A0M3; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000236893; 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:UP000236893}.
FT   DOMAIN          8..140
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          171..262
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          269..370
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          394..451
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   459 AA;  49667 MW;  632B0DB09EC120DA CRC64;
     MTLIKSISGI RGTIGGAPGS ALTPLDVVKF TSAFGQWVIN KTGNKKIVIG RDARISGEMV
     RNLVVGTLQG LGIDVIDLDL STTPTVEIAV PLENAGGGII LTASHNPKQW NALKLLNGKG
     EFISSADGQE VLDIAEKSAF TYADVDELGS YKLDHSYVEK HIEMILALPL VDVDAIKNAN
     FSVVVDAVNS TGGIFVPKLL KALGVEVIHE LYCSPDGKFP HNPEPLAEHL TELSKTVTDK
     KAHLGISVDP DVDRLVFMCE DGNLFGEEYT LVAVADYVLK HNKGNTVSNL SSTRALQDVT
     ESHGGKYSAA AVGEVNVVEM MKATNAVIGG EGNGGIIYPE LHYGRDALVG IALFLTHLAK
     FGKSISVLKN GYPAYHISKN KITLTAEMDI DSLMQKIQDK YKQQPINTID GVRIEFDKQW
     VHLRRSNTEP IIRIYSEGNS ETVADALANK IISDFKEMI
//
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