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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//