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Database: UniProt
Entry: A0A369XVS8_9FUSO
LinkDB: A0A369XVS8_9FUSO
Original site: A0A369XVS8_9FUSO 
ID   A0A369XVS8_9FUSO        Unreviewed;       454 AA.
AC   A0A369XVS8;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Phosphoglucosamine mutase {ECO:0000256|HAMAP-Rule:MF_01554, ECO:0000256|RuleBase:RU004327};
DE            EC=5.4.2.10 {ECO:0000256|HAMAP-Rule:MF_01554, ECO:0000256|RuleBase:RU004327};
GN   Name=glmM {ECO:0000256|HAMAP-Rule:MF_01554};
GN   ORFNames=DV867_13965 {ECO:0000313|EMBL:RDE59089.1};
OS   Psychrilyobacter sp. S5.
OC   Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC   Psychrilyobacter.
OX   NCBI_TaxID=2283384 {ECO:0000313|EMBL:RDE59089.1, ECO:0000313|Proteomes:UP000253914};
RN   [1] {ECO:0000313|EMBL:RDE59089.1, ECO:0000313|Proteomes:UP000253914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S5 {ECO:0000313|EMBL:RDE59089.1,
RC   ECO:0000313|Proteomes:UP000253914};
RA   Yadav S., Villanueva L., Damste J.S.S.;
RT   "Draft genome sequence of Psychrilyobacter sp. strain S5.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of glucosamine-6-phosphate to
CC       glucosamine-1-phosphate. {ECO:0000256|HAMAP-Rule:MF_01554,
CC       ECO:0000256|RuleBase:RU004327}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate;
CC         Xref=Rhea:RHEA:23424, ChEBI:CHEBI:58516, ChEBI:CHEBI:58725;
CC         EC=5.4.2.10; Evidence={ECO:0000256|HAMAP-Rule:MF_01554,
CC         ECO:0000256|RuleBase:RU004327};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01554};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01554};
CC   -!- PTM: Activated by phosphorylation. {ECO:0000256|HAMAP-Rule:MF_01554}.
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC       {ECO:0000256|ARBA:ARBA00010231, ECO:0000256|HAMAP-Rule:MF_01554,
CC       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:RDE59089.1}.
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DR   EMBL; QQOU01000036; RDE59089.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A369XVS8; -.
DR   Proteomes; UP000253914; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008966; F:phosphoglucosamine mutase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd05802; GlmM; 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   HAMAP; MF_01554_B; GlmM_B; 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; IPR006352; GlmM_bact.
DR   NCBIfam; TIGR01455; glmM; 1.
DR   PANTHER; PTHR42946:SF1; PHOSPHOGLUCOSAMINE MUTASE FAMILY PROTEIN; 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, ECO:0000256|HAMAP-Rule:MF_01554};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01554};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01554};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP-
KW   Rule:MF_01554}; Reference proteome {ECO:0000313|Proteomes:UP000253914}.
FT   DOMAIN          4..141
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          165..257
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          263..370
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          379..450
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
FT   ACT_SITE        105
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT   BINDING         105
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via phosphate group"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT   BINDING         246
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT   BINDING         248
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT   BINDING         250
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT   MOD_RES         105
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
SQ   SEQUENCE   454 AA;  49672 MW;  E6CD4ABE0C5077AE CRC64;
     MQKRKYFGTD GIRGEANREL TVDIAMRLGY ALAYYLKKKN PDKKKINVVI GSDTRISGYM
     LRSALMAGLS SMGVHITYVG VLPTPGVAYL TQIKSADAGI MISASHNPAK DNGIKIFRSN
     GTKLPDEIEL ELEVLMDSYE EISKECVAGD KVGKVLMEDD DFFLYRDFLL STVKGDFSGM
     KIILDAANGA AFELARSVFS RLGAEIVSIN DLPNGTNINV NCGSTHPEIL AKVVVGYSAD
     LGLAYDGDAD RLMAVDKFGN IIDGDKIISI LALNLKEKDE LNNNKVVTTV MSNMGFEKYL
     ENKGITLVRA NVGDRYVIAK MKEQGLNLGG EQSGHIIMSD YNTTGDGVLV SLKLVEALRD
     CGKSIDELVS GIVDWPQILV NVRVENSKKN TWNENSVIKE IIKIKEKEMD GLGRVLVRTS
     GTEPLVRVMV EGKDKTQVDS VAEEIAQVVK KELG
//
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