ID K0IZH7_AMPXN Unreviewed; 449 AA.
AC K0IZH7;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
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 ECO:0000313|EMBL:BAM46372.1};
GN OrderedLocusNames=AXY_02400 {ECO:0000313|EMBL:BAM46372.1};
OS Amphibacillus xylanus (strain ATCC 51415 / DSM 6626 / JCM 7361 / LMG 17667
OS / NBRC 15112 / Ep01).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Amphibacillus.
OX NCBI_TaxID=698758 {ECO:0000313|EMBL:BAM46372.1, ECO:0000313|Proteomes:UP000006294};
RN [1] {ECO:0000313|EMBL:BAM46372.1, ECO:0000313|Proteomes:UP000006294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51415 / DSM 6626 / JCM 7361 / LMG 17667 / NBRC 15112 /
RC Ep01 {ECO:0000313|Proteomes:UP000006294};
RA Nakazawa H., Katano Y., Nakamura S., Sasagawa M., Fukada J., Arai T.,
RA Sasakura N., Mochizuki D., Hosoyama A., Harada K., Horikawa H., Kato Y.,
RA Harada T., Sasaki K., Sekiguchi M., Hodoyama M., Nishiko R., Narita H.,
RA Hanamaki A., Hata C., Konno Y., Niimura Y., Yamazaki S., Fujita N.;
RT "Whole genome sequence of Amphibacillus xylinus NBRC 15112.";
RL Submitted (JAN-2011) 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}.
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DR EMBL; AP012050; BAM46372.1; -; Genomic_DNA.
DR AlphaFoldDB; K0IZH7; -.
DR STRING; 698758.AXY_02400; -.
DR KEGG; axl:AXY_02400; -.
DR PATRIC; fig|698758.3.peg.242; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_7_0_9; -.
DR Proteomes; UP000006294; Chromosome.
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; 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, 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:UP000006294}.
FT DOMAIN 4..136
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 159..254
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 258..368
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 374..443
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
FT ACT_SITE 101
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT BINDING 101
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 241
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT BINDING 243
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
SQ SEQUENCE 449 AA; 48680 MW; 3CA55522DC3C2F38 CRC64;
MMVKYFGTDG VRGIANDQLT PELAFKLGRA GGYVLTRDAE KPKVLIGKDT RISGDMLEGA
LISGLLSMGI EVMRLGVIST PGVAYLTKAM GAEAGIMISA SHNPVEDNGI KFFGPDGFKL
SDEQEQEIEE LIDAKDDTLP RPIGSEIGVI NDYFEGAQKY LHYLKQSVDN DFTGLHVVLD
CANGSTSSLA PHLFADLDAD ISTIGASPNG LNINDGVGST HPEKLQAKVL ELEADIGLAF
DGDGDRLIVV DEKGNIVDGD QIIFICANYL NNRGLLRHST VVSTVMSNLG FYKALEERGM
KSDKTDVGDR YVVEEMRRGG YNLGGEQSGH IIFLDYITTG DGMLTALQLL DIMKETGKTI
SELAAQMVKF PQVLKNIEVV DKHQVFVDQR VQDVIAKVEA DLGDQGRVLV RPSGTESLVR
VMVEASTIEQ CHESVDQVVK VIEDVLGLE
//
