ID E4ZBV1_NEIL0 Unreviewed; 444 AA.
AC E4ZBV1;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Phosphoglucosamine mutase {ECO:0000256|HAMAP-Rule:MF_01554};
DE EC=5.4.2.10 {ECO:0000256|HAMAP-Rule:MF_01554};
GN Name=glmM {ECO:0000256|HAMAP-Rule:MF_01554};
GN OrderedLocusNames=NLA_5910 {ECO:0000313|EMBL:CBN86828.1};
OS Neisseria lactamica (strain 020-06).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=489653 {ECO:0000313|EMBL:CBN86828.1, ECO:0000313|Proteomes:UP000008723};
RN [1] {ECO:0000313|EMBL:CBN86828.1, ECO:0000313|Proteomes:UP000008723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=020-06 {ECO:0000313|EMBL:CBN86828.1,
RC ECO:0000313|Proteomes:UP000008723};
RX PubMed=21092259; DOI=10.1186/1471-2164-11-652;
RA Bennett J.S., Bentley S.D., Vernikos G.S., Quail M.A., Cherevach I.,
RA White B., Parkhill J., Maiden M.C.;
RT "Independent evolution of the core and accessory gene sets in the genus
RT Neisseria: insights gained from the genome of Neisseria lactamica isolate
RT 020-06.";
RL BMC Genomics 11:652-652(2010).
CC -!- FUNCTION: Catalyzes the conversion of glucosamine-6-phosphate to
CC glucosamine-1-phosphate. {ECO:0000256|HAMAP-Rule:MF_01554}.
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 -!- 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}.
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DR EMBL; FN995097; CBN86828.1; -; Genomic_DNA.
DR RefSeq; WP_013448589.1; NC_014752.1.
DR AlphaFoldDB; E4ZBV1; -.
DR KEGG; nla:NLA_5910; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_7_0_4; -.
DR Proteomes; UP000008723; 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; 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.
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}.
FT DOMAIN 4..140
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 159..256
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 260..371
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 375..441
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
FT ACT_SITE 104
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT BINDING 104
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 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 BINDING 247
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
SQ SEQUENCE 444 AA; 47566 MW; 2443117EA53D7CDB CRC64;
MAKKYFGTDG VRGEVGQFPI TPDFVLKLGY AAGQVLVQHD TDQKPTVLIG KDTRISGYML
EAALVAGFTA AGVNVIQTGP LPTPGVAYLI RALRLSAGVM ISASHNAYSD NGIKFFAEGG
VKLSDEIELE IEAKIDEEMK TQPSARLGRA RRISGADDRY IEFCKSTFPT HSDLRGLKLV
VDAANGAAYS VAPKVFHELG AQVVSIGNEP NGYNINEKCG ATHTKTLQAA VLQNEADYGI
ALDGDGDRLM MVDKNGQVYD GDSLIYVIAK ARAGEGVNIG GVVGTVMTNM AMENALKEQG
VDFCRAKVGD RYVLEQLNRR GWLVGGEASG HILCMDKHNT GDGIISALQV LAALQTLNQD
LAAVCADWQP YPQTMINVRI GKGQNWQEAS KTVLAEVEKE LEGKGRVVLR ASGTEPVVRV
MVEARQVDWA RDGAERIAAA IGGI
//
