ID A0A3P3VPH2_9GAMM Unreviewed; 451 AA.
AC A0A3P3VPH2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 28-JAN-2026, entry version 27.
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=D0544_05180 {ECO:0000313|EMBL:RRJ84500.1};
OS Aestuariirhabdus litorea.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Oceanospirillales; Aestuariirhabdaceae; Aestuariirhabdus.
OX NCBI_TaxID=2528527 {ECO:0000313|EMBL:RRJ84500.1, ECO:0000313|Proteomes:UP000280792};
RN [1] {ECO:0000313|EMBL:RRJ84500.1, ECO:0000313|Proteomes:UP000280792}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GTF-13 {ECO:0000313|EMBL:RRJ84500.1,
RC ECO:0000313|Proteomes:UP000280792};
RA Khan S.A.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RRJ84500.1, ECO:0000313|Proteomes:UP000280792}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GTF-13 {ECO:0000313|EMBL:RRJ84500.1,
RC ECO:0000313|Proteomes:UP000280792};
RA Shieh W.Y.;
RT "Simiduia agarivorans gen. nov., sp. nov., a marine, agarolytic bacterium
RT isolated from shallow coastal water from Keelung, Taiwan.";
RL Submitted (DEC-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:RRJ84500.1}.
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DR EMBL; QWEZ01000001; RRJ84500.1; -; Genomic_DNA.
DR RefSeq; WP_125014930.1; NZ_QWEZ01000001.1.
DR AlphaFoldDB; A0A3P3VPH2; -.
DR Proteomes; UP000280792; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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:0004615; F:phosphomannomutase activity; IEA:TreeGrafter.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-ARBA.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:TreeGrafter.
DR CDD; cd05802; GlmM; 1.
DR FunFam; 3.30.310.50:FF:000001; Phosphoglucosamine mutase; 1.
DR FunFam; 3.40.120.10:FF:000001; Phosphoglucosamine mutase; 1.
DR FunFam; 3.40.120.10:FF:000003; Phosphoglucosamine mutase; 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 InterPro; IPR050060; Phosphoglucosamine_mutase.
DR NCBIfam; TIGR01455; glmM; 1.
DR NCBIfam; NF008139; PRK10887.1; 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:UP000280792}.
FT DOMAIN 4..132
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 160..257
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 261..367
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 376..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 244
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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 MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
SQ SEQUENCE 451 AA; 48081 MW; BCBE95F9FB6F7E37 CRC64;
MTRHYFGTDG VRGRVGEFPM TPDFAMRLGW AAGKVLAASG TKEVLIGKDT RASGYMLESA
LEAGFSAAGI NIALAGPLPT PAVAYLTSTF RADAGVVISA SHNPYYDNGI KFFSGEGTKL
SDQQEHDIEA LLALALEQGI ECVESAALGK ARRVDDASGR YIEFCKGTFP AQLNLRGLKI
VVDSANGAAY KIAPAVYREL GADVISINDQ PNGVNINAEC GATHLDSLVA AVKEHGADLG
IALDGDADRL MLVDDQGEVV DGDQILFILA RSALDKGTLK GGVVGTQMSN LGLELALADH
NIPFVRAKVG DRYVMEQLHQ RGWCLGGENS GHILVLDEVT TGDAIVASLQ VLAAALENNT
SLAQLKAGMV KFPQQLINVR FGKDVQDPLT DNRVVQAVND AEHSLDNRGR VLLRKSGTEP
LIRVMVEADD ERLCTRHAEH LAEVIRNITA A
//
