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Database: UniProt
Entry: A0A3S4CC36_9HYPH
LinkDB: A0A3S4CC36_9HYPH
Original site: A0A3S4CC36_9HYPH 
ID   A0A3S4CC36_9HYPH        Unreviewed;       471 AA.
AC   A0A3S4CC36;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   28-JAN-2026, entry version 21.
DE   SubName: Full=Phosphoglucosamine mutase {ECO:0000313|EMBL:VDS04733.1};
DE            EC=5.4.2.10 {ECO:0000313|EMBL:VDS04733.1};
GN   Name=glmM_2 {ECO:0000313|EMBL:VDS04733.1};
GN   ORFNames=DEVEQU_01873 {ECO:0000313|EMBL:VDS04733.1};
OS   Devosia equisanguinis.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Hyphomicrobiales; Devosiaceae; Devosia.
OX   NCBI_TaxID=2490941 {ECO:0000313|EMBL:VDS04733.1, ECO:0000313|Proteomes:UP000268844};
RN   [1] {ECO:0000313|EMBL:VDS04733.1, ECO:0000313|Proteomes:UP000268844}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACIP1116281 {ECO:0000313|EMBL:VDS04733.1};
RA   Criscuolo A.;
RL   Submitted (DEC-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}.
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DR   EMBL; UZWD01000024; VDS04733.1; -; Genomic_DNA.
DR   RefSeq; WP_126150285.1; NZ_JBHTMH010000001.1.
DR   AlphaFoldDB; A0A3S4CC36; -.
DR   OrthoDB; 9803322at2; -.
DR   Proteomes; UP000268844; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0008966; F:phosphoglucosamine mutase activity; IEA:UniProtKB-EC.
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:TreeGrafter.
DR   GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:TreeGrafter.
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; 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; IPR050060; Phosphoglucosamine_mutase.
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; PF02880; PGM_PMM_III; 1.
DR   Pfam; PF00408; PGM_PMM_IV; 1.
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:0000313|EMBL:VDS04733.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000268844}.
FT   DOMAIN          5..132
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          256..370
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          411..454
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   471 AA;  49793 MW;  638A5EE81AE60AE9 CRC64;
     MTNSLKFGTS GLRGLAVDLQ GAEARRYTTA FITYLQGLGE AVPALYLAGD YRPSTQGIIA
     DCAAAAAEMG VPAISCGTIP TPALALHAMS AGAPSIMVTG SHIPADRNGL KFYRKSGEIS
     KADEAGIVAA LRDAAPAGNY SEPVADEAEA ARTRYVARYR GVLAVDALKG QRIGVYEHST
     VIRDILAEIF SSYGAEVVRL GRVEGFVAVD TEAFSDAVFA PLAGWIDENQ LDAIISADGD
     ADRPLLMDGQ KRFVRGDVLG LLAAQFIHAD QVVTPVTSNN AIEATGFFHA VRRTRVGSPF
     VIAEMEKALA DAGNAVIGFE ANGGTLLGSQ VSVGNGLSAL MTRDAVLPLL GAFGMAAREG
     RSVAEVVDAL PLRAAVAGRL EDVAQEKSAS LLKDLRDRGW AEKYFYPRVI ERFAEIDGLQ
     FWLNDGAMIH YRPSGNAPEL RCYVEAADEK AAEAALDWGL TAAKKDLAAR G
//
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