ID A0A2A3JWD3_9RHOB Unreviewed; 393 AA.
AC A0A2A3JWD3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Phosphoglucosamine mutase {ECO:0000256|RuleBase:RU004327};
DE EC=5.4.2.10 {ECO:0000256|RuleBase:RU004327};
DE Flags: Fragment;
GN ORFNames=CLG85_12610 {ECO:0000313|EMBL:PBD18824.1};
OS Alloyangia mangrovi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Alloyangia.
OX NCBI_TaxID=1779329 {ECO:0000313|EMBL:PBD18824.1};
RN [1] {ECO:0000313|EMBL:PBD18824.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAOS 153D {ECO:0000313|EMBL:PBD18824.1};
RA Verma A., Krishnamurthi S.;
RT "Yangia sp. SAOS 153D whole genome sequencing.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of glucosamine-6-phosphate to
CC glucosamine-1-phosphate. {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|RuleBase:RU004327};
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, 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:PBD18824.1}.
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DR EMBL; NTHN01000191; PBD18824.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A3JWD3; -.
DR OrthoDB; 9803322at2; -.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0008966; F:phosphoglucosamine mutase activity; IEA:UniProtKB-EC.
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 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; 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 PRINTS; PR00509; PGMPMM.
DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|RuleBase:RU004327};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|RuleBase:RU004326};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 3..137
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 159..255
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 259..367
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT NON_TER 393
FT /evidence="ECO:0000313|EMBL:PBD18824.1"
SQ SEQUENCE 393 AA; 41780 MW; 7471D30776CF85F7 CRC64;
MTRKLFGTDG VRGTANMHPM TAQMALAIGA AAGRYFRREA GGTHRVVIGK DTRLSGYMFE
TALTAGLTST GMNVLLLGPV PTPAVGLLTP SMRADVGIMI SASHNPAHDN GIKFFGPDGF
KLSDEAEAEI EALVEKGVEP AQAGNIGRAK RIDDGRFRYQ ERVKSSFPHG MRLDGMKVVI
DCANGAAYRA APEVLWELGA EVIPVGTHPN GLNINDQCGS TKPQTAAETV VAHGADVGIC
LDGDADRVIL IDEKGTVADG DQIMALMAGR WAEEDRLAGG TLVATVMSNL GLERYLGDRG
LTLARTKVGD RYVVEMMRAR GFNLGGEQSG HIVMTDFATT GDGLMAGLQF LAEMVRTGQP
ASRLARNFEP VPQLLKNVRF DAGQTPLDAA SVR
//
