ID A0A1L3MI04_9MICO Unreviewed; 477 AA.
AC A0A1L3MI04;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Phosphoglucosamine mutase {ECO:0000313|EMBL:APH02015.1};
GN Name=manB {ECO:0000313|EMBL:APH02015.1};
GN ORFNames=ASJ30_11150 {ECO:0000313|EMBL:APH02015.1};
OS Janibacter indicus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Janibacter.
OX NCBI_TaxID=857417 {ECO:0000313|EMBL:APH02015.1, ECO:0000313|Proteomes:UP000182938};
RN [1] {ECO:0000313|EMBL:APH02015.1, ECO:0000313|Proteomes:UP000182938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YFY001 {ECO:0000313|EMBL:APH02015.1,
RC ECO:0000313|Proteomes:UP000182938};
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) 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; CP013290; APH02015.1; -; Genomic_DNA.
DR RefSeq; WP_072625167.1; NZ_CP013290.1.
DR AlphaFoldDB; A0A1L3MI04; -.
DR KEGG; jte:ASJ30_11150; -.
DR Proteomes; UP000182938; Chromosome.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd03089; PMM_PGM; 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 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 PANTHER; PTHR43771; PHOSPHOMANNOMUTASE; 1.
DR PANTHER; PTHR43771:SF1; PHOSPHOMANNOMUTASE; 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};
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:UP000182938}.
FT DOMAIN 10..133
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 162..267
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 278..388
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 393..474
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 477 AA; 50211 MW; C3D0A00488215753 CRC64;
MTTTLSDFVK AYDVRGLVPQ QLNIDVAHAL GAAFAEVVAL EEGASAVVIG HDMRPSSPEL
VDALARGITA RGVDAILIGL ASTDGLYYAS GALGLPGAMF TASHNPARYN GIKFCRPGAR
PVGQESGLAQ IRDLAQAHLD AGVSAFDGVR PGTVFRRDVL ADYAAFLRGL VDLSGCRPLR
VTVDAGNGMG GLTVPAVLGT DSGLPGLPLT IDPMYFELDG TFPNHEANPL DPANLVDLQE
RVRSHGADIG IAFDGDADRC FVVDEHGDPV SPSAITAMIA SREIAREVAA GRAPGDVAIV
HNAITSAAVP QIIAEAGARP VRTRVGHSYV KADMSEHDAV FGGEHSAHYY FRDFWFADTG
MLAAMHVLAA LGESDAPLSE VMAPYERYVA SGEINSTVAD AAAVTEVVRA RHATEGTSVD
ELDGLTVTLP GADGAPQWWF NLRPSNTEPL LRLNVEAADE ATMARVRDDV LTTIREA
//
