ID A0A094PG81_9ACTN Unreviewed; 455 AA.
AC A0A094PG81;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:KGA09952.1};
GN ORFNames=GM46_6235 {ECO:0000313|EMBL:KGA09952.1};
OS actinobacterium acAcidi.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1504320 {ECO:0000313|EMBL:KGA09952.1, ECO:0000313|Proteomes:UP000029305};
RN [1] {ECO:0000313|EMBL:KGA09952.1, ECO:0000313|Proteomes:UP000029305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Ghai R., Mizuno C.M., Picazo A., Camacho A., Rodriguez-Valera F.;
RT "Key roles for freshwater Actinobacteria revealed by deep metagenomic
RT sequencing.";
RL Submitted (MAY-2014) 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}.
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:KGA09952.1}.
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DR EMBL; JNSG01000051; KGA09952.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094PG81; -.
DR PATRIC; fig|1504320.4.peg.1256; -.
DR Proteomes; UP000029305; Unassembled WGS sequence.
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}.
FT DOMAIN 11..134
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 160..260
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 265..374
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 379..451
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 455 AA; 48788 MW; B612FF4D8074258C CRC64;
MSTDPLVLDR IVKAYDIRGT TPDEMNDDVA YALGVAFADF VKAPMVLVGR DMRVTGESLA
DSFSRGVISR GVNVVNLGLA STDLVYFAAG SLDAPGAMFT ASHNPAEYNG IKFCLSGARP
VGIDTGLAAI RDAAKEVLAG RGPADVAAVG TIAERDMLDD FADHVVSFID VDSLIPMKVV
ADTANGMGGL IVPVVFDRLP MMQLEVMYPE LDGSFPNHPA DPIQPSNQRD LQARVVSGGF
DIGLAFDGDA DRVFVVDEQG RGVSGSTTTA ILAAAVLRAN PGATVLHNLI CSRSVPEVIS
ENGGVPVRTK VGHSNIKQVM AETGAVFGGE HSAHYYFLDN YRADSGIIAT MFMLQELSRA
QRPLSELRKP FERYEASGEI NTSVSDAQVV MAEVAKVYSK FPQDWIDGLT VDCGDWWFNL
RPSNTEPLLR LNLEASTRDD CDTYVAEVLS LVTSV
//
