ID I0KWN6_9ACTN Unreviewed; 559 AA.
AC I0KWN6;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=Putative phosphomannomutase {ECO:0000313|EMBL:CCH15983.1};
DE EC=5.4.2.8 {ECO:0000313|EMBL:CCH15983.1};
GN ORFNames=MILUP08_40894 {ECO:0000313|EMBL:CCH15983.1};
OS Micromonospora lupini str. Lupac 08.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1150864 {ECO:0000313|EMBL:CCH15983.1, ECO:0000313|Proteomes:UP000003448};
RN [1] {ECO:0000313|Proteomes:UP000003448}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lupac 08 {ECO:0000313|Proteomes:UP000003448};
RX PubMed=22815450; DOI=10.1128/jb.00628-12;
RA Alonso-Vega P., Normand P., Bacigalupe R., Pujic P., Lajus A., Vallenet D.,
RA Carro L., Coll P., Trujillo M.E.;
RT "Genome Sequence of Micromonospora lupini Lupac 08, Isolated from Root
RT Nodules of Lupinus angustifolius.";
RL J. Bacteriol. 194:4135-4135(2012).
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:CCH15983.1}.
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DR EMBL; CAIE01000010; CCH15983.1; -; Genomic_DNA.
DR RefSeq; WP_007455499.1; NZ_HF570108.1.
DR AlphaFoldDB; I0KWN6; -.
DR STRING; 1150864.MILUP08_40894; -.
DR eggNOG; COG1109; Bacteria.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000003448; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd05799; PGM2; 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; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR PANTHER; PTHR45745:SF1; PHOSPHOGLUCOMUTASE 2A-RELATED; 1.
DR PANTHER; PTHR45745; PHOSPHOMANNOMUTASE 45A; 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:0000313|EMBL:CCH15983.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004326};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000003448}.
FT DOMAIN 54..168
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 218..317
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 334..446
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 459..527
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 559 AA; 57867 MW; 30A24DC00802E608 CRC64;
MAADTTDIDD IREQARRWLA DDPDPASRAE LTAVLDRLPA SAPELADRFA GPLTFGTAGL
RGPLRAGPNG MNLAVVTQAA AGLVGWLAAQ GGTGPLVIGY DARHGSRQFA ERTAQVATAA
GRPALLLPRP LPTPVLAYAV RQLGAVAGVM VTASHNPPQD NGYKVYLGAE LGGELGAGAQ
IVPPADAGIE AAIRAVGPLT QVPLGRPGEV LGDDLVASYV ERATAVIAPD GPRDLSVAYT
PLHGVGAAVL TAAFARAGFP VPGVVPEQAE PDPAFPTVSF PNPEEPGAVD RLIALADATG
ADLAIANDPD ADRCAVVVRT SGGDDGRGWR MLRGDEVGVL LADHLMRRGV TGLYATTIVS
SSLLRAMCAA RGLPYDETLT GFKWIVRAGG GSAPLVFGYE EALGYCVAPE HVRDKDGITA
ALTVAELAAG LKAQSRTLTD RLDELAAEFG VHHTDQLSVR VDDLREIADA MARIRAATPT
TLLGQPVDSA RDLLPEADVV ILRTATARVV IRPSGTEPKL KAYLEVVEPV VDGDVPTARS
RAAQAVATLR GEIAAALGV
//
