ID B8NAT7_ASPFN Unreviewed; 559 AA.
AC B8NAT7;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Phosphoglucomutase, putative {ECO:0000313|EMBL:EED52610.1};
GN ORFNames=AFLA_043120 {ECO:0000313|EMBL:EED52610.1};
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952 {ECO:0000313|EMBL:EED52610.1, ECO:0000313|Proteomes:UP000001875};
RN [1] {ECO:0000313|EMBL:EED52610.1, ECO:0000313|Proteomes:UP000001875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC SRRC 167 {ECO:0000313|Proteomes:UP000001875};
RX PubMed=25883274; DOI=10.1128/genomeA.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
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}.
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DR EMBL; EQ963476; EED52610.1; -; Genomic_DNA.
DR RefSeq; XP_002377774.1; XM_002377733.1.
DR AlphaFoldDB; B8NAT7; -.
DR STRING; 332952.B8NAT7; -.
DR EnsemblFungi; EED52610; EED52610; AFLA_043120.
DR VEuPathDB; FungiDB:AFLA_007872; -.
DR eggNOG; KOG1220; Eukaryota.
DR HOGENOM; CLU_016950_0_1_1; -.
DR OMA; GYCVDPE; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0008973; F:phosphopentomutase activity; IEA:EnsemblFungi.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0046115; P:guanosine catabolic process; IEA:EnsemblFungi.
DR GO; GO:0006148; P:inosine catabolic process; IEA:EnsemblFungi.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:EnsemblFungi.
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; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR016066; A-D-PHexomutase_CS.
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 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 Magnesium {ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|RuleBase:RU004326}.
FT DOMAIN 8..146
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 175..277
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 287..393
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 559 AA; 61575 MW; DC9D23434CAC01F0 CRC64;
MAGVGPRIQF GTAGLRGRMA AGFSCMNSLT VIQASQGLAK YLKDKHPDSA SGGVVIGHDA
RHNSAKFAAL AANAFISQQI PVWFYSEPSV TPSVPFGVTH LKAAAGIMIT ASHNPAQDNG
YKVYFKNGAQ INTPIDVEIA QSIEENLAPW SGAWKDLQAC EYLHADAYKT ILPHYTKTVW
DYANSTVSDW KQPRPFVYTP LHGVGGLVFP DLCQSVGITE FTPVPEQVEP NPDFPTVSFP
NPEEAGALDL AMQTADREGK TLIIAHDPDA DRFAAAEKVD GSWFSFTGNH IGVLLASHLF
DSLENRKDGK RIAVLNSTVS TGMLEKMATA KGIQFEEALT GFKWMGNIAR RLEGEGYNVP
YAFEEALGYM FPAVCHDKDG ITAAMVFLAA QAKWQSQGLT PYMKLQQLFN EYGHYETLNN
YFRSPNPETT TALFRAIRNG PYRAEKTLGP FKILRWRDMT EGYDSGTTNN KPTLPVDKSS
QMLTLWLDQD VRFTFRASGT EPKVKLYVES CGASREQAVD AVCNAFLAVL KEWVVPFAPS
MTYSRQMPTS SGYVFQISE
//
