ID B6QSL2_TALMQ Unreviewed; 568 AA.
AC B6QSL2;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Phosphoglucomutase, putative {ECO:0000313|EMBL:EEA19365.1};
GN ORFNames=PMAA_001600 {ECO:0000313|EMBL:EEA19365.1};
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA19365.1, ECO:0000313|Proteomes:UP000001294};
RN [1] {ECO:0000313|Proteomes:UP000001294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC {ECO:0000313|Proteomes:UP000001294};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(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; DS995905; EEA19365.1; -; Genomic_DNA.
DR RefSeq; XP_002152302.1; XM_002152266.1.
DR AlphaFoldDB; B6QSL2; -.
DR STRING; 441960.B6QSL2; -.
DR VEuPathDB; FungiDB:PMAA_001600; -.
DR HOGENOM; CLU_045514_1_0_1; -.
DR OrthoDB; 1775085at2759; -.
DR PhylomeDB; B6QSL2; -.
DR Proteomes; UP000001294; Unassembled WGS sequence.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR016066; A-D-PHexomutase_CS.
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 SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 2.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|RuleBase:RU004326};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001294}.
FT DOMAIN 18..153
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 197..293
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
SQ SEQUENCE 568 AA; 62480 MW; DC0FCF26F805B839 CRC64;
MPTTTLREGL AYTPQPLKFG TSGRRGLVVD LTQLEIYTNV LAEIHYLQSL PLSEGGIQSG
DDFYYAYDLR PSSTKYVENN RGGLCQAVEQ ALKDGGMRPL NLGAIPTPAL TYFALQRGKG
SIMVTGSHIP FDRNGYKLNT SKGELMKKDE HPINDLVALT REKLMEQEFS ESLFDEQGML
RNKPSTLEPV LPEARSAYIQ RFLDFFEGET LQGMTILAYQ HSAVGRDLLV EIFEKFGANV
IPAGRSETFV PIDTEAIDQA QLDVVQKLYD QAGQSSINAM ISTDGDSDRP LLLAPRNGKL
CFFGGDLLGM IVAQFLRADA AVVPISANDA IDYGSLAEIT EPKTKIGSPY VIAGMQLAIN
KGRSHVCGWE ANGGFLTGSD MKRNGKTLSA LPTRDAMLPL LCALFAAKNE HMTLPDLFAT
LPKRYSRAAL LRNFPRSTSL KIIERFSPPD AVMRDVSFDA SSQIIVRDSN NSQLDTTESH
AGDIKRIRSE LESIFSSERG FGPIVRINYT DGVRMYFGNG DVAHFRPSGN ADELRIYAIA
DQQERADDIA VQGVAEPDGL LRRLQSVV
//
