ID A0A0B7N5Z2_9FUNG Unreviewed; 617 AA.
AC A0A0B7N5Z2;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CEP10434.1};
GN Name=PARPA_04116.1 scaffold 11792 {ECO:0000313|EMBL:CEP10434.1};
OS Parasitella parasitica.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP10434.1, ECO:0000313|Proteomes:UP000054107};
RN [1] {ECO:0000313|EMBL:CEP10434.1, ECO:0000313|Proteomes:UP000054107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP10434.1,
RC ECO:0000313|Proteomes:UP000054107};
RA Ellenberger Sabrina;
RL Submitted (SEP-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}.
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DR EMBL; LN724120; CEP10434.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B7N5Z2; -.
DR STRING; 35722.A0A0B7N5Z2; -.
DR OrthoDB; 1482at2759; -.
DR Proteomes; UP000054107; 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 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 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 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 Reference proteome {ECO:0000313|Proteomes:UP000054107}.
FT DOMAIN 45..183
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 210..316
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 327..452
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 617 AA; 69076 MW; 3AF635B90BECE52A CRC64;
MSESIDALVE KWLSVDKNEE TRNEIIALQK AGNIAELQKR LSTRIEFGTA GLRARMEAGF
SRMNDLTVLQ ASQGLAVYIE KNVKDAKNRG VVVGHDHRHH SKAFAQLTAS AFIQRGFKVW
FYKELVHTPM VPYTIKKLHA AGGVMITASH NPKDDNGYKV YWANACQIIP PHDEGIAATI
LKNLEPWSWD YDLVSTSNLV KDPTDEGVID AYFKEVEALC KNKQDNQDTQ VKFVYTAMHG
VGTPFAERAF ACFGLPPFEP VKAQILPDPD FPTVAFPNPE EGKGALKLAI ETADKVGGNI
ILANDPDADR LAIAEKQSNG KWVIFTGNQL GSILGAASFE KAIASGQRAE HLAMVASTVS
SKFLARMAQV EGFTFEESLT GFKWIGNTAM RLEKQRLNVI FSYEEAIGFT IGDIVKDKDG
VSALAFFSEW AVQLYKRGIT AYDYLEELYK KYGYFVSENS YFICDDKKKI AKIFDRIRFG
DEEHREKAKV MALKCSIQFW SLSEFFQGGH KLCYPETVGG HKVIGIRDLT VGYDSTTVDK
EPTLPVSASS EMITFRLDNH TVFTIRTSGT EPKIKYYSEL RGETEEQAKH DLHQVVEAIG
EELMQYKKNG LAKKKED
//
