ID A0A177DBC1_ALTAL Unreviewed; 583 AA.
AC A0A177DBC1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 08-OCT-2025, entry version 30.
DE RecName: Full=Phosphoribomutase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CC77DRAFT_943642 {ECO:0000313|EMBL:OAG16776.1};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG16776.1, ECO:0000313|Proteomes:UP000077248};
RN [1] {ECO:0000313|EMBL:OAG16776.1, ECO:0000313|Proteomes:UP000077248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG16776.1,
RC ECO:0000313|Proteomes:UP000077248};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231, ECO:0000256|RuleBase:RU004326}.
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DR EMBL; KV441488; OAG16776.1; -; Genomic_DNA.
DR RefSeq; XP_018382197.1; XM_018534921.1.
DR AlphaFoldDB; A0A177DBC1; -.
DR STRING; 5599.A0A177DBC1; -.
DR GeneID; 29120515; -.
DR KEGG; aalt:CC77DRAFT_943642; -.
DR VEuPathDB; FungiDB:CC77DRAFT_943642; -.
DR OMA; GYCVDPE; -.
DR Proteomes; UP000077248; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:TreeGrafter.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0008973; F:phosphopentomutase activity; IEA:EnsemblFungi.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
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 FunFam; 3.40.120.10:FF:000035; Pgm3p; 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 PANTHER; PTHR45745:SF1; PHOSPHOGLUCOMUTASE 2B-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 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 Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Glucose metabolism {ECO:0000256|ARBA:ARBA00022526};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
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:UP000077248}.
FT DOMAIN 45..182
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 229..318
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 327..432
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 525..565
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 583 AA; 64500 MW; AF1DA20DE7140986 CRC64;
MTQDIKELAR QWLELDQDKT TTDEIYKLLV DGDTDELEKR LRHRIAFGTA GLRGPMQGGF
ACMNSLTVIQ ASQGLAAYLL KTEENVKRRG VVIGRDARHN SEKFAKLTAA AFVAKGIKVW
WYEEPSHTPM VPFGVRELEA AAGIMITASH NPAKDNGYKV YWSNGCQIIP PHDSGIADSI
MENLKPVTWD TTLVDSSLLV EGSLGLVQDN YHRAILCAAQ PEHVQVKMDP ELRFVYTPMH
GVGLPAMQRC AETLGVASQM TVVEAQAKPD PDFPTVKFPN PEEKGALDLA IETADKSSTR
LILASDPDAD RLAAAEKVGD RWHIFSGNQL GALLGSYLFE RYPETKPREK LAMLASTVSS
RMLAALAKKE GFKFTETLTG FKWLGNVTRQ LDSEGYDVVY AFEEALGYMI PQTVHDKDSI
SAAAVFLTAA SHWATQGLTP YAKLQQLYEY LGYFEDANTY LVSPSPSVTT SVFTAIRALG
SPHPTTIGSR RILRWRDLTL GYDSKSKDHK PDLPVDVTSQ MITCELDDGA VFTVRGSGTE
PKIKLYIECQ GKSSQEAKKG ANEILDDLLR EWFKPEENGL RLA
//
