ID A0A135LAH9_PENPA Unreviewed; 595 AA.
AC A0A135LAH9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Alpha-D-phosphohexomutase, alpha/beta/alpha domain I {ECO:0000313|EMBL:KXG45977.1};
GN ORFNames=PGRI_048330 {ECO:0000313|EMBL:KXG45977.1};
OS Penicillium patulum (Penicillium griseofulvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=5078 {ECO:0000313|EMBL:KXG45977.1, ECO:0000313|Proteomes:UP000070168};
RN [1] {ECO:0000313|EMBL:KXG45977.1, ECO:0000313|Proteomes:UP000070168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG3 {ECO:0000313|EMBL:KXG45977.1,
RC ECO:0000313|Proteomes:UP000070168};
RX PubMed=26729047; DOI=10.1186/s12864-015-2347-x;
RA Banani H., Marcet-Houben M., Ballester A.R., Abbruscato P.,
RA Gonzalez-Candelas L., Gabaldon T., Spadaro D.;
RT "Genome sequencing and secondary metabolism of the postharvest pathogen
RT Penicillium griseofulvum.";
RL BMC Genomics 17:19-19(2016).
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:KXG45977.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LHQR01000069; KXG45977.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135LAH9; -.
DR STRING; 5078.A0A135LAH9; -.
DR OMA; GYCVDPE; -.
DR OrthoDB; 1482at2759; -.
DR Proteomes; UP000070168; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000070168}.
FT DOMAIN 45..183
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 212..314
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 325..430
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 595 AA; 65842 MW; D0FF2F10CE34ACA6 CRC64;
MAQSISSLTE QWLQWDQDPT TRSEIEQLRD SNATEELEKR LRNRIEFGTA GLRGCMAAGF
SCMNSLIVIQ ASQGLAKFIR DKRSDIASNG VVIGHDARHN SAKFAALAAN AFIAQRIPVW
FFNEEGPTPM VAFGVIHFGA AAGIMVTASH NPPQDNGYKV YSSNGAQINR PEDGEIAQSI
QENLEPWPTA WAELQPSEFL RADSYQKLLP HYSRQVVEFM KTTVADWQPP RPFAYTPLHG
VGGLVLPTLC RSLGIKDFVS VAAQEKPDPN FPTVKFPNPE EAGALDLAIE TADREGKTLI
IANDPDADRF AVAEKVDGKW HTLTGNHVGV LLASHILDLY DARKDWSHVA VLTTTVSSGM
LGKMAAAKGV YFAETLTGFK WMANVARDLE KEGKTVSFAY EEALGYMFPS VCYDKDGITA
AAVFLAAEAK WRAQGLTAYA KLQQLFSEFG HHETLNNYFR SPNPQLTSTL FQGIRGSSGL
ANMQFGRFKI LRWRDLTEGY DSSTPDNKPD LPEDPTSQML TLWLDGGVRF TFRGSGTEPK
VKFYIESCGD SREDAVKAVC DTFLAIREEW VQRFTPSMTY SKQLSTSSGN ILNVE
//
