ID B5VQ45_YEAS6 Unreviewed; 622 AA.
AC B5VQ45;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE SubName: Full=YMR278Wp-like protein {ECO:0000313|EMBL:EDZ69947.1};
GN ORFNames=AWRI1631_134160 {ECO:0000313|EMBL:EDZ69947.1};
OS Saccharomyces cerevisiae (strain AWRI1631) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=545124 {ECO:0000313|EMBL:EDZ69947.1, ECO:0000313|Proteomes:UP000008988};
RN [1] {ECO:0000313|EMBL:EDZ69947.1, ECO:0000313|Proteomes:UP000008988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AWRI1631 {ECO:0000313|EMBL:EDZ69947.1,
RC ECO:0000313|Proteomes:UP000008988};
RX PubMed=18778279; DOI=10.1111/j.1567-1364.2008.00434.x;
RA Borneman A.R., Forgan A.H., Pretorius I.S., Chambers P.J.;
RT "Comparative genome analysis of a Saccharomyces cerevisiae wine strain.";
RL FEMS Yeast Res. 8:1185-1195(2008).
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}.
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:EDZ69947.1}.
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DR EMBL; ABSV01001907; EDZ69947.1; -; Genomic_DNA.
DR AlphaFoldDB; B5VQ45; -.
DR SMR; B5VQ45; -.
DR Proteomes; UP000008988; 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:UniProtKB-KW.
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 Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277}.
FT DOMAIN 53..192
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 226..334
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 348..457
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 622 AA; 71069 MW; E402A69551B36CD3 CRC64;
MLQGILETVP SDLKDPISLW FKQDRNPKTI EEVTALCKKS DWNELHKRFD SRIQFGTAGL
RSQMQAGFSR MNTLVVIQAS QGLATYVRQQ FPDNLVAVVG HDHRFHSKEF ARATAAAFLL
KGFKVHYLNP DHEFVHTPLV PFAVDKLKAS VGVMITASHN PKMDNGYKVY YSNGCQIIPP
HDHAISDSID ANLEPWANVW DFDDVLNKAL KQGKLMYSRE EMLKLYLEEV SKNLVEINPL
KLEVKAKPWF VYTPMHGVGF DIFSTIVKKT LCLVEGKDYL CVPEQQNPDP SFPTVGFPNP
EEKGALDIGI NLAEKHDIDL LVANDPDADR FSVAVKDMQS GEWRQLTGNE IGFLFAFYEY
QKYKSMDKEF QHVHPLAMLN STVSSQMIKK MAEIEGFHYE DTLTGFKWIG NRAILLEKKG
YYVPFGFEEA IGYMFPAMEH DKDGISASIV FLQAYCKWKI DHNLDPLNVL ENGFKKYGVF
KEYNGYYVVP NPTVTKDIFD YIRNVYTPEG ASYPSSIGEE IEVLYYRDLT TGYQSDTINH
KPTLPVDPTS QMITVSARPS NGSENEHIRF TIRGSGTEPK LKVYIEACAN EEQRASFLAK
LTWNVLRREW FRPDEMNIVT KF
//
