ID   AAPC_CENCI              Reviewed;         329 AA.
AC   Q40784;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Putative glucose-6-phosphate 1-epimerase {ECO:0000250|UniProtKB:Q03161};
DE            EC=5.1.3.15 {ECO:0000250|UniProtKB:Q03161};
DE   AltName: Full=Putative D-hexose-6-phosphate mutarotase {ECO:0000250|UniProtKB:Q03161};
DE   AltName: Full=Putative apospory-associated protein C;
OS   Cenchrus ciliaris (Buffelgrass) (Pennisetum ciliare).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Panicodae; Paniceae; Cenchrinae; Cenchrus.
OX   NCBI_TaxID=35872;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Higgins; TISSUE=Flower;
RA   Gustine D.L., Sherwood R.T., Hulce D.A.;
RT   "A strategy for cloning apomixis-associated cDNA markers from
RT   buffelgrass.";
RL   (In) Baker M.J., Crush J.R., Humphreys L.R. (eds.);
RL   Proceedings of the XVII international grassland congress, pp.2:1033-1034,
RL   Dunmore Press, Palmerston North (1993).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-glucose 6-phosphate = beta-D-glucose 6-phosphate;
CC         Xref=Rhea:RHEA:16249, ChEBI:CHEBI:58225, ChEBI:CHEBI:58247;
CC         EC=5.1.3.15; Evidence={ECO:0000250|UniProtKB:Q03161};
CC   -!- SIMILARITY: Belongs to the glucose-6-phosphate 1-epimerase family.
CC       {ECO:0000305}.
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DR   EMBL; U13148; AAA80575.1; -; mRNA.
DR   AlphaFoldDB; Q40784; -.
DR   SMR; Q40784; -.
DR   PRIDE; Q40784; -.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0047938; F:glucose-6-phosphate 1-epimerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd09020; D-hex-6-P-epi_like; 1.
DR   Gene3D; 2.70.98.10; -; 1.
DR   InterPro; IPR008183; Aldose_1/G6P_1-epimerase.
DR   InterPro; IPR025532; G6P_1-epimerase.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR014718; GH-type_carb-bd.
DR   Pfam; PF01263; Aldose_epim; 1.
DR   PIRSF; PIRSF016020; PHexose_mutarotase; 1.
DR   SUPFAM; SSF74650; SSF74650; 1.
PE   2: Evidence at transcript level;
KW   Isomerase.
FT   CHAIN           1..329
FT                   /note="Putative glucose-6-phosphate 1-epimerase"
FT                   /id="PRO_0000213034"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        183
FT                   /evidence="ECO:0000250|UniProtKB:Q03161"
FT   ACT_SITE        287
FT                   /evidence="ECO:0000250|UniProtKB:Q03161"
FT   BINDING         82
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q03161"
FT   BINDING         100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q03161"
FT   BINDING         105
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q03161"
FT   BINDING         228
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q03161"
SQ   SEQUENCE   329 AA;  36401 MW;  F1B8E447A077DFC1 CRC64;
     MAAPAPAGAA ASPSPKPQLP SPFAELVKTP SGLEKVVLRG ARNCCAEIYL YGGQVTSWKN
     DNGEELLFLS SKAIFKPPKA IRGGIPICLP QFGTHGNLEQ HGFARNRFWS IDNDPPPLPV
     NPAIKAFVDL ILRPAEEDLK IWPHSFEFRL RVALGPSGDL SLTSRIRNTN TDGRPFSYTF
     AYHTYFFVSD ISEVRVEGLE TMDYLDNLKA KERFTEQGDA IVFESEVDKV YLAAPSKIAI
     IDHEKKKTFV VTKEGLPDAV VWNPWDKKAK AMQDFGDAEY KNMLCVEPAA VEKPITLKPG
     EEWRGRIALS AVPSSYCSGQ LDPLKVLHG