ID A0A369HD31_9HYPO Unreviewed; 880 AA.
AC A0A369HD31;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=glucose-6-phosphate 1-epimerase {ECO:0000256|ARBA:ARBA00012083};
DE EC=5.1.3.15 {ECO:0000256|ARBA:ARBA00012083};
GN ORFNames=CP533_5473 {ECO:0000313|EMBL:RDA95508.1};
OS Ophiocordyceps camponoti-saundersi (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=2039874 {ECO:0000313|EMBL:RDA95508.1, ECO:0000313|Proteomes:UP000253071};
RN [1] {ECO:0000313|EMBL:RDA95508.1, ECO:0000313|Proteomes:UP000253071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC 79314 {ECO:0000313|EMBL:RDA95508.1,
RC ECO:0000313|Proteomes:UP000253071};
RA Kobmoo N., Wichadakul D., Arnamnart N., Rodriguez De La Vega R.C.,
RA Luangsa-Ard J.-J., Giraud T.;
RT "A genome scan of diversifying selection in the zombie-ant fungus
RT Ophiocordyceps unilateralis complex supports a role of enterotoxins in
RT coevolution and host-specificity.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001096};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glucose-6-phosphate 1-epimerase family.
CC {ECO:0000256|ARBA:ARBA00005866}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. {ECO:0000256|ARBA:ARBA00010992}.
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:RDA95508.1}.
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DR EMBL; PDHQ01000005; RDA95508.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369HD31; -.
DR STRING; 2039874.A0A369HD31; -.
DR Proteomes; UP000253071; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:0022857; F:transmembrane transporter activity; IEA:InterPro.
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 Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 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 InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR003663; Sugar/inositol_transpt.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR NCBIfam; TIGR00879; SP; 1.
DR PANTHER; PTHR48022:SF68; MAJOR FACILITATOR SUPERFAMILY (MFS) PROFILE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR48022; PLASTIDIC GLUCOSE TRANSPORTER 4; 1.
DR Pfam; PF01263; Aldose_epim; 1.
DR Pfam; PF00083; Sugar_tr; 1.
DR PRINTS; PR00171; SUGRTRNSPORT.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000253071};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 77..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 106..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 163..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 193..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 348..366
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 378..401
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 421..437
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 444..463
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 20..467
FT /note="Major facilitator superfamily (MFS) profile"
FT /evidence="ECO:0000259|PROSITE:PS50850"
SQ SEQUENCE 880 AA; 96806 MW; C19992F7CDC87A31 CRC64;
MARSNGYLLG LRGNGLNWAV GAVAGCDFLL FGYDQGVMGG ILTLPVFLDQ FPDINDKDPT
ISNDHALQSR RSTYQGIAVA SYNLGCFVGA VITVFVGNPL GRRRVIFFGT ALMVLGAALQ
ASASSLTHFI IGRVITGLGN GANTSTVPMW QSETCAAHKR GKFVMIEGAL ITGGIMISYW
VDLGLSFAPG SVAWRFPLAF QVVFCFFILA LVFSLPESPR WLVLKGRDDE ARRTIAAVAD
VDEQDKYVEN ELLAIKATVE EMSKGTYADL FARDKNRTLH RTLIAYVNQM FQQVSGINLI
TYYAAKIYSD LGMSPFISRL LAALNGTEYF IASWPAVFLV ERVGRRKLML FGAAGQAATM
AILAGVNSRP ENKACQVAGI VFLFVFNTFF AVGWLGMTWL YPAEITPLRT RAPANALSTS
SNWIFNFLVV MITPIAFQNI QYKTYIVFAV INAFMVPSVY FFFPETAYRS LEEMDTIFQK
VSGWRGAFTV VEQARVEPRR YGKNGELLLR VDEVVEGDKT AAVDKHNGNK TMISSSPLQN
YCLPTYPAMV DRPNKPSALA STPGLPPQAQ FFISDDGSRV TARLHTGESV DVLLYGATVI
SWKDATGSEK LWLSQGSKLD GSRAVRGGIP IVFPSNGSGA DLRVDYNKKL FGPPVASHAA
TCKLSQHGFA RSTRWEFLGK STSEGDPSSS VKLDFGLSPD NLDDATRALW PYKFGLLYSV
TLERESLNTT LVVTNQGEEP FEFQTLIHTY FKVDDISSVH VTGLEDSPYL DKTDGGKEKK
QASEPVTFSR EVDGVFTPAK GPKHPVVISE AGKELFRILR DNLDQVVVWN PWTEKAEGMT
DFMPKTGYKN MVCVEAGSVR GWQKLEKGDT FEGAQTVWLS
//
