ID A0A151PBT7_ALLMI Unreviewed; 347 AA.
AC A0A151PBT7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Glucose-6-phosphatase {ECO:0000256|PIRNR:PIRNR000905};
DE EC=3.1.3.9 {ECO:0000256|PIRNR:PIRNR000905};
GN Name=G6PC3 {ECO:0000313|EMBL:KYO46577.1};
GN ORFNames=Y1Q_0018355 {ECO:0000313|EMBL:KYO46577.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO46577.1};
RN [1] {ECO:0000313|EMBL:KYO46577.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO46577.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000256|ARBA:ARBA00004742, ECO:0000256|PIRNR:PIRNR000905}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glucose-6-phosphatase family.
CC {ECO:0000256|ARBA:ARBA00009266, ECO:0000256|PIRNR:PIRNR000905}.
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:KYO46577.1}.
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DR EMBL; AKHW03000499; KYO46577.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151PBT7; -.
DR STRING; 8496.A0A151PBT7; -.
DR eggNOG; ENOG502QS5D; Eukaryota.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000050525; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004346; F:glucose-6-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR InterPro; IPR016275; Glucose-6-phosphatase.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR PANTHER; PTHR12591; GLUCOSE-6-PHOSPHATASE; 1.
DR PANTHER; PTHR12591:SF2; GLUCOSE-6-PHOSPHATASE 3; 1.
DR Pfam; PF01569; PAP2; 1.
DR PIRSF; PIRSF000905; Glucose-6-phosphatase; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|PIRNR:PIRNR000905};
KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432,
KW ECO:0000256|PIRNR:PIRNR000905};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR000905};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR000905};
KW Reference proteome {ECO:0000313|Proteomes:UP000050525};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 47..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 133..154
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 192..208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 220..242
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 75..209
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
FT ACT_SITE 136
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000905-1"
FT ACT_SITE 189
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000905-1"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000905-2"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000905-2"
SQ SEQUENCE 347 AA; 38252 MW; 72600830BB67AE6B CRC64;
MQGWGGKPQA SELFLVIPCR AAMDALYASG VLFAEVLQSG PPCLERFWLW ATFLGDPKCV
FIVCFPLAYF LNRKVGVAVL WIGLISEWLN VVLKWFLFGE RPFWWVYESG FTSKDSGQLR
QFPVSCETGP GSPSGHCMIT GAALWPMVTA LSAAASRHSS SRLVQLAPFV GYFLLLLAVG
LSRIFILAHF PHQVLGGILA GAALGWLLEA HVPTRRELRF YGLTSLGLLL SACLMYCAMI
ALGTDLDWSI HLATTWCRNP DWIRMDTRPF ASLIRDSGTA LGLGLAACSS TAIQQKHEGP
SWKHRAVCAL VALPALRLLS DTLQPENVAL WDRLQEESRV TSVLRNT
//
