ID A0A087QI54_APTFO Unreviewed; 583 AA.
AC A0A087QI54;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Glucose 1,6-bisphosphate synthase {ECO:0000313|EMBL:KFM00908.1};
DE Flags: Fragment;
GN ORFNames=AS27_10688 {ECO:0000313|EMBL:KFM00908.1};
OS Aptenodytes forsteri (Emperor penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC Aptenodytes.
OX NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM00908.1, ECO:0000313|Proteomes:UP000053286};
RN [1] {ECO:0000313|EMBL:KFM00908.1, ECO:0000313|Proteomes:UP000053286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM00908.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231}.
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DR EMBL; KL225614; KFM00908.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087QI54; -.
DR STRING; 9233.A0A087QI54; -.
DR Proteomes; UP000053286; Unassembled WGS sequence.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; 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 PANTHER; PTHR45745:SF2; GLUCOSE 1,6-BISPHOSPHATE SYNTHASE; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000053286}.
FT DOMAIN 29..172
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 203..307
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 345..430
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFM00908.1"
FT NON_TER 583
FT /evidence="ECO:0000313|EMBL:KFM00908.1"
SQ SEQUENCE 583 AA; 65869 MW; 2D6C4C67CF04B9FB CRC64;
QNEKTKEQIE SLLQNGKHKE LRDRLCCRLT FGTAGLRSAM GAGFCYINDL TVIQSTQGIY
KYLERCFSDF KQRGFVVGYD TRGQVTSNCS SKKLAKLTAA VLLAKDVPVY FFSTYVPTPF
VPYAVQQLKA VAGVMITASH NRKEDNGYKV YWENGAQITS PHDKEIIKCI EECVEPWNGS
WNENLVDTSP LRQDPLKKIC DCYMEDLKKI CYHRELNVQT NLKFVHTSFH GVGHDYVQLA
FKAFGFQPPI PVPEQKDPDP DFSTVKCPNP EEGESVLELS LRLAEKENAK VVVATDPDAD
RLAVAEQQEK MKVCATWCVY YKNGVLFDGF VTNTYRLHNV PSGAQITSRK TSLSFSVLTL
QQSFPLTETL PGFKWIGSRV KDLLDNGKEV LFAFEESIGF MCGTSVLDKD GVSAAVVIAE
MATYLEGKNL TLAQKLIEIY EMYGYHISKT SYFLCYDPPT IKRIFEKLRN FDAPQSYPKF
CGIYNILHVR DITTGYDSSQ PNKKSVLPVS KSSQMITFTF QNGCVATLRT SGTEPKIKYY
AEMCALPEQS DRTVLEEELQ KLIEALIENF LEPDKNGLIW RSA
//
