ID M7C5T9_CHEMY Unreviewed; 591 AA.
AC M7C5T9;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Phosphoglucomutase-2 {ECO:0000313|EMBL:EMP35877.1};
GN ORFNames=UY3_06953 {ECO:0000313|EMBL:EMP35877.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP35877.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
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, ECO:0000256|RuleBase:RU004326}.
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DR EMBL; KB527356; EMP35877.1; -; Genomic_DNA.
DR AlphaFoldDB; M7C5T9; -.
DR STRING; 8469.M7C5T9; -.
DR Proteomes; UP000031443; 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: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 InterPro; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR PANTHER; PTHR45745; PHOSPHOMANNOMUTASE 45A; 1.
DR PANTHER; PTHR45745:SF3; PHOSPHOPENTOMUTASE; 1.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 1.
DR PRINTS; PR00509; PGMPMM.
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 Magnesium {ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|RuleBase:RU004326};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443}.
FT DOMAIN 128..180
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 207..312
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 323..451
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 591 AA; 65055 MW; 6926B8097A130735 CRC64;
MAPMHRGSQG AAHIAPTPIA APTAPIGWEL QSVGAAGVVP ADRAACRTAW LRLCVGAGGG
TCCSFLEMLE NTKTSEIVKQ LVAEENAGEL QKCFGSRMEF GTAGLRAAMG AGISQMNDLT
VIQTTQPYTI THLKLSAGIM ITASHNPKQD NGYKVYWENG AQITSPHDKG ISQAIEENQE
PWPQAWDDSL VDSSLLLHDP YVTINKDYFK DIQKHCFHRN INKETKLKFT HTSVHGVGHE
FVQSAFKAFD FKPPLAVPEQ KDPDPEFPTV KYPNPEEGKG VLTLSFALAE KEGAGIILAN
DPDADRLLVA EKQESGEWKV FSGNELGALL GWWIFTCWKN QNQDPAAIKD VYMLSSTVSS
KILRAIALKE GFHFEETLTG FKWMGNRAKQ LTDQGKTVLF AFEEAIGYMC SPVVLDKDGV
SAAVITAEMS SWLATKNLSL SLQLKAIYDE YGYHITKASY FICHDPKTVK ELFENLRNYD
GKNTYPKSCG KFKVSGVRDL TTGYDSSQPD QKAVLPTSKS SQMITFTFAN GGVATMRTSG
TEPKIKYYAE LCAPPGNSDP DQLKEELGEL VSAIEEYFFQ PEKNKLQPKA E
//