ID A0A3Q0R2R5_AMPCI Unreviewed; 565 AA.
AC A0A3Q0R2R5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Phosphoglucomutase 5 {ECO:0000313|Ensembl:ENSACIP00000003620.1};
OS Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC Cichlasomatinae; Heroini; Amphilophus.
OX NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000003620.1, ECO:0000313|Proteomes:UP000261340};
RN [1] {ECO:0000313|Ensembl:ENSACIP00000003620.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231, ECO:0000256|RuleBase:RU004326}.
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DR Ensembl; ENSACIT00000003738.1; ENSACIP00000003620.1; ENSACIG00000002807.1.
DR GeneTree; ENSGT00940000158126; -.
DR OMA; YIPDYAG; -.
DR Proteomes; UP000261340; Unplaced.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 3.
DR Gene3D; 3.30.310.50; Alpha-D-phosphohexomutase, C-terminal domain; 1.
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 InterPro; IPR045244; PGM.
DR PANTHER; PTHR22573:SF27; PHOSPHOGLUCOMUTASE-LIKE PROTEIN 5; 1.
DR PANTHER; PTHR22573; PHOSPHOHEXOMUTASE FAMILY MEMBER; 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}.
FT DOMAIN 17..159
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 197..302
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 312..422
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 565 AA; 62287 MW; E385C7861999BB06 CRC64;
MLPIPVVTVQ TAPFEDQRPG TNGLRRKTAV FEGKKNYLQN YIQSVLSSID LRDRQGCTMV
VGSDGRYFSR AAIEVIVQMA AANGIGRLVI GHNGLLSTPA VSCIIRKIKA IGGIILTASH
NPGGPGGDFG IKFNVANGGP SPDTVMERIS QVSRTLEEYA ICPDLRIDLX RLGRQEFDLE
NKFKPFRVEI VDSVEVYLQL LRNIFDFTAI KSLLTGPDQL KIHIDAMNGV MGPYVRRILC
DELGAPANSA VNCVPLEDFG GRPPEPNLTY ATSLVEAMKG GDFGFGAAFD ADGDRYMILG
QNGFFVNPSD SVAIMAANLS TVPYFRQHGI KGFARSMATS TALDRVAKAM KLALYETPTG
WRYFGNLMDS GRCSVCGEES FGTGSDHIRE KDGLWSVLVW LSIMASKKQG VEQIVREHWA
RFGRNYFCRF DYEGLDPRAA FYLMRDLEAV ISDKAFTSQK FAVGDHMYSV EKADNFEYID
PVDGTVARNQ GLRIIFTDAS RLVFRMSGSG GGMGATIRIY AESFERDPER HNRETQVVLG
PLIAIALKIS NIHERTGRRG PNIIT
//
