ID A0A2K6Q479_RHIRO Unreviewed; 387 AA.
AC A0A2K6Q479;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Phosphoglucomutase 5 {ECO:0000313|Ensembl:ENSRROP00000023585.1};
GN Name=PGM5 {ECO:0000313|Ensembl:ENSRROP00000023585.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000023585.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000023585.1}
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 AlphaFoldDB; A0A2K6Q479; -.
DR Ensembl; ENSRROT00000047790.1; ENSRROP00000023585.1; ENSRROG00000035630.1.
DR GeneTree; ENSGT00940000158126; -.
DR Proteomes; UP000233200; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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 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; 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; 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:UP000233200}.
FT DOMAIN 23..162
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 200..305
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 313..385
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 387 AA; 41806 MW; C68A0F614475205F CRC64;
MEGSPIPVLT VPTAPYEDQR PAGGGGLRRP TGLFEGQRNY LPNFIQSVLS SIDLRDRQGC
TMVVGSDGRY FSRTAIEIVV QMAAANGIGR LIIGQNGILS TPAVSCIIRK IKAAGGIILT
ASHCPGGPGG EFGVKFNVAN GGPAPDVVSD KIYQISKTIE EYAICPDLRI DLSRLGRQEF
DLENKFKPFR VEIVDPVDIY LNLLRTIFDF HAIKSLLTGP SQLKIRVDAM HGVMGPYVRK
VLCDELGAPA NSAINCVPLE DFGGQHPDPN LTYATTLLEA MKGGEYGFGA AFDADGDRYM
ILGQNGFFVS PSDSLAIIAA NLSCIPYFRQ MGVRGFGRSM PTSMALDRVA KSMKVPVYET
PAGWRFFSNL MDSGRCNLCG EESFGTV
//
