ID A0A5P9CR91_9VIBR Unreviewed; 569 AA.
AC A0A5P9CR91;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 28-JAN-2026, entry version 18.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:QFT28162.1};
DE EC=5.4.2.2 {ECO:0000313|EMBL:QFT28162.1};
GN Name=pgcA {ECO:0000313|EMBL:QFT28162.1};
GN ORFNames=FIV01_17365 {ECO:0000313|EMBL:QFT28162.1};
OS Vibrio aquimaris.
OG Plasmid pthaf100_a {ECO:0000313|Proteomes:UP000326936}.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Vibrionales;
OC Vibrionaceae; Vibrio.
OX NCBI_TaxID=2587862 {ECO:0000313|EMBL:QFT28162.1, ECO:0000313|Proteomes:UP000326936};
RN [1] {ECO:0000313|EMBL:QFT28162.1, ECO:0000313|Proteomes:UP000326936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=THAF100 {ECO:0000313|EMBL:QFT28162.1,
RC ECO:0000313|Proteomes:UP000326936};
RC PLASMID=pthaf100_a {ECO:0000313|Proteomes:UP000326936};
RA Ruckert C., Franco A., Kalinowski J., Glaeser S.;
RT "Complete genome sequence of Vibrio sp. strain THAF100, isolated from non-
RT filtered water from the water column of tank 6 of a marine aquarium
RT containing stony-coral fragments. Water maintained at 26 degree C.";
RL Submitted (OCT-2019) to the EMBL/GenBank/DDBJ databases.
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; CP045351; QFT28162.1; -; Genomic_DNA.
DR RefSeq; WP_152432203.1; NZ_CBCSDK010000008.1.
DR AlphaFoldDB; A0A5P9CR91; -.
DR KEGG; vaq:FIV01_17365; -.
DR OrthoDB; 9803322at2; -.
DR Proteomes; UP000326936; Plasmid pTHAF100_a.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0008973; F:phosphopentomutase activity; IEA:TreeGrafter.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:TreeGrafter.
DR CDD; cd05799; PGM2; 1.
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; IPR005843; A-D-PHexomutase_C.
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:SF1; PHOSPHOGLUCOMUTASE 2B-RELATED; 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 Pfam; PF00408; PGM_PMM_IV; 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 Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:QFT28162.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004326};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Plasmid {ECO:0000313|EMBL:QFT28162.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000326936}.
FT DOMAIN 41..179
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 205..313
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 322..440
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 511..538
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 569 AA; 62593 MW; EB71F17284925154 CRC64;
MKQQVTHWLE RDPDPRTREE LTKLVDDKDE REIADRFSQR LEFGTAGLRG KVGAGPNRMN
QLVIQETAAG LGHYLINNVK DAKQRGVVIG YDGRIDSKQF AHSTASVLTA LGIRVYLTHD
VAATPIVAFG VKQLNAAAAV VVTASHNPPE YNGFKVYWEN GAQIIPPHDS GIASEIEQAA
VQAIPLMSLE QAEKETRLVW LTEEYYKSYR QSVNSNSVLG YRPDTAQVSI AYTAMHGVGA
PMAKALLTDA GFTSVYSVAE QETPDGTFPT VNFPNPEEAG AMDMVIALAK QHNADIACAN
DPDADRFAVA AVKPDGSYQM LTGDQVGALF GHYLLNQTQA SKQLVGNTVV SSSLLEKIAR
SHHAEYYQTL TGFKWLTNVA MTKESPEKQF LFAYEEALGY TIGNKVWDKD GLSALVAFAQ
LVAELKQQGK TVWDQLENIY REHGMYINAQ HSTALDPNAP PIGDRLRAEQ PSHIAGRKVT
EIDDLQLSIR YHADGTSNPI DLPPSDVLIY RLDGGARVIV RPSGTEPKLK CYYEVVEEFS
IEDSFASAEA RAELSLDMLI SEHQTSLDH
//
