ID A0A0P7I270_9RHOB Unreviewed; 541 AA.
AC A0A0P7I270;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent) {ECO:0000256|ARBA:ARBA00012728};
DE EC=5.4.2.2 {ECO:0000256|ARBA:ARBA00012728};
GN ORFNames=AKJ29_02720 {ECO:0000313|EMBL:KPN63074.1};
OS Aliiroseovarius crassostreae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Aliiroseovarius.
OX NCBI_TaxID=154981 {ECO:0000313|EMBL:KPN63074.1, ECO:0000313|Proteomes:UP000050471};
RN [1] {ECO:0000313|EMBL:KPN63074.1, ECO:0000313|Proteomes:UP000050471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CV919-312 {ECO:0000313|EMBL:KPN63074.1,
RC ECO:0000313|Proteomes:UP000050471};
RA Kessner L., Spinard E., Nelson D.;
RT "Draft genome sequence of Aliiroseovarius crassostreae CV919-312TSm, the
RT causative agent of Roseovarius Oyster Disease (formerly Juvenile Oyster
RT Disease).";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate;
CC Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601;
CC EC=5.4.2.2; Evidence={ECO:0000256|ARBA:ARBA00000443};
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPN63074.1}.
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DR EMBL; LKBA01000007; KPN63074.1; -; Genomic_DNA.
DR RefSeq; WP_055190721.1; NZ_LKBA01000007.1.
DR AlphaFoldDB; A0A0P7I270; -.
DR STRING; 154981.AKJ29_02720; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000050471; Unassembled WGS sequence.
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:SF2; PHOSPHOGLUCOMUTASE; 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};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000050471}.
FT DOMAIN 13..151
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 183..284
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 293..405
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 541 AA; 56712 MW; D3C173E3105A2BA1 CRC64;
MIITVPTSPI EGQIPGTSGL RKKTAVFSAP GYLETYVQAT LNAVGAAGKT FVVGGDGRFF
NREAIAVILR MAAANGVRKV IVGQDGILST PAASHLIRKC GADGGFILSA SHNPGGPNGD
FGLKYNIANG GPAPEAVTDA IIKAAQNISE YHLIDRDAPV LSGIGISQLG EMEIEVVDPV
SDYAALMEDL FDFDAIRALI AGGFSLRFDA MHAVTGPYAH EILVNRLGAS RKTVLNGTPS
EDFGGGHPDP NPVWAKPLYD LMMGPDAPDF AAASDGDGDR NMILGRGIYV TPSDSLAVLA
ANAHLAPGYA GGIRGIARSM PTSGASDRVA EALGVDAFQT PTGWKYFGTL LDAGRATLCG
EESAGTGSDH VREKDGLWAV LLWLNILAVR KQPVADILTA HWARFGRNYY SRHDYEAVDA
AIANRVMTGL EAQFPTLAGQ RFGALTVARA ESFSYVDPVD GSETSGQGLI ISFECGARFM
MRLSGTGTEG ATIRVYLESY EGPQGDHSHD AQDALAGVIA ACEQIAGIRQ ASGRSGPDVI
S
//
