ID X7F9J5_9RHOB Unreviewed; 543 AA.
AC X7F9J5;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=RISW2_04610 {ECO:0000313|EMBL:ETX28786.1};
OS Roseivivax isoporae LMG 25204.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseivivax.
OX NCBI_TaxID=1449351 {ECO:0000313|EMBL:ETX28786.1, ECO:0000313|Proteomes:UP000023430};
RN [1] {ECO:0000313|EMBL:ETX28786.1, ECO:0000313|Proteomes:UP000023430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 25204 {ECO:0000313|EMBL:ETX28786.1,
RC ECO:0000313|Proteomes:UP000023430};
RA Lai Q., Li G., Shao Z.;
RT "Roseivivax isoporae LMG 25204 Genome Sequencing.";
RL Submitted (JAN-2014) 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:ETX28786.1}.
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DR EMBL; JAME01000015; ETX28786.1; -; Genomic_DNA.
DR RefSeq; WP_043770709.1; NZ_JAME01000015.1.
DR AlphaFoldDB; X7F9J5; -.
DR STRING; 1449351.RISW2_04610; -.
DR PATRIC; fig|1449351.3.peg.2259; -.
DR eggNOG; COG0033; Bacteria.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000023430; 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:UP000023430}.
FT DOMAIN 14..153
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 184..286
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 295..407
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 543 AA; 57950 MW; A9D0F50FFCF38D08 CRC64;
MDIITVDTAP IAGQKPGTSG LRKKTRTFME PHFLENFVQA IWQGIGGVQG KTLVLGGDGR
YFSDRAAQVI LRMAAASGAS RMIVGQNALL STPAASHLIR SRGTDGGIIL SASHNPGGPD
GDFGVKFNTA NGGPAPESVT SKIFEATKSL TQYRIMETQD VDLSALGTTS LGRMEIEVVD
PVADYAELMA QIFDFDKLRA LFAGGFRMRF DAMHAVTGPY AKAILEDTLG AAPGTVVNGT
PSPDFGEGHP DPNPIWAKDL MDAMHSADGP DFGAASDGDG DRNMIVGRNC YVTPSDSVAV
LAANATLVPG YADGLAGVAR SMPTSRALDR VAEKLDIDCY ETPTGWKFFG NLLDAGRATL
CGEESAGTGS DHVREKDGLW AVLFWLNILA ERKIPVAELM ADHWKTYGRN YYSRHDYEAV
DTDVANALMD DLRARLADLP GQEVAGQTVE TADEFAYDDP VDGSRAEAQG LRVTTREGGR
IVFRLSGTGT EGATIRVYLE RVETDPTAVD DDPQEALAPV IRAADALTGL AERTGRSRPD
VIT
//
