ID A0A345Q5J9_9RHOB Unreviewed; 543 AA.
AC A0A345Q5J9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
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=C1J02_00315 {ECO:0000313|EMBL:AXI40586.1};
OS Sulfitobacter sp. SK011.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=1389004 {ECO:0000313|EMBL:AXI40586.1, ECO:0000313|Proteomes:UP000253968};
RN [1] {ECO:0000313|EMBL:AXI40586.1, ECO:0000313|Proteomes:UP000253968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK011 {ECO:0000313|EMBL:AXI40586.1,
RC ECO:0000313|Proteomes:UP000253968};
RA Pohlner M., Engelen B., Bunk B.;
RT "Comparative analysis of Sulfitobacter strains from the North Sea.";
RL Submitted (JAN-2018) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP025803; AXI40586.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345Q5J9; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000253968; Chromosome.
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:UP000253968}.
FT DOMAIN 14..153
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 189..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; 57632 MW; 422F4C4E4B8FC6A2 CRC64;
MKIETVSTTP IEGQMPGTSG LRKKTRVFME PRFLENFIQA TFDAIGGGAG KTFVVGGDGR
YFNKPAIQTI LKMAAANGAA TVIVGKDGIL STPAASHLIR LNGADGGFIL SASHNPGGID
EDFGVKFNAE NGGPAPEKLT AKIFAATTSI SAYKIAVTDD VDLGTIGRIQ QGQMQIHVID
PVESYQALME TLFDFDAMRG LFSAGFTMRF DAMHAVTGPY AKAILEGALG AAPGTVVNGV
PLEDFGKGHP DPNPIWAKPL MDLMMSDDAP DIGAASDGDG DRNMIVGRGI YVTPSDSLAI
LAANAHLAPA YEKGLAGIAR SMPTSAASDR VAEKLGIGAY ETPTGWKFFG NLLDAGKVTI
CGEESAGTGS DHVREKDGLW AVLLWLNILA VRKQSVAEIV MDHWQTFGRD YYSRYDYENV
AIEQASTLMD DLRAQLPQLT GKNISGLTVT SADEFSYLDP VDGSVSKNQG LRIGFAGGGR
AVFRLSGTGT QGATLRLYLE QYSGIGGDLE MDSQEALRKV RDAAQAICRM DATIGRLKPD
VIT
//
