ID A0A4R3JLX2_9RHOB Unreviewed; 497 AA.
AC A0A4R3JLX2;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE SubName: Full=Phosphomannomutase/phosphoglucomutase {ECO:0000313|EMBL:TCS66590.1};
GN ORFNames=EDD52_102407 {ECO:0000313|EMBL:TCS66590.1};
OS Primorskyibacter sedentarius.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Rhodobacterales; Roseobacteraceae; Primorskyibacter.
OX NCBI_TaxID=745311 {ECO:0000313|EMBL:TCS66590.1, ECO:0000313|Proteomes:UP000295696};
RN [1] {ECO:0000313|EMBL:TCS66590.1, ECO:0000313|Proteomes:UP000295696}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 104836 {ECO:0000313|EMBL:TCS66590.1,
RC ECO:0000313|Proteomes:UP000295696};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAR-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}.
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:TCS66590.1}.
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; SLZU01000002; TCS66590.1; -; Genomic_DNA.
DR RefSeq; WP_132242790.1; NZ_CBDUOC010000043.1.
DR AlphaFoldDB; A0A4R3JLX2; -.
DR OrthoDB; 9803322at2; -.
DR Proteomes; UP000295696; Unassembled WGS sequence.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd03089; PMM_PGM; 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; IPR005841; Alpha-D-phosphohexomutase_SF.
DR PANTHER; PTHR43771; PHOSPHOMANNOMUTASE; 1.
DR PANTHER; PTHR43771:SF2; PHOSPHOMANNOMUTASE_PHOSPHOGLUCOMUTASE; 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.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000295696}.
FT DOMAIN 24..152
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 173..270
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 276..387
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 424..481
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 497 AA; 54250 MW; B4DD3C2A95397474 CRC64;
MKPLHDVTPN TWDFLLKPMI APTGFREYDA RWKYPEEINL PGMTALGLGL GTQMRKRGIP
PVIAVGNDYR AYSLDVKNAL MIGLMQAGIT VKDIGPAVSP MAYFAQFHLD APAVAMVTAS
HNPNGWTGVK MGFERPLTHG PDEMAELRDI VMEGRGEPAP GGAWELVDGV REAYLDDLVG
DFRLSRPLRV VCATGNGTAG AFAPDLLRRI GAEVVERHCP LDYTFPHYNP NPESMEMLHD
MTACLKESGA DLALGFDGDG DRCGVVDDEG EEIFADKMGV ILARDLSAIH PGAIFVADVK
STGLFASDPV LTANGARAEY WKTGHSHMKR RVKELGALAG FEKSGHYFLA EPLGRGYDCG
LRVAVEICKL MDRHPENSLS DLRRALPRTW TSPTMSPYAS DTQKRDILAR IVARLEEMEQ
AGATLGGHKI TGMVTVNGAR VLLEGGNWAL VRASSNTPNL VVVCESTESE DDLRAIFRDI
DAVIRTEPDV GEYDQTL
//
