ID F2AY45_RHOBT Unreviewed; 604 AA.
AC F2AY45;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Phosphoglucomutase/phosphomannomutase family protein {ECO:0000313|EMBL:EGF25362.1};
GN ORFNames=RBWH47_00832 {ECO:0000313|EMBL:EGF25362.1};
OS Rhodopirellula baltica WH47.
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=991778 {ECO:0000313|EMBL:EGF25362.1, ECO:0000313|Proteomes:UP000006222};
RN [1] {ECO:0000313|EMBL:EGF25362.1, ECO:0000313|Proteomes:UP000006222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH47 {ECO:0000313|EMBL:EGF25362.1,
RC ECO:0000313|Proteomes:UP000006222};
RX PubMed=23273849;
RA Wegner C.E., Richter-Heitmann T., Klindworth A., Klockow C., Richter M.,
RA Achstetter T., Glockner F.O., Harder J.;
RT "Expression of sulfatases in Rhodopirellula baltica and the diversity of
RT sulfatases in the genus Rhodopirellula.";
RL Mar. Genomics 0:0-0(2012).
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:EGF25362.1}.
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; AFAR01000232; EGF25362.1; -; Genomic_DNA.
DR AlphaFoldDB; F2AY45; -.
DR PATRIC; fig|991778.3.peg.4924; -.
DR Proteomes; UP000006222; Unassembled WGS sequence.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR016066; A-D-PHexomutase_CS.
DR PANTHER; PTHR45745:SF1; PHOSPHOGLUCOMUTASE 2A-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 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;
FT DOMAIN 65..199
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 236..329
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 344..467
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 604 AA; 65792 MW; 4D0C5FC5885BDA31 CRC64;
MTVDEALAAI DQACQEKKLT AGAVENIRSW LTEDRYRDYC DQTIQHIADG MWQKLDDVFW
TIIPFGTGGR RGRMYEIGSN AINDRTIGES AQGLADYVVQ YHGGAKQLSC AIAYDTRHKS
RHFTELCAGI MVAAGFKVYL LDDYRATPQL SFAVRHLNCD CGIMVTASHN PPSDNAVKVY
WSTGGQVLPP HDKAIIDGVM SCQEIRATPF AEAMADGRIE VVTDQIDAAF IDAASQCAFE
GSRDVKVLYS PLHGVGEEAV VPLMKRDGFT QLDVYEGHRE KSGDFPNVPG HVSNPENAAV
FEAPIETARA GGYDLVLATD PDCDRLGVAA PLTTDPSGEW GTFTGNQIAA LLADYVLEQT
VKSGKLTERS YVIKTLVTTE LVRRIAESHG ARCVGDLLVG YKYIAEAMDR EGPEDFVYGC
EESHGYLVGT YARDKDGAVA CMLMGELAAK LKAEGKSMHQ YMAGLYSKHG LHRENLINVF
MEGSEGMAAM QGLMKAFRAE PPKSLGGIAV SQVRDYGSAT ILNVAEGSTS PLEGPSGNLV
IMDLEMDGNY VAVRPSGTEP KVKFYVFTRL EAAESQDASA ADIKLSDRLR AIEEDVRDFA
RLHS
//