ID A0A1D9E160_9MICO Unreviewed; 470 AA.
AC A0A1D9E160;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Phosphomannomutase/phosphoglucomutase {ECO:0000313|EMBL:AOY56750.1};
GN Name=manB {ECO:0000313|EMBL:AOY56750.1};
GN ORFNames=A4Z71_05320 {ECO:0000313|EMBL:AOY56750.1};
OS Candidatus Rhodoluna planktonica.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Luna cluster; Luna-1 subcluster; Rhodoluna.
OX NCBI_TaxID=535712 {ECO:0000313|EMBL:AOY56750.1, ECO:0000313|Proteomes:UP000243784};
RN [1] {ECO:0000313|EMBL:AOY56750.1, ECO:0000313|Proteomes:UP000243784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MWH-Dar1 {ECO:0000313|EMBL:AOY56750.1,
RC ECO:0000313|Proteomes:UP000243784};
RX PubMed=27659506; DOI=10.1016/j.bbabio.2016.09.006;
RA Nakamura S., Kikukawa T., Tamogami J., Kamiya M., Aizawa T., Hahn M.W.,
RA Ihara K., Kamo N., Demura M.;
RT "Photochemical characterization of actinorhodopsin and its functional
RT existence in the natural host.";
RL Biochim. Biophys. Acta 1857:1900-1908(2016).
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}.
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DR EMBL; CP015208; AOY56750.1; -; Genomic_DNA.
DR RefSeq; WP_070955266.1; NZ_CP015208.1.
DR AlphaFoldDB; A0A1D9E160; -.
DR STRING; 535712.A4Z71_05320; -.
DR KEGG; rpla:A4Z71_05320; -.
DR OrthoDB; 9803322at2; -.
DR Proteomes; UP000243784; Chromosome.
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:SF1; PHOSPHOMANNOMUTASE; 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:UP000243784}.
FT DOMAIN 8..131
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 159..263
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 270..382
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 388..468
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 470 AA; 50979 MW; BDAD5C5B0EE2DBFC CRC64;
MTVNWDAIVK TYDVRGLVGK DLTNEVVAAL AAAFVDELDA AGTDVIVGHD MRDSSPEFAE
AFAEGAQARG AHVVSIGLCS TDESYFASGA LDAPAAMFTA SHNPATYNGI KFSRAGARGI
SLDTGLAAIR DRAKVYLENG INEVDEPGSF REEHILVRYA SYLRELVSLN TIRPLKVVVD
AGNGMGGLTV PAVLGHANDL ERLPLEIVPM YFELDGTFPN HEANPLDPKN LVDLQRAVVD
YQADLGLAFD GDADRVFVVD EKGQPVTPSA VAAIVARREI AREKIQNPGA PITVLHNLLT
SNVVREVVEA DGARAVRTKV GHSLIKDKMA ETNAVFGGEH SAHYYFRDFW GADNGMLAAM
HVLAEFGNQD KSMSEFAASY NPYFLSGEIN STVADAQAAK DRIREAFADR ADFEEFDGIT
AQGKSADAGT WWWFNVRTSN TEPLLRLNVE ASNEADMIRV RDEVLSLIRA
//
