ID A2BUQ9_PROM5 Unreviewed; 486 AA.
AC A2BUQ9;
DT 20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 20-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Phosphotransferase superclass {ECO:0000313|EMBL:ABM71520.1};
DE EC=5.4.2.2 {ECO:0000313|EMBL:ABM71520.1};
DE EC=5.4.2.8 {ECO:0000313|EMBL:ABM71520.1};
GN OrderedLocusNames=P9515_03111 {ECO:0000313|EMBL:ABM71520.1};
OS Prochlorococcus marinus (strain MIT 9515).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=167542 {ECO:0000313|EMBL:ABM71520.1, ECO:0000313|Proteomes:UP000001589};
RN [1] {ECO:0000313|EMBL:ABM71520.1, ECO:0000313|Proteomes:UP000001589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9515 {ECO:0000313|EMBL:ABM71520.1,
RC ECO:0000313|Proteomes:UP000001589};
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
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; CP000552; ABM71520.1; -; Genomic_DNA.
DR RefSeq; WP_011819629.1; NC_008817.1.
DR AlphaFoldDB; A2BUQ9; -.
DR STRING; 167542.P9515_03111; -.
DR GeneID; 60201777; -.
DR KEGG; pmc:P9515_03111; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_7_1_3; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000001589; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd05800; PGM_like2; 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; 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 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, ECO:0000313|EMBL:ABM71520.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:ABM71520.1}.
FT DOMAIN 9..142
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 164..272
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 284..387
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 431..471
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 486 AA; 55452 MW; 63E28C1FE4D7ED41 CRC64;
MSENELDKIK FGTDGWRGII GFDFNLSNLS RVVVASCQEL DYQYFDETKS KKILIGYDRR
FMASEFANEI ASYVKGCGFE PVLSHTYVPT PACSLYAKHN MFLGCLVITA SHNPYNWLGL
KIKSFKGCSV DESFTKEVEK RLLLENSIER LEGPYDKVDI KKFHLDQIKS NFNIDFIVNN
LKKMNLHIFV DSMHGSAANC ISQIFDSYDS NIFTEIRANY DPLFGGNPPE PLLKYLENLS
EILITNSKKG IKTLGIIFDG DGDRIAVIDE KGRFCSTQVL LPFFISYLGE KNKNLFPVLK
TVSGSDIIGN IAKNQNREVV ELPVGFKYIA KKMINEEIFI GGEESGGVGF GDFMPERDAL
YAAMVLLNGI AEKSKYLCET LDEIQQKFGP SFYRRIDIKF PNQSEKEIFK KFINNNIPSE
ICGHKIISIS HVDGIKLRLD NNFWLLFRFS GTEPLLRLYC EATSEYDLNE VLQWSQKFIN
RVKQNQ
//
