ID Q7V4S4_PROMM Unreviewed; 487 AA.
AC Q7V4S4;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 116.
DE SubName: Full=Phosphotransferase superclass {ECO:0000313|EMBL:CAE22046.1};
DE EC=5.4.2.- {ECO:0000313|EMBL:CAE22046.1};
GN OrderedLocusNames=PMT_1871 {ECO:0000313|EMBL:CAE22046.1};
OS Prochlorococcus marinus (strain MIT 9313).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=74547 {ECO:0000313|EMBL:CAE22046.1, ECO:0000313|Proteomes:UP000001423};
RN [1] {ECO:0000313|EMBL:CAE22046.1, ECO:0000313|Proteomes:UP000001423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9313 {ECO:0000313|Proteomes:UP000001423};
RX PubMed=12917642; DOI=10.1038/nature01947;
RA Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA Chisholm S.W.;
RT "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT differentiation.";
RL Nature 424:1042-1047(2003).
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}.
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DR EMBL; BX548175; CAE22046.1; -; Genomic_DNA.
DR RefSeq; WP_011131238.1; NC_005071.1.
DR AlphaFoldDB; Q7V4S4; -.
DR KEGG; pmt:PMT_1871; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_7_1_3; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000001423; Chromosome.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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; IPR016066; A-D-PHexomutase_CS.
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.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:CAE22046.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004326};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001423};
KW Transferase {ECO:0000313|EMBL:CAE22046.1}.
FT DOMAIN 14..147
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 168..276
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 284..389
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 431..474
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 487 AA; 52068 MW; 233189741FE24CEA CRC64;
MASAPLPLAA APIHFGTDGW RGVIGVDITV ERLLTVAAAA AQELAYRAPT ELKSRSVIIG
YDRRFLAPEM AEAIAAAVRG CELEPLLTET PVPTPACSWA VVQHQAIGAL VVTASHNPPE
WLGLKIKGAF GGSVEDTFTA AVEQRLAAGG ISVPINGITK RFDGRGQHLK GLREKLDLTS
LIKGLQKMGL KVIIDPMHGS AAGCIAELLD PHNQGLVQEI RAQRDPLFGG NPPEPLAPYL
SQLIAAVQAS SATGQPAVGL VFDGDGDRIA AIDEAGNFCS TQLLMPLLID HLARAKQLPG
KVVKTVSGSD LMRLVAEDLG REVLELPVGF KYIAAEMLSG DVLVGGEESG GVGFGMHLPE
RDALFAALLV LEALVEGGQP LGARMKALQE RCRGSSFYER FDLRLADMDS RQRLETLLEQ
TPPATVADQP VQTVIRTDGV KFRLGPSHWL MLRFSGTEPL LRIYCEAPSE TDVKAALNWA
KQLAERT
//