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Database: UniProt
Entry: Q7V4S4_PROMM
LinkDB: Q7V4S4_PROMM
Original site: Q7V4S4_PROMM 
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
//
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