ID Q7V317_PROMP Unreviewed; 486 AA.
AC Q7V317;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE SubName: Full=Phosphotransferase superclass {ECO:0000313|EMBL:CAE18737.1};
DE EC=5.4.2.- {ECO:0000313|EMBL:CAE18737.1};
GN OrderedLocusNames=PMM0278 {ECO:0000313|EMBL:CAE18737.1};
OS Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 /
OS MED4).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=59919 {ECO:0000313|EMBL:CAE18737.1, ECO:0000313|Proteomes:UP000001026};
RN [1] {ECO:0000313|EMBL:CAE18737.1, ECO:0000313|Proteomes:UP000001026}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1986 / NIES-2087 / MED4
RC {ECO:0000313|Proteomes:UP000001026};
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}.
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DR EMBL; BX548174; CAE18737.1; -; Genomic_DNA.
DR RefSeq; WP_011131915.1; NC_005072.1.
DR AlphaFoldDB; Q7V317; -.
DR STRING; 59919.PMM0278; -.
DR KEGG; pmm:PMM0278; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_7_1_3; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000001026; 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: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:CAE18737.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:CAE18737.1}.
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..385
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 438..471
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 486 AA; 55447 MW; 2993ADE1E5656701 CRC64;
MSSNELDEIK FGTDGWRGII GFDFNLSNLS RVVVASCQEL YYQYFEETNS KKILIGYDRR
FMANEFAKEI ASFVKGCGFE PILSTSYVPT PSCSLYAKKF MFLGCLVITA SHNPYNWLGL
KIKSFKGCSV DESFTKEVEK RLLLGNSIER LEGAYEKVDI KKFHLDQIKS NFNIDFIANN
LKKMNLHIFV DSMHGSAANC LSQIFEGYDS KIFTEIRADY DPLFGGNPPE PLLKYLDNLT
KTLTKTSKNG IKTLGIIFDG DGDRIAVIDE KGRFCSTQVL LPFFISYLGE KNKNLYPVLK
TVSGSDIISN IAKNQDREVF ELPVGFKYIA KKMIKEKIFI GGEESGGVGF GDFMPERDAL
YAAMILLNGI AEKSKYLYET LDQIQENFGP SFYRRIDVKF PNQSEKEILE KYIKNNIPSK
ICGYSIKSVS NIDGIKLRMD NNFWLLFRFS GTEPLLRLYC EAKSENDLNE VLEWSQKYIN
KVKNIK
//
