(data stored in SCRATCH zone)

SWISSPROT: C1E0Y4_MICCC

ID   C1E0Y4_MICCC            Unreviewed;       437 AA.
AC   C1E0Y4;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   07-JUN-2017, entry version 39.
DE   RecName: Full=Phosphoglycerate kinase {ECO:0000256|RuleBase:RU000532};
DE            EC=2.7.2.3 {ECO:0000256|RuleBase:RU000532};
GN   Name=PGK_1 {ECO:0000313|EMBL:ACO62083.1};
GN   ORFNames=MICPUN_104767 {ECO:0000313|EMBL:ACO62083.1};
OS   Micromonas commoda (strain RCC299 / NOUM17 / CCMP2709) (Picoplanktonic
OS   green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; prasinophytes; Mamiellophyceae;
OC   Mamiellales; Mamiellaceae; Micromonas.
OX   NCBI_TaxID=296587 {ECO:0000313|EMBL:ACO62083.1, ECO:0000313|Proteomes:UP000002009};
RN   [1] {ECO:0000313|EMBL:ACO62083.1, ECO:0000313|Proteomes:UP000002009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC299 / NOUM17 {ECO:0000313|Proteomes:UP000002009};
RX   PubMed=19359590; DOI=10.1126/science.1167222;
RA   Worden A.Z., Lee J.H., Mock T., Rouze P., Simmons M.P., Aerts A.L.,
RA   Allen A.E., Cuvelier M.L., Derelle E., Everett M.V., Foulon E.,
RA   Grimwood J., Gundlach H., Henrissat B., Napoli C., McDonald S.M.,
RA   Parker M.S., Rombauts S., Salamov A., Von Dassow P., Badger J.H.,
RA   Coutinho P.M., Demir E., Dubchak I., Gentemann C., Eikrem W.,
RA   Gready J.E., John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F.,
RA   Moreau H., Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I.,
RA   Piegu B., Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T.,
RA   Zelensky A., Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W.,
RA   Van de Peer Y., Grigoriev I.V.;
RT   "Green evolution and dynamic adaptations revealed by genomes of the
RT   marine picoeukaryotes Micromonas.";
RL   Science 324:268-272(2009).
CC   -!- CATALYTIC ACTIVITY: ATP + 3-phospho-D-glycerate = ADP + 3-phospho-
CC       D-glyceroyl phosphate. {ECO:0000256|RuleBase:RU000532}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|RuleBase:RU000696}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000256|RuleBase:RU000532}.
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DR   EMBL; CP001324; ACO62083.1; -; Genomic_DNA.
DR   RefSeq; XP_002500825.1; XM_002500779.1.
DR   GeneID; 8241570; -.
DR   KEGG; mis:MICPUN_104767; -.
DR   HOGENOM; HOG000227107; -.
DR   InParanoid; C1E0Y4; -.
DR   KO; K00927; -.
DR   Proteomes; UP000002009; Chromosome 3.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004618; F:phosphoglycerate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:InterPro.
DR   CDD; cd00318; Phosphoglycerate_kinase; 1.
DR   Gene3D; 3.40.50.1260; -; 2.
DR   HAMAP; MF_00145; Phosphoglyc_kinase; 1.
DR   InterPro; IPR001576; Phosphoglycerate_kinase.
DR   InterPro; IPR015911; Phosphoglycerate_kinase_CS.
DR   InterPro; IPR015824; Phosphoglycerate_kinase_N.
DR   PANTHER; PTHR11406; PTHR11406; 1.
DR   Pfam; PF00162; PGK; 1.
DR   PIRSF; PIRSF000724; Pgk; 1.
DR   PRINTS; PR00477; PHGLYCKINASE.
DR   SUPFAM; SSF53748; SSF53748; 1.
DR   PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; C1E0Y4.
DR   SWISS-2DPAGE; C1E0Y4.
KW   ATP-binding {ECO:0000256|PIRSR:PIRSR000724-2};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002009};
KW   Kinase {ECO:0000256|RuleBase:RU000532, ECO:0000313|EMBL:ACO62083.1};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000724-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002009};
KW   Transferase {ECO:0000256|RuleBase:RU000532}.
FT   NP_BIND     393    396       ATP. {ECO:0000256|PIRSR:PIRSR000724-2}.
FT   REGION       63     65       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000724-1}.
FT   REGION      102    105       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000724-1}.
FT   BINDING      79     79       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000724-1}.
FT   BINDING     161    161       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000724-1}.
FT   BINDING     194    194       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000724-1}.
FT   BINDING     245    245       ATP. {ECO:0000256|PIRSR:PIRSR000724-2}.
FT   BINDING     367    367       ATP. {ECO:0000256|PIRSR:PIRSR000724-2}.
SQ   SEQUENCE   437 AA;  46110 MW;  8549520B083CC7CC CRC64;
     MAAFAAAPAL SARAFFAKSS VRAKKTSVRA QARAALKVEA KKKSVGDLKK ADLEGKTVFV
     RCDLNVPLDK DLKITDDTRI RAAIPTLEYL VENGAKVLVT SHLGRPKDGP EDKFRLTPVG
     ARLSELLSCS VSKVDDCVGD VVKDAVGGMA NGSVCLLENV RFYKDEEKNG KDFAKQLSEY
     ADLYVNDAFG TAHRAHASTA GVTEFLSPSV AGFLLQKELD YLDGAVSNPD RPFCAIVGGS
     KVSSKIGVIE TLLNKADKVI LGGGMIFTFY KALGKDVGSS LVEDDKIDLA KELMAKAEEK
     GVKLLLPTDV VVADAFAADA KTQTVSVDAI PDGWMGLDIG PDSVKEFQKE LNECKSVIWN
     GPMGVFEMDA FAKGTFAIAD TLANLDGITI IGGGDSVAAV EKAGLADKMS HISTGGGASL
     ELLEGKVLPG VDALDEA
//

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