(data stored in ACNUC7421 zone)

SWISSPROT: PCKA_PSEHT

ID   PCKA_PSEHT              Reviewed;         513 AA.
AC   Q3ILP3;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   07-JUN-2017, entry version 78.
DE   RecName: Full=Phosphoenolpyruvate carboxykinase (ATP) {ECO:0000255|HAMAP-Rule:MF_00453};
DE            Short=PCK {ECO:0000255|HAMAP-Rule:MF_00453};
DE            Short=PEP carboxykinase {ECO:0000255|HAMAP-Rule:MF_00453};
DE            Short=PEPCK {ECO:0000255|HAMAP-Rule:MF_00453};
DE            EC=4.1.1.49 {ECO:0000255|HAMAP-Rule:MF_00453};
GN   Name=pckA {ECO:0000255|HAMAP-Rule:MF_00453};
GN   OrderedLocusNames=PSHAa0228;
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- FUNCTION: Involved in the gluconeogenesis. Catalyzes the
CC       conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP)
CC       through direct phosphoryl transfer between the nucleoside
CC       triphosphate and OAA. {ECO:0000255|HAMAP-Rule:MF_00453}.
CC   -!- CATALYTIC ACTIVITY: ATP + oxaloacetate = ADP + phosphoenolpyruvate
CC       + CO(2). {ECO:0000255|HAMAP-Rule:MF_00453}.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00453};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00453};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00453}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00453}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00453}.
CC   -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase (ATP)
CC       family. {ECO:0000255|HAMAP-Rule:MF_00453}.
DR   EMBL; CR954246; CAI85331.1; -; Genomic_DNA.
DR   RefSeq; WP_011326945.1; NC_007481.1.
DR   ProteinModelPortal; Q3ILP3; -.
DR   SMR; Q3ILP3; -.
DR   STRING; 326442.PSHAa0228; -.
DR   EnsemblBacteria; CAI85331; CAI85331; PSHAa0228.
DR   KEGG; pha:PSHAa0228; -.
DR   PATRIC; fig|326442.8.peg.219; -.
DR   eggNOG; ENOG4105DJ1; Bacteria.
DR   eggNOG; COG1866; LUCA.
DR   HOGENOM; HOG000271471; -.
DR   KO; K01610; -.
DR   OMA; MRYAGEM; -.
DR   OrthoDB; POG091H03CD; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004612; F:phosphoenolpyruvate carboxykinase (ATP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR   CDD; cd00484; PEPCK_ATP; 1.
DR   Gene3D; 3.40.449.10; -; 1.
DR   Gene3D; 3.90.228.20; -; 2.
DR   HAMAP; MF_00453; PEPCK_ATP; 1.
DR   InterPro; IPR001272; PEP_carboxykinase_ATP.
DR   InterPro; IPR013035; PEP_carboxykinase_C.
DR   InterPro; IPR008210; PEP_carboxykinase_N.
DR   InterPro; IPR015994; PEPCK_ATP_CS.
DR   PANTHER; PTHR30031; PTHR30031; 1.
DR   Pfam; PF01293; PEPCK_ATP; 1.
DR   PIRSF; PIRSF006294; PEP_crbxkin; 1.
DR   SUPFAM; SSF68923; SSF68923; 1.
DR   TIGRFAMs; TIGR00224; pckA; 1.
DR   PROSITE; PS00532; PEPCK_ATP; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3ILP3.
DR   SWISS-2DPAGE; Q3ILP3.
KW   ATP-binding; Complete proteome; Cytoplasm; Decarboxylase;
KW   Gluconeogenesis; Lyase; Manganese; Metal-binding; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN         1    513       Phosphoenolpyruvate carboxykinase (ATP).
FT                                /FTId=PRO_0000236932.
FT   NP_BIND     219    227       ATP. {ECO:0000255|HAMAP-Rule:MF_00453}.
FT   METAL       184    184       Manganese. {ECO:0000255|HAMAP-
FT                                Rule:MF_00453}.
FT   METAL       203    203       Manganese; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00453}.
FT   METAL       240    240       Manganese. {ECO:0000255|HAMAP-
FT                                Rule:MF_00453}.
FT   BINDING      44     44       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00453}.
FT   BINDING     178    178       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00453}.
FT   BINDING     184    184       ATP. {ECO:0000255|HAMAP-Rule:MF_00453}.
FT   BINDING     184    184       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00453}.
FT   BINDING     203    203       ATP. {ECO:0000255|HAMAP-Rule:MF_00453}.
FT   BINDING     268    268       ATP. {ECO:0000255|HAMAP-Rule:MF_00453}.
FT   BINDING     304    304       ATP. {ECO:0000255|HAMAP-Rule:MF_00453}.
FT   BINDING     304    304       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00453}.
FT   BINDING     430    430       ATP. {ECO:0000255|HAMAP-Rule:MF_00453}.
SQ   SEQUENCE   513 AA;  56108 MW;  448BA0FD93ABE5A9 CRC64;
     MTSSATRFVD LTAAELVEHA IRRGEGTLAA NGAFVANTGH RTGRSPKDRF IVQESSTENE
     IQWGNVNRPF DADKFDALWA RVEAYVQSND HFISHLEVGA DPEHYLPVVV TTETAWHHIF
     AKNMFIQPKS YNSSDVPQWQ VMNVPSFVCE PERDGTNSDG TVLINFAQRK VLLAGMRYAG
     EMKKSMFSVQ NFLLPAKGVL PMHCSANVGE AGDTALFFGL SGTGKTTLSA DPTRFLIGDD
     EHGWAPGSVF NIEGGCYAKC IDLSQKNEPV IWDAIRFGTI LENVVLDENR VPDFNDTSLT
     QNSRAAYPLE HVEKRKVENR AGEPKAVVFL TCDVSGVLPP VSILTEEAAA FHFLSGYTAK
     VGSTEIGSTS DIESTFSTCF GAPFFPRPAG VYAELLMKRV REFGAKVYLV NTGWTGGPYG
     TGKRFDIPTT RAVVDAIVSG KLVGVETQHI DVLNLDVPVA VPGVDSNLLN PINTWEDKAK
     YAEYAAKLAA DFTENFTKYD VSDEIKNAGP KAQ
//

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