(data stored in SCRATCH zone)

SWISSPROT: A0KFS2_AERHH

ID   A0KFS2_AERHH            Unreviewed;       541 AA.
AC   A0KFS2;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 100.
DE   RecName: Full=Phosphoenolpyruvate carboxykinase (ATP) {ECO:0000256|HAMAP-Rule:MF_00453, ECO:0000256|SAAS:SAAS01086626};
DE            Short=PCK {ECO:0000256|HAMAP-Rule:MF_00453};
DE            Short=PEP carboxykinase {ECO:0000256|HAMAP-Rule:MF_00453};
DE            Short=PEPCK {ECO:0000256|HAMAP-Rule:MF_00453};
DE            EC=4.1.1.49 {ECO:0000256|HAMAP-Rule:MF_00453, ECO:0000256|SAAS:SAAS01086626};
GN   Name=pckA {ECO:0000256|HAMAP-Rule:MF_00453,
GN   ECO:0000313|EMBL:ABK38879.1};
GN   OrderedLocusNames=AHA_0565 {ECO:0000313|EMBL:ABK38879.1};
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 /
OS   JCM 1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK38879.1, ECO:0000313|Proteomes:UP000000756};
RN   [1] {ECO:0000313|EMBL:ABK38879.1, ECO:0000313|Proteomes:UP000000756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240
RC   {ECO:0000313|Proteomes:UP000000756};
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
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:0000256|HAMAP-Rule:MF_00453}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + oxaloacetate = ADP + CO2 + phosphoenolpyruvate;
CC         Xref=Rhea:RHEA:18617, ChEBI:CHEBI:16452, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216;
CC         EC=4.1.1.49; Evidence={ECO:0000256|HAMAP-Rule:MF_00453,
CC         ECO:0000256|SAAS:SAAS01121795};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00453};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00453};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00453, ECO:0000256|SAAS:SAAS00051732}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00453}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00453}.
CC   -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase (ATP)
CC       family. {ECO:0000256|HAMAP-Rule:MF_00453,
CC       ECO:0000256|SAAS:SAAS01086645}.
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DR   EMBL; CP000462; ABK38879.1; -; Genomic_DNA.
DR   RefSeq; WP_011704536.1; NC_008570.1.
DR   RefSeq; YP_855098.1; NC_008570.1.
DR   STRING; 380703.AHA_0565; -.
DR   EnsemblBacteria; ABK38879; ABK38879; AHA_0565.
DR   GeneID; 4489387; -.
DR   KEGG; aha:AHA_0565; -.
DR   PATRIC; fig|380703.7.peg.559; -.
DR   eggNOG; ENOG4105DJ1; Bacteria.
DR   eggNOG; COG1866; LUCA.
DR   HOGENOM; HOG000271471; -.
DR   KO; K01610; -.
DR   OMA; MRYAGEM; -.
DR   BioCyc; AHYD380703:G1G7B-566-MONOMER; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000000756; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016301; F:kinase activity; 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-UniRule.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR   CDD; cd00484; PEPCK_ATP; 1.
DR   Gene3D; 3.40.449.10; -; 1.
DR   Gene3D; 3.90.228.20; -; 1.
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; A0KFS2.
DR   SWISS-2DPAGE; A0KFS2.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00453,
KW   ECO:0000256|SAAS:SAAS01086643};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000756};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00453};
KW   Decarboxylase {ECO:0000256|HAMAP-Rule:MF_00453,
KW   ECO:0000256|SAAS:SAAS00051790};
KW   Gluconeogenesis {ECO:0000256|HAMAP-Rule:MF_00453,
KW   ECO:0000256|SAAS:SAAS00442775}; Kinase {ECO:0000313|EMBL:ABK38879.1};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00453, ECO:0000256|SAAS:SAAS00442795,
KW   ECO:0000313|EMBL:ABK38879.1};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_00453};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00453};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00453,
KW   ECO:0000256|SAAS:SAAS00071028};
KW   Pyruvate {ECO:0000313|EMBL:ABK38879.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000756};
KW   Transferase {ECO:0000313|EMBL:ABK38879.1}.
FT   NP_BIND     249    257       ATP. {ECO:0000256|HAMAP-Rule:MF_00453}.
FT   NP_BIND     450    451       ATP. {ECO:0000256|HAMAP-Rule:MF_00453}.
FT   METAL       214    214       Manganese. {ECO:0000256|HAMAP-Rule:
FT                                MF_00453}.
FT   METAL       233    233       Manganese; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00453}.
FT   METAL       270    270       Manganese. {ECO:0000256|HAMAP-Rule:
FT                                MF_00453}.
FT   BINDING      68     68       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00453}.
FT   BINDING     208    208       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00453}.
FT   BINDING     214    214       ATP. {ECO:0000256|HAMAP-Rule:MF_00453}.
FT   BINDING     214    214       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00453}.
FT   BINDING     233    233       ATP. {ECO:0000256|HAMAP-Rule:MF_00453}.
FT   BINDING     298    298       ATP. {ECO:0000256|HAMAP-Rule:MF_00453}.
FT   BINDING     334    334       ATP. {ECO:0000256|HAMAP-Rule:MF_00453}.
FT   BINDING     334    334       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00453}.
FT   BINDING     456    456       ATP. {ECO:0000256|HAMAP-Rule:MF_00453}.
SQ   SEQUENCE   541 AA;  59682 MW;  800AA9C2EB7E090F CRC64;
     MTIVAEPTLA KQLGLDQYGI KNSTEILRNP SYDQLFAEET RADLEGFERG VVTELGAVNV
     NTGIFTGRSP KDKYIVKDAT TQNTVWWSDQ GKNDNKAISP EVWSHLKSLV TKQLSGKRLF
     VVDGFCGANP DTRLAVRIIT EVAWQAHFVK NMFIRPSDEE LKTFKPDFVV MNGAKCTNPN
     WKEQGLNSEN FVAFNLTEKI QLIGGTWYGG EMKKGMFSMM NYFLPLRGIA SMHCSANVGQ
     DGDVAIFFGL SGTGKTTLST DPKRQLIGDD EHGWDDDGVF NFEGGCYAKT IKLSKEAEPD
     IYNAIRRDAL LENVTVAADG TIDFDDGSKT ENTRVSYPIY HIENIVKPVS KAGHANKVIF
     LTADAFGVLP PVSKLTKEQT KYHFLSGFTA KLAGTERGIT EPTPTFSSCF GAAFLSLHPT
     KYGQELVKRM EAAGAEAYLV NTGWNGTGKR ISIKDTRAII DAILDGSIEK AETKVLPIFN
     LEVPTALHDV NPAILDPRDT YANKAEWDAK AVDLAGRFIK NFERFTDNEE GKRLVAAGPQ
     L
//

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