(data stored in SCRATCH zone)

SWISSPROT: D3UY44_XENBS

ID   D3UY44_XENBS            Unreviewed;       539 AA.
AC   D3UY44;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 63.
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=pck {ECO:0000313|EMBL:CBJ79222.1};
GN   Synonyms=pckA {ECO:0000256|HAMAP-Rule:MF_00453};
GN   OrderedLocusNames=XBJ1_0071 {ECO:0000313|EMBL:CBJ79222.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79222.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|EMBL:CBJ79222.1, ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79222.1,
RC   ECO:0000313|Proteomes:UP000002045};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
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; FN667741; CBJ79222.1; -; Genomic_DNA.
DR   RefSeq; WP_012986693.1; NC_013892.1.
DR   STRING; 406818.XBJ1_0071; -.
DR   EnsemblBacteria; CBJ79222; CBJ79222; XBJ1_0071.
DR   GeneID; 8829697; -.
DR   KEGG; xbo:XBJ1_0071; -.
DR   PATRIC; fig|406818.4.peg.63; -.
DR   eggNOG; ENOG4105DJ1; Bacteria.
DR   eggNOG; COG1866; LUCA.
DR   HOGENOM; HOG000271471; -.
DR   KO; K01610; -.
DR   OMA; MRYAGEM; -.
DR   BioCyc; XBOV406818:XBJ1_RS00330-MONOMER; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000002045; 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; D3UY44.
DR   SWISS-2DPAGE; D3UY44.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00453,
KW   ECO:0000256|SAAS:SAAS01086643};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002045};
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:CBJ79222.1};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00453, ECO:0000256|SAAS:SAAS00442795,
KW   ECO:0000313|EMBL:CBJ79222.1};
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:CBJ79222.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002045};
KW   Transferase {ECO:0000313|EMBL:CBJ79222.1}.
FT   NP_BIND     247    255       ATP. {ECO:0000256|HAMAP-Rule:MF_00453}.
FT   NP_BIND     448    449       ATP. {ECO:0000256|HAMAP-Rule:MF_00453}.
FT   METAL       212    212       Manganese. {ECO:0000256|HAMAP-Rule:
FT                                MF_00453}.
FT   METAL       231    231       Manganese; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00453}.
FT   METAL       268    268       Manganese. {ECO:0000256|HAMAP-Rule:
FT                                MF_00453}.
FT   BINDING      64     64       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00453}.
FT   BINDING     206    206       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00453}.
FT   BINDING     212    212       ATP. {ECO:0000256|HAMAP-Rule:MF_00453}.
FT   BINDING     212    212       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00453}.
FT   BINDING     231    231       ATP. {ECO:0000256|HAMAP-Rule:MF_00453}.
FT   BINDING     296    296       ATP. {ECO:0000256|HAMAP-Rule:MF_00453}.
FT   BINDING     332    332       ATP. {ECO:0000256|HAMAP-Rule:MF_00453}.
FT   BINDING     332    332       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00453}.
FT   BINDING     454    454       ATP. {ECO:0000256|HAMAP-Rule:MF_00453}.
SQ   SEQUENCE   539 AA;  59026 MW;  E9ECA4D1C682998F CRC64;
     MSVKGITAQE LAVYGICDVS EIVYNPSYEL LFSEETQPSL QGYERGTLTH LGAVAVDTGI
     FTGRSPKDKY IVRDDVTCDT VWWADQGKGK NDNKPLSQET WSQLKGLVTQ QLSGKRLFVV
     DAFCGANADT RLKVRFITEV AWQAHFVKNM FIRPSDEELV NFTPDFIVMN GAKCTNPQWK
     EQELNSENFV AFNLTERMQL IGGTWYGGEM KKGMFSIMNY LLPLKGIASM HCSANVGGEG
     DVAIFFGLSG TGKTTLSTDP KRKLIGDDEH GWDDDGVFNF EGGCYAKTIN LSKEAEPDIY
     HAICRDALLE NVTVLADGTV DFNDGSKTEN TRVSYPIYHI ENIVKPVSKA GHATKVIFLT
     ADAFGVLPPV SCLTPEQTQY HFLSGFTAKL AGTERGVTEP TPTFSACFGA AFLSLHPTQY
     AEVLVKRMQA SGAKAYLVNT GWNGTGKRIS IKDTRAIIDA ILNGDIEDAD TIELPIFDLA
     VPTALPGVDT GILDPRNTYA DKSEWDVKAK DLAQRFVDNF DKYTDTAAGA ALVKAGPNL
//

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