GenomeNet

Database: UniProt
Entry: S3IJE4_9ENTR
LinkDB: S3IJE4_9ENTR
Original site: S3IJE4_9ENTR 
ID   S3IJE4_9ENTR            Unreviewed;       539 AA.
AC   S3IJE4;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   RecName: Full=Phosphoenolpyruvate carboxykinase (ATP) {ECO:0000256|ARBA:ARBA00012363, ECO:0000256|HAMAP-Rule:MF_00453};
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|ARBA:ARBA00012363, ECO:0000256|HAMAP-Rule:MF_00453};
GN   Name=pckA {ECO:0000256|HAMAP-Rule:MF_00453};
GN   ORFNames=HMPREF0201_04358 {ECO:0000313|EMBL:EPF13165.1};
OS   Cedecea davisae DSM 4568.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Cedecea.
OX   NCBI_TaxID=566551 {ECO:0000313|EMBL:EPF13165.1, ECO:0000313|Proteomes:UP000014585};
RN   [1] {ECO:0000313|EMBL:EPF13165.1, ECO:0000313|Proteomes:UP000014585}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4568 {ECO:0000313|EMBL:EPF13165.1,
RC   ECO:0000313|Proteomes:UP000014585};
RA   Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA   Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA   Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA   Pepin K.H., Palsikar V.B., Zhang X., Suruliraj S., Perna N.T., Plunkett G.,
RA   Warren W., Mitreva M., Mardis E.R., Wilson R.K.;
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the gluconeogenesis. Catalyzes the conversion of
CC       oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct
CC       phosphoryl transfer between the nucleoside triphosphate and OAA.
CC       {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|ARBA:ARBA00001389,
CC         ECO:0000256|HAMAP-Rule:MF_00453};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00453};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00453};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000256|ARBA:ARBA00004742, ECO:0000256|HAMAP-Rule:MF_00453}.
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|ARBA:ARBA00006052, ECO:0000256|HAMAP-
CC       Rule:MF_00453}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EPF13165.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ATDT01000036; EPF13165.1; -; Genomic_DNA.
DR   RefSeq; WP_016538532.1; NZ_KE161030.1.
DR   AlphaFoldDB; S3IJE4; -.
DR   STRING; 566551.HMPREF0201_04358; -.
DR   PATRIC; fig|566551.4.peg.3986; -.
DR   HOGENOM; CLU_018247_0_1_6; -.
DR   OrthoDB; 9806325at2; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000014585; Unassembled WGS sequence.
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   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00484; PEPCK_ATP; 1.
DR   Gene3D; 3.90.228.20; -; 1.
DR   Gene3D; 3.40.449.10; Phosphoenolpyruvate Carboxykinase, domain 1; 1.
DR   Gene3D; 2.170.8.10; Phosphoenolpyruvate Carboxykinase, domain 2; 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   NCBIfam; TIGR00224; pckA; 1.
DR   PANTHER; PTHR30031:SF0; PHOSPHOENOLPYRUVATE CARBOXYKINASE (ATP); 1.
DR   PANTHER; PTHR30031; PHOSPHOENOLPYRUVATE CARBOXYKINASE ATP; 1.
DR   Pfam; PF01293; PEPCK_ATP; 1.
DR   PIRSF; PIRSF006294; PEP_crbxkin; 1.
DR   SUPFAM; SSF68923; PEP carboxykinase N-terminal domain; 1.
DR   SUPFAM; SSF53795; PEP carboxykinase-like; 1.
DR   PROSITE; PS00532; PEPCK_ATP; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00453}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00453};
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW   Rule:MF_00453}; Gluconeogenesis {ECO:0000256|HAMAP-Rule:MF_00453};
KW   Kinase {ECO:0000313|EMBL:EPF13165.1};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00453};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_00453};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00453};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00453}; Pyruvate {ECO:0000313|EMBL:EPF13165.1};
KW   Transferase {ECO:0000313|EMBL:EPF13165.1}.
FT   BINDING         64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT   BINDING         206
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT   BINDING         212
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT   BINDING         212
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT   BINDING         212
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT   BINDING         231
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT   BINDING         231
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT   BINDING         247..255
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT   BINDING         268
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT   BINDING         296
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT   BINDING         332
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT   BINDING         332
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT   BINDING         448..449
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT   BINDING         454
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
SQ   SEQUENCE   539 AA;  59427 MW;  2660055C6315D3A9 CRC64;
     MRVKGITPQD LKAYGINDVS EVIHNPDYDT LYREELDPKL EGYERGVVTN LGAVAVDTGI
     FTGRSPKDKY IVRDDTTRDT LWWADNGKGK NDNKPLSEET WHQLKGLVTG QLSGKRLFIL
     DAFCGANADT RLSVRFITEV AWQAHFVKNM FIRPTDEELA TFEPDFVVMN GAKCTNPNWK
     EQGLNSENFV AFNLTERMQL IGGTWYGGEM KKGMFSIMNY LLPLKGIASM HCSANVGEKG
     DVAVFFGLSG TGKTTLSTDP KRRLIGDDEH GWDDDGVFNF EGGCYAKTIR LSEEAEPDIY
     HAIRRDALLE NVTVRADGTI DFDDASKTEN TRVSYPIYHI DNIVKPVSKA GHATKVIFLT
     ADAFGVLPPV SRLTANQTQY HFLSGFTAKL AGTERGVTEP TPTFSACFGA AFLSLHPTQY
     AEVLVKRMQA AGAQAYLVNT GWNGTGKRIS IKDTRAIIDA ILDGSLDDAE TFTLPMFNLA
     IPTSLAGVDS HILDPRNTYG SPEQWQEKAE QLAKLFVENF EKYTDTPAGA ALVAAGPKL
//
DBGET integrated database retrieval system