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Database: UniProt
Entry: A0A1I0YC59_9FLAO
LinkDB: A0A1I0YC59_9FLAO
Original site: A0A1I0YC59_9FLAO 
ID   A0A1I0YC59_9FLAO        Unreviewed;       541 AA.
AC   A0A1I0YC59;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
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=SAMN05660845_1624 {ECO:0000313|EMBL:SFB10377.1};
OS   Flavobacterium swingsii.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=498292 {ECO:0000313|EMBL:SFB10377.1, ECO:0000313|Proteomes:UP000199604};
RN   [1] {ECO:0000313|EMBL:SFB10377.1, ECO:0000313|Proteomes:UP000199604}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21789 {ECO:0000313|EMBL:SFB10377.1,
RC   ECO:0000313|Proteomes:UP000199604};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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   -!- 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}.
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DR   EMBL; FOJT01000004; SFB10377.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0YC59; -.
DR   STRING; 498292.SAMN05660845_1624; -.
DR   OrthoDB; 9806325at2; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000199604; 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|HAMAP-Rule:MF_00453};
KW   Gluconeogenesis {ECO:0000256|HAMAP-Rule:MF_00453};
KW   Kinase {ECO:0000313|EMBL:SFB10377.1};
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:SFB10377.1};
KW   Transferase {ECO:0000313|EMBL:SFB10377.1}.
FT   BINDING         66
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT   BINDING         208
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT   BINDING         214
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT   BINDING         214
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT   BINDING         214
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT   BINDING         233
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT   BINDING         233
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT   BINDING         249..257
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT   BINDING         270
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT   BINDING         298
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT   BINDING         334
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT   BINDING         334
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT   BINDING         450..451
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT   BINDING         456
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
SQ   SEQUENCE   541 AA;  60153 MW;  7F48552136F3DB90 CRC64;
     METYKQSTKS ISLEKYGITN ASEIIHNPSF EFLYQEELNP ALEGYERGQL TELGAVNVMT
     GEFTGRSPKD KYIVKDAVTE NTIWWTSDKA VNDNKAISQD TWNALKETTV KQLSGKRLFV
     VDTFCGANEN SRLKVRFIVE VAWQAHFVKN MFIRPTDAEM ETYGEPDFVV MNGSKTEFKD
     FAAHGLNSEV YVAFNLTEKI QLIGGTWYGG EMKKGLFSMM NYYLPLQGMA SMHCSANKGK
     DGDVAVFFGL SGTGKTTLST DPKRELIGDD EHGWDNDGVF NFEGGCYAKT IDLSEANEPD
     IYKAIRKNAL LENVTVDANG KIDFKDGSVT QNTRVSYPID HIDNIVRPVS KAGHATKVIF
     LTADAFGVMP PVSKLTPEQT KYYFLSGFTA KLAGTERGVT QPEPTFSACF GKAFLSLHPT
     QYGQELVKKM EEHKATAYMV NTGWNGTGKR ISIKDTRAII DAILDGSIEK AETKIVPIFN
     FAVPTTLPDV NTDILDPRNT YADASEWTTK AEDLAGRFIK NFVQYTDNEE GKNLIKAGPQ
     L
//
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