ID A0A8M9PZI9_DANRE Unreviewed; 630 AA. AC A0A8M9PZI9; DT 03-AUG-2022, integrated into UniProtKB/TrEMBL. DT 03-AUG-2022, sequence version 1. DT 27-NOV-2024, entry version 14. DE RecName: Full=Phosphoenolpyruvate carboxykinase, cytosolic [GTP] {ECO:0000256|ARBA:ARBA00040372}; DE EC=4.1.1.32 {ECO:0000256|ARBA:ARBA00012306}; DE AltName: Full=Serine-protein kinase PCK1 {ECO:0000256|ARBA:ARBA00042054}; GN Name=pck1 {ECO:0000313|RefSeq:XP_021332473.1, GN ECO:0000313|ZFIN:ZDB-GENE-030909-11}; GN Synonyms=cb856 {ECO:0000313|RefSeq:XP_021332473.1}, cb924 GN {ECO:0000313|RefSeq:XP_021332473.1}, fj93h11 GN {ECO:0000313|RefSeq:XP_021332473.1}, wu:fc51c05 GN {ECO:0000313|RefSeq:XP_021332473.1}, wu:fj93h11 GN {ECO:0000313|RefSeq:XP_021332473.1}, zgc:63869 GN {ECO:0000313|RefSeq:XP_021332473.1}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Danionidae; Danioninae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|Proteomes:UP000000437, ECO:0000313|RefSeq:XP_021332473.1}; RN [1] {ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23594743; DOI=10.1038/nature12111; RG Genome Reference Consortium Zebrafish; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J., RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D., RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B., RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J., RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D., RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B., RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P., RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., RA Rogers J., Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the human RT genome."; RL Nature 496:498-503(2013). RN [2] {ECO:0000313|RefSeq:XP_021332473.1} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:XP_021332473.1}; RG RefSeq; RL Submitted (AUG-2024) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-seryl-[protein] + GTP = O-phospho-L-seryl-[protein] + GDP + CC H(+); Xref=Rhea:RHEA:64020, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:58189, ChEBI:CHEBI:83421; CC Evidence={ECO:0000256|ARBA:ARBA00036764}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64021; CC Evidence={ECO:0000256|ARBA:ARBA00036764}; CC -!- CATALYTIC ACTIVITY: CC Reaction=oxaloacetate + GTP = phosphoenolpyruvate + GDP + CO2; CC Xref=Rhea:RHEA:10388, ChEBI:CHEBI:16452, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:37565, ChEBI:CHEBI:58189, ChEBI:CHEBI:58702; EC=4.1.1.32; CC Evidence={ECO:0000256|ARBA:ARBA00035922}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10389; CC Evidence={ECO:0000256|ARBA:ARBA00035922}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10390; CC Evidence={ECO:0000256|ARBA:ARBA00035922}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|ARBA:ARBA00001936}; CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC {ECO:0000256|ARBA:ARBA00004742}. CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. CC -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase [GTP] CC family. {ECO:0000256|ARBA:ARBA00005796}. 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 RefSeq; XP_021332473.1; XM_021476798.1. DR SMR; A0A8M9PZI9; -. DR Ensembl; ENSDART00000008752; ENSDARP00000018261; ENSDARG00000013522. DR AGR; ZFIN:ZDB-GENE-030909-11; -. DR ZFIN; ZDB-GENE-030909-11; pck1. DR OMA; GPTNNWV; -. DR UniPathway; UPA00138; -. DR Proteomes; UP000000437; Chromosome 6. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0030145; F:manganese ion binding; IBA:GO_Central. DR GO; GO:0004613; F:phosphoenolpyruvate carboxykinase (GTP) activity; IBA:GO_Central. DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IBA:GO_Central. DR GO; GO:0071333; P:cellular response to glucose stimulus; IBA:GO_Central. DR GO; GO:0032869; P:cellular response to insulin stimulus; IBA:GO_Central. DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central. DR GO; GO:0046327; P:glycerol biosynthetic process from pyruvate; IBA:GO_Central. DR GO; GO:0070365; P:hepatocyte differentiation; IBA:GO_Central. DR GO; GO:0050801; P:monoatomic ion homeostasis; IMP:ZFIN. DR GO; GO:0006107; P:oxaloacetate metabolic process; IBA:GO_Central. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0019543; P:propionate catabolic process; IBA:GO_Central. DR GO; GO:0009749; P:response to glucose; IDA:ZFIN. DR GO; GO:0042594; P:response to starvation; IBA:GO_Central. DR CDD; cd00819; PEPCK_GTP; 1. DR FunFam; 3.90.228.20:FF:000005; Phosphoenolpyruvate carboxykinase [GTP], mitochondrial; 1. DR FunFam; 2.170.8.10:FF:000006; Phosphoenolpyruvate carboxykinase, cytosolic [GTP]; 1. DR FunFam; 3.40.449.10:FF:000003; Phosphoenolpyruvate carboxykinase, cytosolic [GTP]; 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_00452; PEPCK_GTP; 1. DR InterPro; IPR018091; PEP_carboxykin_GTP_CS. DR InterPro; IPR013035; PEP_carboxykinase_C. DR InterPro; IPR008209; PEP_carboxykinase_GTP. DR InterPro; IPR035077; PEP_carboxykinase_GTP_C. DR InterPro; IPR035078; PEP_carboxykinase_GTP_N. DR InterPro; IPR008210; PEP_carboxykinase_N. DR PANTHER; PTHR11561; PHOSPHOENOLPYRUVATE CARBOXYKINASE; 1. DR PANTHER; PTHR11561:SF19; PHOSPHOENOLPYRUVATE CARBOXYKINASE, CYTOSOLIC [GTP]; 1. DR Pfam; PF00821; PEPCK_GTP; 1. DR Pfam; PF17297; PEPCK_N; 1. DR PIRSF; PIRSF001348; PEP_carboxykinase_GTP; 1. DR SUPFAM; SSF68923; PEP carboxykinase N-terminal domain; 1. DR SUPFAM; SSF53795; PEP carboxykinase-like; 1. DR PROSITE; PS00505; PEPCK_GTP; 1. PE 3: Inferred from homology; KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793}; KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432}; KW GTP-binding {ECO:0000256|ARBA:ARBA00023134}; KW Kinase {ECO:0000256|ARBA:ARBA00022777}; KW Lyase {ECO:0000256|ARBA:ARBA00023239}; KW Manganese {ECO:0000256|ARBA:ARBA00023211}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 29..257 FT /note="Phosphoenolpyruvate carboxykinase GTP-utilising N- FT terminal" FT /evidence="ECO:0000259|Pfam:PF17297" FT DOMAIN 261..619 FT /note="Phosphoenolpyruvate carboxykinase C-terminal P-loop" FT /evidence="ECO:0000259|Pfam:PF00821" SQ SEQUENCE 630 AA; 69721 MW; 88E31B9C3012D8AA CRC64; MPPQLQSQDR SCPRVLQGDL ASLSASVREF IDSSVSLCQP DALHICDGSE QENSTILSLL EEQGAIKRLR KYSNCWLART DPRDVARVES KTVIVTAEQR DTVPTPTGGG VSQLGRWMCP EEWDKAMNLR FPGCMKGRVM YVIPFSMGPV GSPLSKIGVE LTDSPYVVAS MRIMTRMGKT VLSALGNGEF VRCLHSVGCP LPLRKPLVNN WPCNPELTLV AHIPDQRKIV SFGSGYGGNS LLGKKCFALR IASRIAKEEG WLAEHMLILG ITNPAGQKKY FAAAFPSACG KTNLAMLKPS LPGWKVECVG DDIAWMKFDK EGNLRAINPE NGFFGVAPGT SSKTNPNAMS TISCNTLFTN VAESSDGGVF WEGMDEDLPE GVTLTSWKNQ PWTPEDGEPC AHPNSRFCTP AAQCPIIDPQ WESPEGVPIE AIIFGGRRPQ GVPLVYEAFD WAHGVFVGAS MRSEATAAAE HKGKVIMHDP FAMRPFFGYN FGQYLSHWLS MEQRPGAKLP KIFHVNWFGR SSSGRFLWPG FGENIRVLEW MFGRLSGGAE ARTTAVGLVP ADGALNLHGL PDVEPLELFR VSQEFWMQEL QEIREYFSRE LNRDLPQEMQ RQLELLEHRL THTHVSSKHG //