ID A0A060JL07_9MICO Unreviewed; 1066 AA.
AC A0A060JL07;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Phosphoenolpyruvate carboxykinase [GTP] {ECO:0000256|HAMAP-Rule:MF_00452};
DE Short=PEP carboxykinase {ECO:0000256|HAMAP-Rule:MF_00452};
DE Short=PEPCK {ECO:0000256|HAMAP-Rule:MF_00452};
DE EC=4.1.1.32 {ECO:0000256|HAMAP-Rule:MF_00452};
DE AltName: Full=GTP-dependent phosphoenolpyruvate carboxykinase {ECO:0000256|HAMAP-Rule:MF_00452};
DE Short=GTP-PEPCK {ECO:0000256|HAMAP-Rule:MF_00452};
GN Name=pckG {ECO:0000256|HAMAP-Rule:MF_00452};
GN ORFNames=Rhola_00001340 {ECO:0000313|EMBL:AIC46964.1};
OS Rhodoluna lacicola.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Luna cluster; Luna-1 subcluster; Rhodoluna.
OX NCBI_TaxID=529884 {ECO:0000313|EMBL:AIC46964.1, ECO:0000313|Proteomes:UP000067708};
RN [1] {ECO:0000313|EMBL:AIC46964.1, ECO:0000313|Proteomes:UP000067708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MWH-Ta8 {ECO:0000313|EMBL:AIC46964.1,
RC ECO:0000313|Proteomes:UP000067708};
RX PubMed=24984700; DOI=10.1099/ijs.0.065292-0;
RA Hahn M., Schmidt J., Taipale S.J., Doolittle W.F., Koll U.;
RT "Rhodoluna lacicola gen. nov., sp. nov., a planktonic freshwater bacterium
RT with stream-lined genome.";
RL Int. J. Syst. Evol. Microbiol. 64:3254-3263(2014).
CC -!- FUNCTION: Catalyzes the conversion of oxaloacetate (OAA) to
CC phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic
CC pathway that produces glucose from lactate and other precursors derived
CC from the citric acid cycle. {ECO:0000256|HAMAP-Rule:MF_00452}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + oxaloacetate = CO2 + GDP + phosphoenolpyruvate;
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|HAMAP-Rule:MF_00452};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00452};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00452};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000256|HAMAP-Rule:MF_00452}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00452}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00452}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000256|RuleBase:RU000397}.
CC -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase [GTP]
CC family. {ECO:0000256|ARBA:ARBA00005796, ECO:0000256|HAMAP-
CC Rule:MF_00452}.
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DR EMBL; CP007490; AIC46964.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060JL07; -.
DR STRING; 529884.Rhola_00001340; -.
DR KEGG; rla:Rhola_00001340; -.
DR PATRIC; fig|529884.3.peg.126; -.
DR eggNOG; COG0057; Bacteria.
DR eggNOG; COG1274; Bacteria.
DR HOGENOM; CLU_288336_0_0_11; -.
DR OrthoDB; 9758871at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000067708; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0004613; F:phosphoenolpyruvate carboxykinase (GTP) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00819; PEPCK_GTP; 1.
DR Gene3D; 3.90.228.20; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; IPR020831; GlycerAld/Erythrose_P_DH.
DR InterPro; IPR020830; GlycerAld_3-P_DH_AS.
DR InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
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:SF0; PHOSPHOENOLPYRUVATE CARBOXYKINASE (GTP)-RELATED; 1.
DR Pfam; PF02800; Gp_dh_C; 1.
DR Pfam; PF00044; Gp_dh_N; 1.
DR Pfam; PF00821; PEPCK_GTP; 1.
DR Pfam; PF17297; PEPCK_N; 1.
DR PRINTS; PR00078; G3PDHDRGNASE.
DR SMART; SM00846; Gp_dh_N; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF68923; PEP carboxykinase N-terminal domain; 1.
DR SUPFAM; SSF53795; PEP carboxykinase-like; 1.
DR PROSITE; PS00071; GAPDH; 1.
DR PROSITE; PS00505; PEPCK_GTP; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00452};
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW Rule:MF_00452};
KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432, ECO:0000256|HAMAP-
KW Rule:MF_00452};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00452}; Kinase {ECO:0000313|EMBL:AIC46964.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00452};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_00452};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00452};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00452}; Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyruvate {ECO:0000313|EMBL:AIC46964.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000067708};
KW Transferase {ECO:0000313|EMBL:AIC46964.1}.
FT DOMAIN 716..877
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT REGION 361..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 266
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 213..215
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 222
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 242
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 264
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 265..270
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 289
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 379..381
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 381
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 412
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 506..509
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
SQ SEQUENCE 1066 AA; 117213 MW; 38B6C336B12666D7 CRC64;
MGNHPLKSTL PQEIGLEKWV NQVAELTQPD QIVWCDGSAA EYQALSQKLV DRGTFIPLNP
AKRPESFLAR TDPADVARVE ERTFICSAQQ IDAGPTNNWM APDEMKDLLL PLFAGAMRGR
TMYVIPFSMG PVNSPLARFG VQITDSEYVV VNMHLMTRVD VAVFEQIRSG ANWVATMHSV
GAPNDNSVWP SNPEKYISHF PDTLEVWSFG SGYGGNALLG KKCMSLRIGS VLARREGWLA
EHMLIMRMIS PEGKKFHFSA AFPSACGKTN LAMLQPSIPG WKVETLGDDI AWIAQAPSGK
LRAINPENGF FGVAPGTSVK TNPVAMELVA KQTIFTNVAL TADGDVWWEG MSKEVPDGLT
NWRGEPHDKN SGKPAAHPNG RFTSPARNCP TISSDWDDPE GVELDAIIFG GRRAKDVPLV
TEASSWQHGV FLGATMASEQ TAAAEGPVGE VRRDPFAMLP FTGYNMADYW RHWLSFAERE
GVQLPKIFRV NWFLKNDEGQ FVWPGFSENA RVLRWIAERL DGKVEANETA IGNLPNLADL
GVDELGLDDA SKQQLLAWNK DAVVKDLESI QRYLGAFGER TPAELKIEAE SRLASLSPMW
EQSLTAAEAM VPLIGRLYRS NGVLLSVHGR TLINRTPIQL IKAMKYARHI DGEPLDIHHA
LSLIKLLDRM GLGPASIDVA RMLAKQKSSG QQLNEFVREE LRELAQMVSI ITESERDVVL
YGFGRIGRLV ARILIAQDGD RRGLKLRAIV VRKGAEDDLT KRAGLLRRDS VHGMFEGTIS
INEERNSIIA NGNEIRVIYS NDPATVDYES YGINDALLID NTGIWRDEAG LSQHLKSKGI
SKVLLTAPGQ GNLPNVVYGV NHSEITANSK IITAASCTTN AIVPVLKVLN DAFGVNHGHV
ETVHSFTNDQ NLIDNYHKGD RRGRSAVLNM VITETGAAKA VAKALPVLAG KLTGNAIRVP
TPDVSMAILN LDFARDVSRE ELNKVLMKAA QSPETRNQVD YVESPEVVST DFVGSNRAGI
VDGLATVGEG NHGVVYVWYD NENGYSHQVA RIAEKMMLQE RPSYPR
//
