ID D7BM12_ARCHD Unreviewed; 616 AA.
AC D7BM12;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
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 OrderedLocusNames=Arch_0200 {ECO:0000313|EMBL:ADH91961.1};
OS Arcanobacterium haemolyticum (strain ATCC 9345 / DSM 20595 / CCUG 17215 /
OS LMG 16163 / NBRC 15585 / NCTC 8452 / 11018).
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Arcanobacterium.
OX NCBI_TaxID=644284 {ECO:0000313|EMBL:ADH91961.1, ECO:0000313|Proteomes:UP000000376};
RN [1] {ECO:0000313|EMBL:ADH91961.1, ECO:0000313|Proteomes:UP000000376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9345 / DSM 20595 / CCUG 17215 / LMG 16163 / NBRC 15585 /
RC NCTC 8452 / 11018 {ECO:0000313|Proteomes:UP000000376};
RX PubMed=21304742; DOI=10.4056/sigs.1123072;
RA Yasawong M., Teshima H., Lapidus A., Nolan M., Lucas S.,
RA Glavina Del Rio T., Tice H., Cheng J., Bruce D., Detter C., Tapia R.,
RA Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA Mikhailova N., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y., Jeffries C., Rohde M., Sikorski J., Pukall R., Goker M.,
RA Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P., Kyrpides N.,
RA Klenk H.;
RT "Complete genome sequence of Arcanobacterium haemolyticum type strain
RT (11018).";
RL Stand. Genomic Sci. 3:126-135(2010).
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 phosphoenolpyruvate carboxykinase [GTP]
CC family. {ECO:0000256|ARBA:ARBA00005796, ECO:0000256|HAMAP-
CC Rule:MF_00452}.
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DR EMBL; CP002045; ADH91961.1; -; Genomic_DNA.
DR AlphaFoldDB; D7BM12; -.
DR STRING; 644284.Arch_0200; -.
DR KEGG; ahe:Arch_0200; -.
DR eggNOG; COG1274; Bacteria.
DR HOGENOM; CLU_028872_1_1_11; -.
DR OrthoDB; 9758871at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000000376; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004613; F:phosphoenolpyruvate carboxykinase (GTP) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR CDD; cd00819; PEPCK_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:SF0; PHOSPHOENOLPYRUVATE CARBOXYKINASE (GTP)-RELATED; 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 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};
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}; Reference proteome {ECO:0000313|Proteomes:UP000000376}.
FT DOMAIN 24..247
FT /note="Phosphoenolpyruvate carboxykinase GTP-utilising N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF17297"
FT DOMAIN 251..610
FT /note="Phosphoenolpyruvate carboxykinase C-terminal P-loop"
FT /evidence="ECO:0000259|Pfam:PF00821"
FT ACT_SITE 280
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 84
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 226..228
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 235
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 255
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 278
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 279..284
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 303
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 393..395
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 395
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 426
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 521..524
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
SQ SEQUENCE 616 AA; 68455 MW; 661DD35C7EE3FF4B CRC64;
MTDMYTVEAV REGAPSVAPA DLIEWVTEVA NLTQPKNIEW VDGSQEEWDR LTSMMVESGM
FTRLNPEKRP NSFLARSLPS DVARVESRTF ICSEKEEDAG PTNHWADPKE MKETLLGEKG
VFRGAMRGRT MYVIPFSMGP LGGPISQLGI ELTDSPYVVV NMRIMTRMGI KALELIGEGK
PWVPAVHSVG SPLEEGQEDT SWPCNDEKYI THFPETNEIW SFGSGYGGNA LLGKKCFALR
IASTMARRDT WMAEHMLILR LTNEKTGQQF HVTAAFPSAC GKTNLAMLQP TIEGYKVETV
GDDIAWMRPG ADGRLRAINP EAGFFGVAPG TSYKTNPMAM ETMKANTIFT NVALTDDGDV
WWEGIDGETP EHLIDWHGND WTPESGENAA HPNSRFTTPA SQCPIICPDW EAPEGVAIDA
ILFGGRRATN VPLVAEQYTP AHGVFIGANV SSEVTAAALD VKAGALRHDP FAMLPFCGYN
MADYWGHWLD MQEELGEKFP KVYQVNWFRK DANGKFLWPG YGDNARVLDW IVRRVAGEVE
AIEGMTGLYP HREDFNLEGA GVSEEDWNAM YTLDPEAWEA ETVDTEEYFA KFGDKVPEAL
VEELKALRER IAAAKN
//
