PCKA_THET8
ID PCKA_THET8 Reviewed; 529 AA.
AC Q5SLL5; P84128; Q7SIC6;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Phosphoenolpyruvate carboxykinase (ATP) {ECO:0000255|HAMAP-Rule:MF_00453};
DE Short=PCK {ECO:0000255|HAMAP-Rule:MF_00453};
DE Short=PEP carboxykinase {ECO:0000255|HAMAP-Rule:MF_00453};
DE Short=PEPCK {ECO:0000255|HAMAP-Rule:MF_00453};
DE EC=4.1.1.49 {ECO:0000255|HAMAP-Rule:MF_00453};
GN Name=pckA {ECO:0000255|HAMAP-Rule:MF_00453}; Synonyms=tthHB8IM;
GN OrderedLocusNames=TTHA0278;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ATP AND CALCIUM ION,
RP FUNCTION, AND SUBUNIT.
RX PubMed=16239727; DOI=10.1107/s090744490502651x;
RA Sugahara M., Ohshima N., Ukita Y., Sugahara M., Kunishima N.;
RT "Structure of ATP-dependent phosphoenolpyruvate carboxykinase from Thermus
RT thermophilus HB8 showing the structural basis of induced fit and
RT thermostability.";
RL Acta Crystallogr. D 61:1500-1507(2005).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH ATP AND CALCIUM ION,
RP AND SUBUNIT.
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of ATP-dependent phosphoenolpyruvate carboxykinase from
RT Thermus thermophilus HB8.";
RL Submitted (OCT-2007) to the PDB data bank.
CC -!- FUNCTION: Involved in gluconeogenesis. Catalyzes the conversion of
CC oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct
CC phosphoryl transfer between the nucleoside triphosphate and OAA (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:16239727}.
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:0000255|HAMAP-Rule:MF_00453};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00453};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00453};
CC -!- ACTIVITY REGULATION: Allosterically activated by calcium.
CC {ECO:0000250}.
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000255|HAMAP-Rule:MF_00453}.
CC -!- SUBUNIT: Dimer of dimers. {ECO:0000305|PubMed:16239727,
CC ECO:0000305|Ref.3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00453}.
CC -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase (ATP)
CC family. {ECO:0000255|HAMAP-Rule:MF_00453}.
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DR EMBL; AP008226; BAD70101.1; -; Genomic_DNA.
DR RefSeq; WP_011227826.1; NC_006461.1.
DR RefSeq; YP_143544.1; NC_006461.1.
DR PDB; 1J3B; X-ray; 2.00 A; A/B=1-529.
DR PDB; 1XKV; X-ray; 2.20 A; A/B=1-529.
DR PDB; 2PC9; X-ray; 2.40 A; A/B/C/D=1-529.
DR PDBsum; 1J3B; -.
DR PDBsum; 1XKV; -.
DR PDBsum; 2PC9; -.
DR AlphaFoldDB; Q5SLL5; -.
DR SMR; Q5SLL5; -.
DR STRING; 300852.55771660; -.
DR EnsemblBacteria; BAD70101; BAD70101; BAD70101.
DR GeneID; 3168667; -.
DR KEGG; ttj:TTHA0278; -.
DR PATRIC; fig|300852.9.peg.278; -.
DR eggNOG; COG1866; Bacteria.
DR HOGENOM; CLU_018247_0_1_0; -.
DR OMA; MRYAGEM; -.
DR PhylomeDB; Q5SLL5; -.
DR BRENDA; 4.1.1.49; 2305.
DR UniPathway; UPA00138; -.
DR EvolutionaryTrace; Q5SLL5; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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 CDD; cd00484; PEPCK_ATP; 1.
DR Gene3D; 3.40.449.10; -; 1.
DR Gene3D; 3.90.228.20; -; 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 PANTHER; PTHR30031; PTHR30031; 1.
DR Pfam; PF01293; PEPCK_ATP; 1.
DR PIRSF; PIRSF006294; PEP_crbxkin; 1.
DR SUPFAM; SSF68923; SSF68923; 1.
DR TIGRFAMs; TIGR00224; pckA; 1.
DR PROSITE; PS00532; PEPCK_ATP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Calcium; Cytoplasm; Decarboxylase;
KW Gluconeogenesis; Lyase; Manganese; Metal-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..529
FT /note="Phosphoenolpyruvate carboxykinase (ATP)"
FT /id="PRO_0000236952"
FT BINDING 52
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 130
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:16239727, ECO:0000269|Ref.3,
FT ECO:0007744|PDB:1J3B, ECO:0007744|PDB:1XKV,
FT ECO:0007744|PDB:2PC9"
FT BINDING 131
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:16239727, ECO:0000269|Ref.3,
FT ECO:0007744|PDB:1J3B, ECO:0007744|PDB:1XKV,
FT ECO:0007744|PDB:2PC9"
FT BINDING 133
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:16239727, ECO:0000269|Ref.3,
FT ECO:0007744|PDB:1J3B, ECO:0007744|PDB:2PC9"
FT BINDING 191
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 197
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453,
FT ECO:0007744|PDB:2PC9"
FT BINDING 197
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453,
FT ECO:0007744|PDB:2PC9"
FT BINDING 216
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 216
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P22259"
FT BINDING 232..240
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453,
FT ECO:0000269|PubMed:16239727, ECO:0000269|Ref.3,
FT ECO:0007744|PDB:1XKV, ECO:0007744|PDB:2PC9"
FT BINDING 253
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 267
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:16239727, ECO:0000269|Ref.3,
FT ECO:0007744|PDB:1J3B, ECO:0007744|PDB:1XKV,
FT ECO:0007744|PDB:2PC9"
FT BINDING 281
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 319
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453,
FT ECO:0000269|Ref.3, ECO:0007744|PDB:2PC9"
FT BINDING 319
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 438..439
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:16239727, ECO:0000305|Ref.3,
FT ECO:0007744|PDB:1XKV, ECO:0007744|PDB:2PC9"
FT BINDING 439
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453,
FT ECO:0000269|PubMed:16239727, ECO:0000269|Ref.3"
FT BINDING 444
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453,
FT ECO:0000269|PubMed:16239727, ECO:0000269|Ref.3,
FT ECO:0007744|PDB:1XKV, ECO:0007744|PDB:2PC9"
FT HELIX 5..7
FT /evidence="ECO:0007829|PDB:1J3B"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:1J3B"
FT HELIX 21..30
FT /evidence="ECO:0007829|PDB:1J3B"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:1J3B"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:1J3B"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:1J3B"
FT TURN 63..68
FT /evidence="ECO:0007829|PDB:1J3B"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:1J3B"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:1J3B"
FT HELIX 80..95
FT /evidence="ECO:0007829|PDB:1J3B"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:1J3B"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:1J3B"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:1J3B"
FT HELIX 123..132
FT /evidence="ECO:0007829|PDB:1J3B"
FT HELIX 136..139
FT /evidence="ECO:0007829|PDB:1J3B"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:1J3B"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:1J3B"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:1J3B"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:1J3B"
FT TURN 179..182
FT /evidence="ECO:0007829|PDB:1J3B"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:1J3B"
FT HELIX 193..206
FT /evidence="ECO:0007829|PDB:1J3B"
FT HELIX 207..210
FT /evidence="ECO:0007829|PDB:1J3B"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:1J3B"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:1J3B"
FT STRAND 227..232
FT /evidence="ECO:0007829|PDB:1J3B"
FT HELIX 238..241
FT /evidence="ECO:0007829|PDB:1J3B"
FT STRAND 249..257
FT /evidence="ECO:0007829|PDB:1J3B"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:1J3B"
FT STRAND 267..272
FT /evidence="ECO:0007829|PDB:1J3B"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:1J3B"
FT HELIX 282..288
FT /evidence="ECO:0007829|PDB:1J3B"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:1J3B"
FT TURN 302..304
FT /evidence="ECO:0007829|PDB:1J3B"
FT STRAND 319..323
FT /evidence="ECO:0007829|PDB:1J3B"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:1J3B"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:1J3B"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:1J3B"
FT STRAND 339..346
FT /evidence="ECO:0007829|PDB:1J3B"
FT STRAND 355..359
FT /evidence="ECO:0007829|PDB:1J3B"
FT HELIX 361..370
FT /evidence="ECO:0007829|PDB:1J3B"
FT STRAND 372..375
FT /evidence="ECO:0007829|PDB:1J3B"
FT STRAND 387..390
FT /evidence="ECO:0007829|PDB:1J3B"
FT HELIX 392..394
FT /evidence="ECO:0007829|PDB:1J3B"
FT HELIX 396..398
FT /evidence="ECO:0007829|PDB:1J3B"
FT HELIX 403..417
FT /evidence="ECO:0007829|PDB:1J3B"
FT STRAND 420..425
FT /evidence="ECO:0007829|PDB:1J3B"
FT STRAND 427..432
FT /evidence="ECO:0007829|PDB:1J3B"
FT TURN 433..435
FT /evidence="ECO:0007829|PDB:1J3B"
FT STRAND 436..438
FT /evidence="ECO:0007829|PDB:1J3B"
FT HELIX 441..452
FT /evidence="ECO:0007829|PDB:1J3B"
FT HELIX 455..458
FT /evidence="ECO:0007829|PDB:1J3B"
FT STRAND 461..463
FT /evidence="ECO:0007829|PDB:1J3B"
FT TURN 465..467
FT /evidence="ECO:0007829|PDB:1J3B"
FT STRAND 470..473
FT /evidence="ECO:0007829|PDB:1J3B"
FT HELIX 480..483
FT /evidence="ECO:0007829|PDB:1J3B"
FT HELIX 485..488
FT /evidence="ECO:0007829|PDB:1J3B"
FT HELIX 492..514
FT /evidence="ECO:0007829|PDB:1J3B"
FT HELIX 519..523
FT /evidence="ECO:0007829|PDB:1J3B"
SQ SEQUENCE 529 AA; 59314 MW; 62FC60C17D719D70 CRC64;
MQRLEALGIH PKKRVFWNTV SPVLVEHTLL RGEGLLAHHG PLVVDTTPYT GRSPKDKFVV
REPEVEGEIW WGEVNQPFAP EAFEALYQRV VQYLSERDLY VQDLYAGADR RYRLAVRVVT
ESPWHALFAR NMFILPRRFG NDDEVEAFVP GFTVVHAPYF QAVPERDGTR SEVFVGISFQ
RRLVLIVGTK YAGEIKKSIF TVMNYLMPKR GVFPMHASAN VGKEGDVAVF FGLSGTGKTT
LSTDPERPLI GDDEHGWSED GVFNFEGGCY AKVIRLSPEH EPLIYKASNQ FEAILENVVV
NPESRRVQWD DDSKTENTRS SYPIAHLENV VESGVAGHPR AIFFLSADAY GVLPPIARLS
PEEAMYYFLS GYTARVAGTE RGVTEPRATF SACFGAPFLP MHPGVYARML GEKIRKHAPR
VYLVNTGWTG GPYGVGYRFP LPVTRALLKA ALSGALENVP YRRDPVFGFE VPLEAPGVPQ
ELLNPRETWA DKEAYDQQAR KLARLFQENF QKYASGVAKE VAEAGPRTE
