PCKA_ACTSZ
ID PCKA_ACTSZ Reviewed; 538 AA.
AC A6VKV4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
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}; OrderedLocusNames=Asuc_0221;
OS Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / CCUG 43843 /
OS 130Z).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=339671;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55618 / DSM 22257 / CCUG 43843 / 130Z;
RX PubMed=21118570; DOI=10.1186/1471-2164-11-680;
RA McKinlay J.B., Laivenieks M., Schindler B.D., McKinlay A.A.,
RA Siddaramappa S., Challacombe J.F., Lowry S.R., Clum A., Lapidus A.L.,
RA Burkhart K.B., Harkins V., Vieille C.;
RT "A genomic perspective on the potential of Actinobacillus succinogenes for
RT industrial succinate production.";
RL BMC Genomics 11:680-680(2010).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH MANGANESE, SUBSTRATE
RP AND ATP ANALOGS, AND COFACTOR.
RX PubMed=15983413; DOI=10.1107/s0907444905008723;
RA Leduc Y.A., Prasad L., Laivenieks M., Zeikus J.G., Delbaere L.T.;
RT "Structure of PEP carboxykinase from the succinate-producing Actinobacillus
RT succinogenes: a new conserved active-site motif.";
RL Acta Crystallogr. D 61:903-912(2005).
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}.
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 ECO:0000269|PubMed:15983413};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00453,
CC ECO:0000269|PubMed:15983413};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000255|HAMAP-Rule:MF_00453}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00453}.
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; CP000746; ABR73601.1; -; Genomic_DNA.
DR RefSeq; WP_011978877.1; NC_009655.1.
DR PDB; 1YGG; X-ray; 1.85 A; A=1-538.
DR PDB; 1YLH; X-ray; 1.70 A; A=1-538.
DR PDBsum; 1YGG; -.
DR PDBsum; 1YLH; -.
DR AlphaFoldDB; A6VKV4; -.
DR SMR; A6VKV4; -.
DR STRING; 339671.Asuc_0221; -.
DR EnsemblBacteria; ABR73601; ABR73601; Asuc_0221.
DR KEGG; asu:Asuc_0221; -.
DR eggNOG; COG1866; Bacteria.
DR HOGENOM; CLU_018247_0_1_6; -.
DR OMA; MRYAGEM; -.
DR OrthoDB; 146648at2; -.
DR UniPathway; UPA00138; -.
DR EvolutionaryTrace; A6VKV4; -.
DR Proteomes; UP000001114; 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; Cytoplasm; Decarboxylase; Gluconeogenesis;
KW Lyase; Manganese; Metal-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..538
FT /note="Phosphoenolpyruvate carboxykinase (ATP)"
FT /id="PRO_1000072371"
FT BINDING 64
FT /ligand="substrate"
FT BINDING 152
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 205
FT /ligand="substrate"
FT BINDING 211
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 211
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453,
FT ECO:0000269|PubMed:15983413"
FT BINDING 211
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 230
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 230
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453,
FT ECO:0000269|PubMed:15983413"
FT BINDING 246..254
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 267
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453,
FT ECO:0000269|PubMed:15983413"
FT BINDING 295
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 331
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 331
FT /ligand="substrate"
FT BINDING 344
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 447..448
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 453
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT HELIX 4..13
FT /evidence="ECO:0007829|PDB:1YLH"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:1YLH"
FT HELIX 28..36
FT /evidence="ECO:0007829|PDB:1YLH"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:1YLH"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:1YLH"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:1YLH"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:1YLH"
FT TURN 75..80
FT /evidence="ECO:0007829|PDB:1YLH"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:1YLH"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:1YLH"
FT HELIX 97..110
FT /evidence="ECO:0007829|PDB:1YLH"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:1YLH"
FT STRAND 116..123
FT /evidence="ECO:0007829|PDB:1YLH"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:1YLH"
FT STRAND 131..138
FT /evidence="ECO:0007829|PDB:1YLH"
FT HELIX 140..149
FT /evidence="ECO:0007829|PDB:1YLH"
FT HELIX 155..159
FT /evidence="ECO:0007829|PDB:1YLH"
FT STRAND 164..170
FT /evidence="ECO:0007829|PDB:1YLH"
FT TURN 176..182
FT /evidence="ECO:0007829|PDB:1YLH"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:1YLH"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:1YLH"
FT TURN 193..196
FT /evidence="ECO:0007829|PDB:1YLH"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:1YLH"
FT HELIX 207..223
FT /evidence="ECO:0007829|PDB:1YLH"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:1YLH"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:1YLH"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:1YLH"
FT HELIX 252..255
FT /evidence="ECO:0007829|PDB:1YLH"
FT STRAND 261..271
FT /evidence="ECO:0007829|PDB:1YLH"
FT STRAND 276..279
FT /evidence="ECO:0007829|PDB:1YLH"
FT STRAND 281..286
FT /evidence="ECO:0007829|PDB:1YLH"
FT TURN 292..294
FT /evidence="ECO:0007829|PDB:1YLH"
FT HELIX 296..301
FT /evidence="ECO:0007829|PDB:1YLH"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:1YLH"
FT STRAND 331..335
FT /evidence="ECO:0007829|PDB:1YLH"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:1YLH"
FT STRAND 339..342
FT /evidence="ECO:0007829|PDB:1YLH"
FT STRAND 345..348
FT /evidence="ECO:0007829|PDB:1YLH"
FT STRAND 352..359
FT /evidence="ECO:0007829|PDB:1YLH"
FT STRAND 368..371
FT /evidence="ECO:0007829|PDB:1YLH"
FT HELIX 374..383
FT /evidence="ECO:0007829|PDB:1YLH"
FT STRAND 385..388
FT /evidence="ECO:0007829|PDB:1YGG"
FT STRAND 400..403
FT /evidence="ECO:0007829|PDB:1YGG"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:1YLH"
FT HELIX 409..411
FT /evidence="ECO:0007829|PDB:1YLH"
FT HELIX 416..430
FT /evidence="ECO:0007829|PDB:1YLH"
FT STRAND 433..438
FT /evidence="ECO:0007829|PDB:1YLH"
FT STRAND 445..447
FT /evidence="ECO:0007829|PDB:1YLH"
FT HELIX 450..462
FT /evidence="ECO:0007829|PDB:1YLH"
FT HELIX 464..467
FT /evidence="ECO:0007829|PDB:1YLH"
FT STRAND 470..473
FT /evidence="ECO:0007829|PDB:1YLH"
FT TURN 474..477
FT /evidence="ECO:0007829|PDB:1YLH"
FT STRAND 478..482
FT /evidence="ECO:0007829|PDB:1YLH"
FT TURN 489..491
FT /evidence="ECO:0007829|PDB:1YLH"
FT HELIX 494..497
FT /evidence="ECO:0007829|PDB:1YLH"
FT STRAND 498..500
FT /evidence="ECO:0007829|PDB:1YGG"
FT HELIX 501..519
FT /evidence="ECO:0007829|PDB:1YLH"
FT HELIX 520..524
FT /evidence="ECO:0007829|PDB:1YLH"
FT HELIX 526..529
FT /evidence="ECO:0007829|PDB:1YLH"
FT HELIX 530..534
FT /evidence="ECO:0007829|PDB:1YLH"
SQ SEQUENCE 538 AA; 59154 MW; 40205AB2A8D79871 CRC64;
MTDLNKLVKE LNDLGLTDVK EIVYNPSYEQ LFEEETKPGL EGFDKGTLTT LGAVAVDTGI
FTGRSPKDKY IVCDETTKDT VWWNSEAAKN DNKPMTQETW KSLRELVAKQ LSGKRLFVVE
GYCGASEKHR IGVRMVTEVA WQAHFVKNMF IRPTDEELKN FKADFTVLNG AKCTNPNWKE
QGLNSENFVA FNITEGIQLI GGTWYGGEMK KGMFSMMNYF LPLKGVASMH CSANVGKDGD
VAIFFGLSGT GKTTLSTDPK RQLIGDDEHG WDESGVFNFE GGCYAKTINL SQENEPDIYG
AIRRDALLEN VVVRADGSVD FDDGSKTENT RVSYPIYHID NIVRPVSKAG HATKVIFLTA
DAFGVLPPVS KLTPEQTEYY FLSGFTAKLA GTERGVTEPT PTFSACFGAA FLSLHPIQYA
DVLVERMKAS GAEAYLVNTG WNGTGKRISI KDTRGIIDAI LDGSIEKAEM GELPIFNLAI
PKALPGVDPA ILDPRDTYAD KAQWQVKAED LANRFVKNFV KYTANPEAAK LVGAGPKA
