ID M4S061_9SPHN Unreviewed; 532 AA.
AC M4S061;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Phosphoenolpyruvate carboxykinase (ATP) {ECO:0000256|ARBA:ARBA00012363, ECO:0000256|HAMAP-Rule:MF_00453};
DE Short=PCK {ECO:0000256|HAMAP-Rule:MF_00453};
DE Short=PEP carboxykinase {ECO:0000256|HAMAP-Rule:MF_00453};
DE Short=PEPCK {ECO:0000256|HAMAP-Rule:MF_00453};
DE EC=4.1.1.49 {ECO:0000256|ARBA:ARBA00012363, ECO:0000256|HAMAP-Rule:MF_00453};
GN Name=pckA {ECO:0000256|HAMAP-Rule:MF_00453};
GN ORFNames=G432_02930 {ECO:0000313|EMBL:AGH48313.1};
OS Sphingomonas sp. MM-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=745310 {ECO:0000313|EMBL:AGH48313.1, ECO:0000313|Proteomes:UP000011816};
RN [1] {ECO:0000313|EMBL:AGH48313.1, ECO:0000313|Proteomes:UP000011816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MM-1 {ECO:0000313|EMBL:AGH48313.1};
RX PubMed=23682148;
RA Tabata M., Ohtsubo Y., Ohhata S., Tsuda M., Nagata Y.;
RT "Complete Genome Sequence of the gamma-Hexachlorocyclohexane-Degrading
RT Bacterium Sphingomonas sp. Strain MM-1.";
RL Genome Announc. 1:E00247-13(2013).
CC -!- FUNCTION: Involved in the gluconeogenesis. Catalyzes the conversion of
CC oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct
CC phosphoryl transfer between the nucleoside triphosphate and OAA.
CC {ECO:0000256|HAMAP-Rule:MF_00453}.
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:0000256|ARBA:ARBA00001389,
CC ECO:0000256|HAMAP-Rule:MF_00453};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00453};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00453};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000256|ARBA:ARBA00004742, ECO:0000256|HAMAP-Rule:MF_00453}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00453}.
CC -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase (ATP)
CC family. {ECO:0000256|ARBA:ARBA00006052, ECO:0000256|HAMAP-
CC Rule:MF_00453}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00453}.
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DR EMBL; CP004036; AGH48313.1; -; Genomic_DNA.
DR RefSeq; WP_015457329.1; NC_020561.1.
DR AlphaFoldDB; M4S061; -.
DR STRING; 745310.G432_02930; -.
DR KEGG; sphm:G432_02930; -.
DR PATRIC; fig|745310.14.peg.600; -.
DR eggNOG; COG1866; Bacteria.
DR HOGENOM; CLU_018247_0_1_5; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000011816; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00484; PEPCK_ATP; 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_00453; PEPCK_ATP; 1.
DR InterPro; IPR001272; PEP_carboxykinase_ATP.
DR InterPro; IPR013035; PEP_carboxykinase_C.
DR InterPro; IPR008210; PEP_carboxykinase_N.
DR NCBIfam; TIGR00224; pckA; 1.
DR PANTHER; PTHR30031:SF0; PHOSPHOENOLPYRUVATE CARBOXYKINASE (ATP); 1.
DR PANTHER; PTHR30031; PHOSPHOENOLPYRUVATE CARBOXYKINASE ATP; 1.
DR Pfam; PF01293; PEPCK_ATP; 1.
DR PIRSF; PIRSF006294; PEP_crbxkin; 1.
DR SUPFAM; SSF68923; PEP carboxykinase N-terminal domain; 1.
DR SUPFAM; SSF53795; PEP carboxykinase-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00453}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00453};
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW Rule:MF_00453};
KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432, ECO:0000256|HAMAP-
KW Rule:MF_00453}; Kinase {ECO:0000313|EMBL:AGH48313.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00453};
KW Manganese {ECO:0000256|HAMAP-Rule:MF_00453};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00453};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00453}; Pyruvate {ECO:0000313|EMBL:AGH48313.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000011816};
KW Transferase {ECO:0000313|EMBL:AGH48313.1}.
FT BINDING 58
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT BINDING 200
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT BINDING 200
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT BINDING 219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT BINDING 219
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT BINDING 235..243
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT BINDING 256
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT BINDING 284
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT BINDING 322
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT BINDING 322
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT BINDING 447
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
SQ SEQUENCE 532 AA; 57793 MW; 7460B1E5A02BE98C CRC64;
MSSPIPAHDL AAQGIKVDAA LHWNLPTAPL VEEAVRRGEG VLAKDGPLVV KTGKHTGRSA
NDKFIVRDAE TENTVWWGKT NKGMTPEHFA ALKEDFLKHL GTKETLFVQD LYGGSQPEYR
VNVRVINELA WHNLFIKTLL VRPGAEELPG FVPEYTIIDL PSFRADPERH GVRSETVIAV
NLTEKLILIG GTAYAGEMKK SVFGILNYKL PVEGVMPMHC SANIGPKGDT AVFFGLSGTG
KTTLSADASR TLIGDDEHGW SDTAVFNFEG GCYAKMIRLS PEAEPEIYAT TKRFGTVLEN
VVIDMDTREI DLDDDSLAEN SRGSYPIDFI PNASEKNLGP VPKNIIFLTA DAYGVLPPIA
KLTPDQAMYH FLSGYTARVA GTEIGVTEPT ATFSTCFGAP FMPRHPSVYG NLLKERIAKG
GVDCWLVNTG WTGGSYGVGH RMPIKATRAL LNAALDGSLN AATFEIDPNF GFQVPQAVPG
VDSAILNPRE TWADKAAYDA TARKLVDQFI ENFSQFADHV DEGVRQAAPK AA
//
