ID A0A0F5AQM7_9GAMM Unreviewed; 542 AA.
AC A0A0F5AQM7;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=WN56_07445 {ECO:0000313|EMBL:KKA44967.1};
OS Salinivibrio sp. KP-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Salinivibrio.
OX NCBI_TaxID=1406902 {ECO:0000313|EMBL:KKA44967.1, ECO:0000313|Proteomes:UP000033449};
RN [1] {ECO:0000313|EMBL:KKA44967.1, ECO:0000313|Proteomes:UP000033449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KP-1 {ECO:0000313|EMBL:KKA44967.1,
RC ECO:0000313|Proteomes:UP000033449};
RA Kaur G., Kumar A., Mathan Kumar R., Kumar N., Singh N.K., Arora A.,
RA Kaur N., Bala M., Mayilraj S.;
RT "Taxonomic description and genome sequence of Salinivibrio halophilus sp.
RT nov., a novel halotolerant gammaproteobacterium isolated from marine
RT sediment and emended description of the genus Salinivibrio.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBUNIT: Monomer. {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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKA44967.1}.
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DR EMBL; LAQR01000004; KKA44967.1; -; Genomic_DNA.
DR RefSeq; WP_046074439.1; NZ_LAQR01000004.1.
DR AlphaFoldDB; A0A0F5AQM7; -.
DR PATRIC; fig|1406902.3.peg.1525; -.
DR OrthoDB; 9806325at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000033449; Unassembled WGS sequence.
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 InterPro; IPR015994; PEPCK_ATP_CS.
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.
DR PROSITE; PS00532; PEPCK_ATP; 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:KKA44967.1};
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:KKA44967.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033449};
KW Transferase {ECO:0000313|EMBL:KKA44967.1}.
FT BINDING 68
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT BINDING 208
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT BINDING 214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT BINDING 214
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT BINDING 233
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT BINDING 233
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT BINDING 249..257
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT BINDING 270
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT BINDING 298
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT BINDING 334
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT BINDING 334
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT BINDING 450..451
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT BINDING 456
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
SQ SEQUENCE 542 AA; 60196 MW; E34CB036612F3881 CRC64;
MTVLNVEPEV ADIDLSRHGL ENVKEVIRNP SYEQLFEEET KPGLEGYEKG VVTELGAVAV
DTGIFTGRSP KDKYIVRDDT TRDTIWWSDQ GKNDNKPIDQ AVWKDLKALV TDQLSGKRLF
VIDGYCGANP NTRLRIRVIT EVAWQAHFVK NMFIRPTDEE LKDFEPDFVV MNGAKCVNTK
WREQGLNSEN FTVFNLTERM QLIGGTWYGG EMKKGMFAMM NYFLPLQDIA SMHCSANMGK
DGDVAIFFGL SGTGKTTLST DPKRQLIGDD EHGWDDHGVF NFEGGCYAKT IKLSKEAEPD
IYNAIRRDAL LENVTVRGNG TIDFDDNTKT ENTRVSYPIY HIDNIVKPVS KGGHANKVIF
LSADAFGVLP PVSKLTPEQT KYHFLSGFTA KLAGTERGIT EPTPAFSAAF GAAFLTLHPT
KYAEVLVKRM EAAGAEAYLV NTGWNGSGKR ISIKDTRAII DAILDGSIEK AETKSIPIFN
LEVPVSLDEV SDGILDPRDT YVDPLQWESK ANDLAQRFID NFEKYTDTPE GAALVSAGPK
LD
//
