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Database: UniProt
Entry: A0A060SPY3_PYCCI
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ID   A0A060SPY3_PYCCI        Unreviewed;       667 AA.
AC   A0A060SPY3;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Phosphoenolpyruvate carboxykinase (ATP) {ECO:0000256|ARBA:ARBA00021932};
DE            EC=4.1.1.49 {ECO:0000256|ARBA:ARBA00012363};
GN   ORFNames=BN946_scf184643.g4 {ECO:0000313|EMBL:CDO74264.1};
OS   Pycnoporus cinnabarinus (Cinnabar-red polypore) (Trametes cinnabarina).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Polyporaceae; Trametes.
OX   NCBI_TaxID=5643 {ECO:0000313|EMBL:CDO74264.1, ECO:0000313|Proteomes:UP000029665};
RN   [1] {ECO:0000313|EMBL:CDO74264.1, ECO:0000313|Proteomes:UP000029665}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRFM137 {ECO:0000313|EMBL:CDO74264.1,
RC   ECO:0000313|Proteomes:UP000029665};
RA   Levasseur A., Lomascolo A., Ruiz-Duenas F.J., Uzan E., Piumi F., Kues U.,
RA   Ram A.F.J., Murat C., Haon M., Benoit I., Arfi Y., Chevret D., Drula E.,
RA   Kwon M.J., Gouret P., Lesage-Meessen L., Lombard V., Mariette J.,
RA   Noirot C., Park J., Patyshakuliyeva A., Wieneger R.A.B., Wosten H.A.B.,
RA   Martin F., Coutinho P.M., de Vries R., Martinez A.T., Klopp C.,
RA   Pontarotti P., Henrissat B., Record E.;
RT   "The genome of the white-rot fungus Pycnoporus cinnabarinus: a
RT   basidiomycete model with a versatile arsenal for lignocellulosic biomass
RT   breakdown.";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
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   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000256|ARBA:ARBA00004742}.
CC   -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase (ATP)
CC       family. {ECO:0000256|ARBA:ARBA00006052}.
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:CDO74264.1}.
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DR   EMBL; CCBP010000142; CDO74264.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A060SPY3; -.
DR   STRING; 5643.A0A060SPY3; -.
DR   HOGENOM; CLU_018247_2_0_1; -.
DR   OMA; MRYAGEM; -.
DR   OrthoDB; 3740611at2759; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000029665; Unassembled WGS sequence.
DR   GO; GO:0042729; C:DASH complex; IEA:InterPro.
DR   GO; GO:0072686; C:mitotic spindle; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004612; F:phosphoenolpyruvate carboxykinase (ATP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR   GO; GO:0000278; P:mitotic cell cycle; IEA:InterPro.
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; IPR013963; DASH_Dad2.
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; PF08654; DASH_Dad2; 1.
DR   Pfam; PF01293; PEPCK_ATP; 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};
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW   Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029665}.
FT   REGION          635..667
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        653..667
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   667 AA;  74749 MW;  2D5A89640217D86B CRC64;
     MVYTHGTPYV TPHILHKHYA QAFDAEQSGL IGKDLEYFSQ AGFDMDRIQI KRNAPPAVLY
     EDAIRNEGAV ISSSGALINF SGKKTGRSPK DKRIVYEETS KDEIWWGSVN IKMDEHTFEI
     NRERAIDYLN TRDNVYVFDG YAGWDPKYRI KVRVICARAY HALFMNNMLI RPTEEELANF
     GDPEFIIYNA GQFPANRFTK GMSSTTSVEI NFKRMEMVIL GTEYAGEMKK GIFSVMHYLQ
     PVKFGQLSLH SSANVGEAGD VTLFFGLSGT GKTTLSADAR RKLIGDDEHV WSDDGVFNIE
     GGCYAKCINL SAEKEPEIFS AIRFGAVLEN VVYNPLTRVP DYDDASITEN TRCAYPIEFI
     PNAQIPCHVK SQPKNIIMLT CDAFGVLPPV SKLTPEQASY HFLAGYTSKT PGTEDGVLEP
     IPTFSTCYSA PFIVLHPGRY AEMLAERMSK NNVDCWLINT GWTGGKFGSG KRCPLKYTRR
     IVDAVHSGEL AKAEYETFGV FNLQIPTSLE GVPRELLNPR LAWSNTEAFE REVRKLAGMF
     QKAFALYEND VDEKSQAPGA IASAAATAKL LEKKKEYEAV AALERASAQF LRRIEGLEDD
     FDVIADAGIV HGQVLEQWPN MFRILNLFLS QRQQHQDEDE SAPTPATGER LVRVPIEELR
     QAESKQS
//
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