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Database: UniProt
Entry: F8NU73_SERL9
LinkDB: F8NU73_SERL9
Original site: F8NU73_SERL9 
ID   F8NU73_SERL9            Unreviewed;       563 AA.
AC   F8NU73;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Phosphoenolpyruvate carboxykinase (ATP) {ECO:0000256|ARBA:ARBA00021932};
DE            EC=4.1.1.49 {ECO:0000256|ARBA:ARBA00012363};
GN   ORFNames=SERLADRAFT_355562 {ECO:0000313|EMBL:EGO25147.1};
OS   Serpula lacrymans var. lacrymans (strain S7.9) (Dry rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX   NCBI_TaxID=578457;
RN   [1] {ECO:0000313|EMBL:EGO25147.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S7.9 {ECO:0000313|EMBL:EGO25147.1};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA   Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA   Coutinho P.M., Cullen D., Cullen D., Gathman A., Goodell B., Henrissat B.,
RA   Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A., Lavin J.L.,
RA   Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E., Murat C.,
RA   Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A., Salamov A.,
RA   Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A., Xie X.,
RA   Kues U., Hibbett D.S., Hoffmeister D., Hogberg N., Martin F.,
RA   Grigoriev I.V., Watkinson S.C.;
RT   "Evolution of plant cell wall degrading machinery underlies the functional
RT   diversity of forest fungi.";
RL   Submitted (APR-2011) 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}.
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DR   EMBL; GL945433; EGO25147.1; -; Genomic_DNA.
DR   RefSeq; XP_007317269.1; XM_007317207.1.
DR   AlphaFoldDB; F8NU73; -.
DR   GeneID; 18809479; -.
DR   KEGG; sla:SERLADRAFT_355562; -.
DR   HOGENOM; CLU_018247_2_0_1; -.
DR   OrthoDB; 3740611at2759; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000008064; Unassembled WGS sequence.
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   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};
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}.
SQ   SEQUENCE   563 AA;  63088 MW;  C9A9DEBE7783F4F6 CRC64;
     MVLPHQTPYV TPHILHRNYA QEYDADAFVV IGRDLEYFSQ AGFDMDKIHL KRNAPVAQLY
     EDAVRNEGAI ISSSGALINF SGKKTGRSPK DKRIVYEETS KDDIWWGSVN IKMDEHTFEI
     NRERAIDYLN TRDNVYVFDG FAGWDPKYRI KVRVICARAY HALFMNNMLI RPTEEELANF
     GEPDFIIYNA GQFPANRFTK GMSSTTSVEI NFKRMEMVIL GTEYAGEMKK GVFSVMHYLQ
     PVKFGQLSLH SSANVGMDKG DVTLFFGLSG TGKTTLSADP HRLLIGDDEH VWSDTGVFNI
     EGGCYAKCIN LSAEKEPEIY NAIRFGSILE NVVYNPATRV PDYDDVGITE NTRCAYPIEY
     IPNAKIPCMV DQQPSNIIML TCDAFGVLPP VSKLTPDQAS YHFLAGYTSK TPGTEDGVLE
     PIPTFSTCYS APFIVLHPGR YAEMLADRMS KHNVNCWLIN TGWTGGKFGT GKRCPLAYTR
     RIVDAVHSGE LLKADFESFD VFGLSIPTGL EGVPREVLNP SLAWADKEAF GREVRKLAGM
     FQKAFRLYEG DVQESVRMAG PKV
//
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