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Database: UniProt
Entry: B7GA98_PHATC
LinkDB: B7GA98_PHATC
Original site: B7GA98_PHATC 
ID   B7GA98_PHATC            Unreviewed;      1264 AA.
AC   B7GA98;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   24-JAN-2024, entry version 78.
DE   RecName: Full=pyruvate carboxylase {ECO:0000256|ARBA:ARBA00013057};
DE            EC=6.4.1.1 {ECO:0000256|ARBA:ARBA00013057};
GN   Name=PYC2 {ECO:0000313|EMBL:EEC44575.1};
GN   ORFNames=PHATRDRAFT_49339 {ECO:0000313|EMBL:EEC44575.1};
OS   Phaeodactylum tricornutum (strain CCAP 1055/1).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC   Bacillariophyceae; Bacillariophycidae; Naviculales; Phaeodactylaceae;
OC   Phaeodactylum.
OX   NCBI_TaxID=556484 {ECO:0000313|EMBL:EEC44575.1, ECO:0000313|Proteomes:UP000000759};
RN   [1] {ECO:0000313|EMBL:EEC44575.1, ECO:0000313|Proteomes:UP000000759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCAP 1055/1 {ECO:0000313|EMBL:EEC44575.1,
RC   ECO:0000313|Proteomes:UP000000759};
RX   PubMed=18923393; DOI=10.1038/nature07410;
RA   Bowler C., Allen A.E., Badger J.H., Grimwood J., Jabbari K., Kuo A.,
RA   Maheswari U., Martens C., Maumus F., Otillar R.P., Rayko E., Salamov A.,
RA   Vandepoele K., Beszteri B., Gruber A., Heijde M., Katinka M., Mock T.,
RA   Valentin K., Verret F., Berges J.A., Brownlee C., Cadoret J.P.,
RA   Chiovitti A., Choi C.J., Coesel S., De Martino A., Detter J.C., Durkin C.,
RA   Falciatore A., Fournet J., Haruta M., Huysman M.J., Jenkins B.D.,
RA   Jiroutova K., Jorgensen R.E., Joubert Y., Kaplan A., Kroger N., Kroth P.G.,
RA   La Roche J., Lindquist E., Lommer M., Martin-Jezequel V., Lopez P.J.,
RA   Lucas S., Mangogna M., McGinnis K., Medlin L.K., Montsant A.,
RA   Oudot-Le Secq M.P., Napoli C., Obornik M., Parker M.S., Petit J.L.,
RA   Porcel B.M., Poulsen N., Robison M., Rychlewski L., Rynearson T.A.,
RA   Schmutz J., Shapiro H., Siaut M., Stanley M., Sussman M.R., Taylor A.R.,
RA   Vardi A., von Dassow P., Vyverman W., Willis A., Wyrwicz L.S.,
RA   Rokhsar D.S., Weissenbach J., Armbrust E.V., Green B.R., Van de Peer Y.,
RA   Grigoriev I.V.;
RT   "The Phaeodactylum genome reveals the evolutionary history of diatom
RT   genomes.";
RL   Nature 456:239-244(2008).
RN   [2] {ECO:0000313|Proteomes:UP000000759}
RP   GENOME REANNOTATION.
RC   STRAIN=CCAP 1055/1 {ECO:0000313|Proteomes:UP000000759};
RG   Diatom Consortium;
RA   Grigoriev I., Grimwood J., Kuo A., Otillar R.P., Salamov A., Detter J.C.,
RA   Lindquist E., Shapiro H., Lucas S., Glavina del Rio T., Pitluck S.,
RA   Rokhsar D., Bowler C.;
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000256|ARBA:ARBA00004742}.
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DR   EMBL; CM000623; EEC44575.1; -; Genomic_DNA.
DR   RefSeq; XP_002183906.1; XM_002183870.1.
DR   AlphaFoldDB; B7GA98; -.
DR   STRING; 556484.B7GA98; -.
DR   PaxDb; 2850-Phatr49339; -.
DR   GeneID; 7195500; -.
DR   KEGG; pti:PHATRDRAFT_49339; -.
DR   eggNOG; KOG0369; Eukaryota.
DR   HOGENOM; CLU_000395_0_1_1; -.
DR   InParanoid; B7GA98; -.
DR   OrthoDB; 1129179at2759; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000000759; Chromosome 21.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004736; F:pyruvate carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR   CDD; cd06850; biotinyl_domain; 1.
DR   CDD; cd07937; DRE_TIM_PC_TC_5S; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 3.10.600.10; pyruvate carboxylase f1077a mutant domain; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR005481; BC-like_N.
DR   InterPro; IPR001882; Biotin_BS.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR003379; Carboxylase_cons_dom.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR000891; PYR_CT.
DR   InterPro; IPR005930; Pyruv_COase.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   NCBIfam; TIGR01235; pyruv_carbox; 1.
DR   PANTHER; PTHR43778; PYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR43778:SF2; PYRUVATE CARBOXYLASE, MITOCHONDRIAL; 1.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   Pfam; PF02436; PYC_OADA; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF89000; post-HMGL domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS00188; BIOTIN; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW   Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EEC44575.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Pyruvate {ECO:0000313|EMBL:EEC44575.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000759};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..1264
FT                   /note="pyruvate carboxylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002855624"
FT   DOMAIN          92..544
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          215..412
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          650..919
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   DOMAIN          1189..1264
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   1264 AA;  137882 MW;  DC58358F55F60D75 CRC64;
     MRRVAVFVLV LSMPSMAAAF APRRSWTTAT TPAGIETAAT MARRSLLSSL LRVSTGTDSE
     KDTNASTDSI QTDSVVTEAS ARNSKLVRNV PPFQRILAAN RAEIAVRIMR AATELNAGTV
     AMYTHEDRYS QHRWGADQSF LLDKKNPTSS PISAYLDIPQ IIRLALDAGV DAIHPGYGFL
     SESPEFAQAC ADASITFVGP TVENLQRFSD KTSARQAAIE ADVPVVPGSD GALETEADVT
     AFVEANGLPV ILKAAMGGGG KGMRVVRRME DLIPFFQAAS SEALASFGDG AVFVERFVER
     PRHIEVQIIG DGTGNVVHLW ERDCSIQRRH QKVIEMAPAW TLPDELRAQL HEYAVRLTSQ
     AKYKNAGTVE FLIDAELRPY FIEVNPRIQV EHTVTEEVTG IDLVQAQIKI AAGATLEEVG
     LVQANIQPRG VAIQCRVTTE NPERDFAPDT GTVTLYRHSA GKGVRMDGIG YSGMTITPYF
     DSMIVKYTAL GANFPETVAR MKRVLQECRI RGVKTNVGFL LNVLSHPEFE TGIVTTSFID
     ENPQLKQTSM SMYDFASEEQ ADPRKTFATE RLVRYLANLA VNGQPPELGA DSQKLTRTTA
     IADIPAPEIR SEGNAAVPSD ESPNQPGWRH LLLEQGPKAY AKAVREHQGL LITDTTWRDA
     HQSLLATRMR TQELIKSADY TNMALANAFS LEMWGGATFD VAMRFLRECP WERLEALREK
     VPNVPFQMLL RGANAVGYTN YADNVVHKFC KQAHDSGVDV FRVFDSLNYI ENLQLGVDAA
     GEAGGFVEGA MSYTGDVADP TKGKYSLEYY MNLASELVDM GVHSLAIKDM AGLLTPKAST
     LLVSALREAH PDIPIHVHTH DTAGSGVASM LAAAQAGADI VDSSMDAFSG MTSQPSLGAL
     VANLAGTERD TGIQLSNLPP LNSYWEDVRS LYAPFESGQL SGSSDVYFHE IPGGQYTNLL
     FQSKQLGLSD RWTEIKTKYA EANIILGDIP KVTPSSKVVG DLAQFLVSQN LEANEVLEKA
     DTLAFPDSVI NYLKGDIGVP PGGFPEPLRN KVLQSRNLEP IEGRPGKFLP DYNFDKEREL
     LEKRFGKANI DEKDCLSYAL YPDVFTEWKD FQALYGDVGK LPTRLFLNPM QVGDEVEIEI
     AKGQTLIVEL VSIQDVKEDG TRTVIFEVNG EPWYMPVTDQ NLLGDSAVRE KAVAPGQVGA
     SMPGVVVGLK VKAGDTVQEG ETVATLSAMK METSIPATAS GVIKRVLVNV GDKVNGDDLI
     LEIE
//
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