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
//