ID B9X0T8_EMIHU Unreviewed; 1274 AA.
AC B9X0T8;
DT 14-APR-2009, integrated into UniProtKB/TrEMBL.
DT 14-APR-2009, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE RecName: Full=pyruvate carboxylase {ECO:0000256|ARBA:ARBA00013057};
DE EC=6.4.1.1 {ECO:0000256|ARBA:ARBA00013057};
GN Name=EhPYC {ECO:0000313|EMBL:BAH22705.1};
OS Emiliania huxleyi (Coccolithophore) (Pontosphaera huxleyi).
OC Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Isochrysidales;
OC Noelaerhabdaceae; Emiliania.
OX NCBI_TaxID=2903 {ECO:0000313|EMBL:BAH22705.1};
RN [1] {ECO:0000313|EMBL:BAH22705.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIES 837 {ECO:0000313|EMBL:BAH22705.1};
RX PubMed=19109302; DOI=10.1093/pcp/pcn200;
RA Tsuji Y., Suzuki I., Shiraiwa Y.;
RT "Photosynthetic carbon assimilation in the coccolithophorid Emiliania
RT huxleyi (Haptophyta): Evidence for the predominant operation of the c3
RT cycle and the contribution of {beta}-carboxylases to the active anaplerotic
RT reaction.";
RL Plant Cell Physiol. 50:318-329(2009).
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; AB461363; BAH22705.1; -; mRNA.
DR AlphaFoldDB; B9X0T8; -.
DR SMR; B9X0T8; -.
DR BRENDA; 6.4.1.1; 2068.
DR UniPathway; UPA00138; -.
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 2: Evidence at transcript level;
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:BAH22705.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Pyruvate {ECO:0000313|EMBL:BAH22705.1};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..1274
FT /note="pyruvate carboxylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002894181"
FT DOMAIN 75..527
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 198..395
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 631..900
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 1172..1248
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 573..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1247..1274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1274 AA; 137324 MW; 633BFEB19FB9990F CRC64;
MTKILLMLAL ALGAAGLRWP AAVPQRRATS GRAAGARLER AVGPVAVAPV EAPSVSRSSE
SAVDAMRGAA EAPSPFKKLM AANRAEIAVR IMRAATELNV ATVAIYGYED RFSQHRWGAD
QSFQLEKKDP ADAAVRAYLD IEQIVALAKR EGVDAIHPGY GFLSESPEFA QACSDAGITF
VGPTVANLKT FSDKTTARVA AIAADVPVVP GTDEPVTTEA GARAFVEEYG LPVIIKAAMG
GGGKGMRLVR DMEELGASFA SASTEAEAAF GDGSVFLERY IESPRHIEVQ IIGDGKGGAV
HLCERDCSVQ RRYQKVVEIA PAWSLDPALR NKLHEDSLRL MRSAKYLNAG TVEFLVDGEG
RHYFIEVNPR IQVEHTVTEE VTGIDLVQAQ MRIASGASFE EVGLVQDQIQ ARGIAVQCRV
TTENPERNFA PDTGTLSVYR HSAGYGMRQD GIGYSGMTVT PYYDSLLVKY TARGSNWGEV
IRRMTRALQE ARIRGVKTNI PFLLNVLTHP EFKAGVVTTG FIDEHPELLQ VTGKNWDFAN
VHQADQEKVM QVEKLLRYLA NLAVNGHPKE LGANPARLRT APQPQVKPPR VLIPGKDDAP
TAGRRPGGWR SLLLAEGPAA YAKAVREHKG LLVMDTTWRD AHQSLLATRM RTADLVKAGA
ATNAALSNAF SLEMWGGATF DVAMRFLHEC PWQRLERLRE EVPDVPFQML LRGANAVGYT
NYPDNLVYRF CKQAAASGID VFRVFDSLNY LENLKLGIEA AGEAGGFVEA AICYTGDITD
PSKGKYTLDY YLEYARQLAQ LGVHSIAIKD MAGLLKPRAA ALLVGAIRKE LPDMLIHVHS
HDTAGNSLAS MLSAAEAGAD VVDVAIDSMS GITSQPSLGA LAAATAGSEL DIGVRPQDLE
PLNSYWEQVR SLYAPFESGQ LSGSSDVYRN EIPGGQYTNL LFQASQLGLG DQWVEVKRKY
AQANLLLGDI PKVTPSSKVV GDLAQLMVAQ KLEPDQLIEQ AESLAFPDSV VSYFQGGIGL
PPGGFPEPLR SKVLKGRSLE DGRAAYDGRP GATMKPYDFD KELGLLQASY PSNKGERDAL
SYALYPQVFR DWQEHRAVYG EVEALPTEAF LHPMAVGDEV EFATEPGRSW IVKLVSVPKP
DENGQTQVIM ELNGERWFVP VTDNSVQSAT AREKAGGSPG SVGSPMPGVV VDVKVKPGDT
IREGEPLVVL SAMKMETAIP APASGVVERL LVSAGDKVEG DDLLAQIGEG APKEEGGSSA
KGGLFSSLFK GSGE
//
