ID A0A1E7FCX0_9STRA Unreviewed; 1231 AA.
AC A0A1E7FCX0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
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:OEU16010.1};
GN ORFNames=FRACYDRAFT_186955 {ECO:0000313|EMBL:OEU16010.1};
OS Fragilariopsis cylindrus CCMP1102.
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Bacillariophyceae; Bacillariophycidae; Bacillariales; Bacillariaceae;
OC Fragilariopsis.
OX NCBI_TaxID=635003 {ECO:0000313|EMBL:OEU16010.1, ECO:0000313|Proteomes:UP000095751};
RN [1] {ECO:0000313|EMBL:OEU16010.1, ECO:0000313|Proteomes:UP000095751}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1102 {ECO:0000313|EMBL:OEU16010.1,
RC ECO:0000313|Proteomes:UP000095751};
RG DOE Joint Genome Institute;
RA Mock T., Otillar R.P., Strauss J., Dupont C., Frickenhaus S., Maumus F.,
RA Mcmullan M., Sanges R., Schmutz J., Toseland A., Valas R., Veluchamy A.,
RA Ward B.J., Allen A., Barry K., Falciatore A., Ferrante M., Fortunato A.E.,
RA Gloeckner G., Gruber A., Hipkin R., Janech M., Kroth P., Leese F.,
RA Lindquist E., Lyon B.R., Martin J., Mayer C., Parker M., Quesneville H.,
RA Raymond J., Uhlig C., Valentin K.U., Worden A.Z., Armbrust E.V., Bowler C.,
RA Green B., Moulton V., Van Oosterhout C., Grigoriev I.;
RT "Extensive genetic diversity and differential bi-allelic expression allows
RT diatom success in the polar Southern Ocean.";
RL Submitted (SEP-2016) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV784359; OEU16010.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E7FCX0; -.
DR EnsemblProtists; OEU16010; OEU16010; FRACYDRAFT_186955.
DR KEGG; fcy:FRACYDRAFT_186955; -.
DR InParanoid; A0A1E7FCX0; -.
DR OrthoDB; 1129179at2759; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000095751; Unassembled WGS sequence.
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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Pyruvate {ECO:0000313|EMBL:OEU16010.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000095751};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1231
FT /note="pyruvate carboxylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009192958"
FT DOMAIN 68..519
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 190..387
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 617..886
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 1156..1231
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 1231 AA; 134247 MW; 6B84D1C8E50095C1 CRC64;
MWKLSAAFLA TLALCNNNNN AVDAFTGPFS SVGSKVSSSS PTLLRETVEK EATSSAPSVS
SPSSEKFFFK NIMAANRAEI AVRIMRAATE MNAGTVGIYV NEDKYSQHRW GADRSFLLEK
EDDATPISAY LDIDQIIQIA KDADVDAIHP GYGFLSESPE FAQACADADI AFVGPTVENL
NRFADKTSAR IAAINAGVPV VPGSDGALRT SEEVVEFVEG IGLPVIIKAS MGGGGKGMRV
VKRMEDLVSL FESASSEALT SFGDGSVFIE RFVDRPRHIE VQVIGDGTGN VVHLWERDCS
IQRRHQKVIE MAPAFTLPME LRVQLQDYAV KLTSEAKYKN AGTVEFLVDS EMRPYFIEVN
PRIQVEHTVT EEVTGIDLVQ AQMKIAAGAT LEEAGLIQEN ISARGVAIQC RITTENPERD
FAPDTGTISL YRHAAGCGVR MDGVGYSGLK ITPFFDSMIV KYTVRGSNFE EATARMSRVL
QECRIRGVKT NIPFLLNCLQ HPDFTNGELT TAFIDEHPGL KKTSTSMWQF ANEFQADPKK
LGSSERRLRY LANLAVNGHP PELGVDVNRL ASGATASIPR PVVPKSTSAK KERSLRSILL
NEGPEGMAKA VRDNKGLLIM DTTWRDAHQS LLATRMRTQE FERCSEATNE AMANAFSLEM
WGGATFDVAM RFLHECPWKR LESLREKVPD IPFQMLLRGA NAVGYTNYAD NVNYKFCQQA
KDSGIDVFRV FDSLNYLDNL KLGVDAAGKA GGFVEGTMSY TGDVADPSKG KYNLEYYMKL
GRELVDMGSH SLAIKDMAGL LTPRAATLLV SALRAEFPDI PIHVHTHDTA GSGVASMLAA
AEAGADVVDG AIDAMSGMTS QPSIGAIAAN LRGTDLDTGL EMAQLAPLNT YWENVRSLYA
PFESGQLSGS SDVYQHEIPG GQYTNLLFQS KQLGLTERWP EIKRKYAEAN IVLGDIPKVT
PSSKVVGDLA QFMVQQNLEG KDVLDQAETL AFPDSVVNFL RGDIGIPPGG FPEPLRTKVL
KSRGLEPVEG RPGSFLKDYD FEKEREALYK AYGEENIDEK DLLSYALYPG VFKDWKDYQV
VYGDTDILPT ELFLNPMKVG QEVDLELGKG RSRVIKMVAI QDVDENGSRE VLFEVNGEPY
YMSVTDHSAE VEGGVREKAG APGTVGSPMP GVVVGIKVKV GDKIKEGDTV ATLSAMKMET
SVPATSTGVV TRIVVNVGDK VDGDDLLIEI E
//
