ID K1VUK6_TRIAC Unreviewed; 1051 AA.
AC K1VUK6;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=pyruvate carboxylase {ECO:0000256|ARBA:ARBA00013057};
DE EC=6.4.1.1 {ECO:0000256|ARBA:ARBA00013057};
GN ORFNames=A1Q2_01507 {ECO:0000313|EMBL:EKD04161.1};
OS Trichosporon asahii var. asahii (strain CBS 8904) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Trichosporon.
OX NCBI_TaxID=1220162 {ECO:0000313|EMBL:EKD04161.1, ECO:0000313|Proteomes:UP000006757};
RN [1] {ECO:0000313|EMBL:EKD04161.1, ECO:0000313|Proteomes:UP000006757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 8904 {ECO:0000313|EMBL:EKD04161.1,
RC ECO:0000313|Proteomes:UP000006757};
RX PubMed=23193141; DOI=10.1128/EC.00264-12;
RA Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT "Genome sequence of the Trichosporon asahii environmental strain CBS
RT 8904.";
RL Eukaryot. Cell 11:1586-1587(2012).
CC -!- FUNCTION: Pyruvate carboxylase catalyzes a 2-step reaction, involving
CC the ATP-dependent carboxylation of the covalently attached biotin in
CC the first step and the transfer of the carboxyl group to pyruvate in
CC the second. {ECO:0000256|ARBA:ARBA00002380}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + hydrogencarbonate + pyruvate = ADP + H(+) + oxaloacetate
CC + phosphate; Xref=Rhea:RHEA:20844, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:17544,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=6.4.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000564};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000256|ARBA:ARBA00004742}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKD04161.1}.
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DR EMBL; AMBO01000233; EKD04161.1; -; Genomic_DNA.
DR AlphaFoldDB; K1VUK6; -.
DR STRING; 1220162.K1VUK6; -.
DR eggNOG; KOG0369; Eukaryota.
DR HOGENOM; CLU_000395_0_1_1; -.
DR InParanoid; K1VUK6; -.
DR OMA; YAIQSRV; -.
DR OrthoDB; 1129179at2759; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000006757; 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; 2.
DR CDD; cd07937; DRE_TIM_PC_TC_5S; 1.
DR Gene3D; 2.40.50.100; -; 2.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011761; ATP-grasp.
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; 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; PF00364; Biotin_lipoyl; 2.
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; SSF51246; Rudiment single hybrid motif; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 2.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00188; BIOTIN; 2.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR PROSITE; PS00867; CPSASE_2; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000006757}.
FT DOMAIN 1..351
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 1..63
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 22..218
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 437..706
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 972..1050
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 1051 AA; 114495 MW; 9383A53C983B3ADE CRC64;
MGGVVVEVRV KEGQDVKAGD PIAVLSAMKM ESVVSAPVSG KVARVLVAEN DSLGSGDLMA
AMGGGGRGMR VVRDEASFKD NFERAVSEAK SAFGDGTVFI ERFLDKPRHI EVQLLADSQG
NCVHLFERDC SVQRRHQKVV EVAPAPHLDE NTRQAILSDA LKLAHAVGYR NAGTAEFLVD
QQNRHYFIEI NPRIQVEHTI TEEITGIDIV AAQIQIAAGV TLEQLGLTQD HIHRRGFAIQ
SRITTEDPAA GFQPDTGKIE VYRSAGGNGV RLDAASGYAG AQITPHYDSL LVKCSVSGAT
YEVARRKMLR ALIEFRIRGV KTNIPFLIRL LTHPVFESGR TWTTFIDDTP ELFKLVQSQN
RAQKLLAYLG DLTVNGSSIM GQSGEPGLKT EALIPSIVDK DGKKVDTSVS QQKGWRNIIV
NEGPEAFAKA IRAYPGCLIM DTTWRDAHQS LLATRMRTVD MANIAKETSH ALANAYSLEC
WGGATFDVAM RFLYEDPWER LRTLRKLVPN IPLQALVRGA NAVGYTSYPD NAIYEFSKKA
VENGLDIFRV FDSLNYFENL KVGIDAAKKA GGVVEGTICY SGDVANPKKT KYTLDYYLDL
TNKLVGEGIH VLGIKDMAGL LKPEAATMLV GAIRKAHPNL PIHVHSHDTA GIAVASMLAA
AKAGADVVDV AIDDLSGLTS QPAMGAVCAA LEQSNLGPGI SHENITALNT YWSQIRQLYQ
CFEANVRASD SGVFDHEMPG GQYTNLQFQA SQLGLGTQWI EIKKAYQEAN QLCGDIVKVT
PSSKVVGDFA QFMVSNKLTP EEVIERADKL DFPSSVVEFF QGYLGQPVGG FPEPLRSKII
RDKPKIDQRP GLSMKPLDFK KIKAELREQY GNQINDNDVM SYVMYPAVFK EFQKFLESYG
DLSVVPTRWF LGKPQIGEEM AIPIEQGKTL TVKLLAVGPL DTNKGTREVF WELNGETRAV
VVTDKNAAVE VVTREKATSE PGSVGAPMGG VVVEVRVKEG QDVKAGDPIA VLSAMKMESV
VSAPVSGKVA RVLVAENDSL GSGDLMVEIT H
//
