ID A0A0V0XAJ5_9BILA Unreviewed; 647 AA.
AC A0A0V0XAJ5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 22-FEB-2023, entry version 24.
DE SubName: Full=Pyruvate carboxylase 1 {ECO:0000313|EMBL:KRX85033.1};
DE Flags: Fragment;
GN Name=pyc-1 {ECO:0000313|EMBL:KRX85033.1};
GN ORFNames=T06_9652 {ECO:0000313|EMBL:KRX85033.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX85033.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX85033.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX85033.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KRX85033.1}.
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DR EMBL; JYDK01000003; KRX85033.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0XAJ5; -.
DR Proteomes; UP000054673; 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:InterPro.
DR GO; GO:0006094; P:gluconeogenesis; IEA:InterPro.
DR GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR CDD; cd07937; DRE_TIM_PC_TC_5S; 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; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
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 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; PF02786; CPSase_L_D2; 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; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 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 Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Pyruvate {ECO:0000313|EMBL:KRX85033.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054673}.
FT DOMAIN 1..434
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 104..301
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 511..647
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX85033.1"
SQ SEQUENCE 647 AA; 72602 MW; 8E55C19289B48067 CRC64;
LRALNELQIR SVGIYSEQDV NQMHRLKADE AYLVGRGMTA VSAYLNIHEI IKLAKIHDVD
AIHPGYGFLS ERADFAQACH DASITFIGPS PEVMLRMGDK ISARVAAAEA GVSVVPGIEN
PIENAEEAAE FGKQYGFPVI FKAAYGGGGR GMRRVDKLDQ VQEAFNRATS EALAAFGNGL
MFVEKFIERP RHIEVQILGD MYGNIVHLYE RDCSVQRRHQ KIIEIAPAPN LDPQKRQLML
DDAVRLARHV KYENAGTVEF LLDQDGRHYF IEVNARLQVE HTVTEDITGV DLVQAQVRIA
EGKSLEELHL CQDLVTPIGS ALQCRITAED PSMDFCPDSG RIEVFRSGEG MGIRIDSASA
YAGALISPYY DSLLVKVIAH SRNYKTTVNK MMRALKEFRI RGVKTNIPFL LNVLNNQRFL
DGLVDTCFID ENPDLFKFMP SQNRAQKLLR FLKDVKVNGP MTPLVTGIPS AKVTPIVPEY
DTRPLLKGWR DVLLEKGPVN FAKEIRKNRG ILLTDTTFRD AHQSLLATRV RTYDLQRIAP
FLAHAMPNLF SIEMWGGATF DVSMRFLHEC PWERLEILRK HVPNIPFQML LRGANAVGYT
SYPDNVVVKF CELAKKSGID VFRIFDSLNY MPNIILGIEA VANAGKD
//
