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Database: UniProt
Entry: A0A0V1A1V3_9BILA
LinkDB: A0A0V1A1V3_9BILA
Original site: A0A0V1A1V3_9BILA 
ID   A0A0V1A1V3_9BILA        Unreviewed;       543 AA.
AC   A0A0V1A1V3;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   22-FEB-2023, entry version 13.
DE   SubName: Full=Pyruvate carboxylase 1 {ECO:0000313|EMBL:KRY18722.1};
GN   Name=pyc-1 {ECO:0000313|EMBL:KRY18722.1};
GN   ORFNames=T12_1126 {ECO:0000313|EMBL:KRY18722.1};
OS   Trichinella patagoniensis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY18722.1, ECO:0000313|Proteomes:UP000054783};
RN   [1] {ECO:0000313|EMBL:KRY18722.1, ECO:0000313|Proteomes:UP000054783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS2496 {ECO:0000313|EMBL:KRY18722.1};
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:KRY18722.1}.
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DR   EMBL; JYDQ01000043; KRY18722.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1A1V3; -.
DR   Proteomes; UP000054783; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004736; F:pyruvate carboxylase activity; IEA:InterPro.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR   CDD; cd06850; biotinyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.10.600.10; pyruvate carboxylase f1077a mutant domain; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR003379; Carboxylase_cons_dom.
DR   InterPro; IPR000891; PYR_CT.
DR   InterPro; IPR005930; Pyruv_COase.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR43778; PYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR43778:SF2; PYRUVATE CARBOXYLASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   Pfam; PF02436; PYC_OADA; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   SUPFAM; SSF89000; post-HMGL domain-like; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   4: Predicted;
KW   Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432};
KW   Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000313|EMBL:KRY18722.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054783};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..543
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006874132"
FT   DOMAIN          1..150
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   DOMAIN          411..480
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   543 AA;  59847 MW;  AFD9325DBD6FA2B1 CRC64;
     MRIVFLFFSF SMCGVIETAI SYTGDVADSN RQMYNLNYYL KLADEIVKAG THILCIKDMA
     GLLKPRSSKV LLSALRDRFP DLPIHVHSHD TAGVSVASML ACVEAGADIV DVAVDSMSGM
     TSQPSMGIDS ADVSKYSAYW ESARQLYGPF ECTTTMKSGN ADVYVHEIPG GQYTNLQFQA
     YSLGLGDKFE QIKRKYVEAD ALLGKLIKVT PTSKIVGDLA QFMVHNNLDG PTLLKQASTL
     SFPESVVQFM QGMIGQPPYG FPEPLRTQIL RHRERIDGRP GESLPPVDFE TLRQQLQQKH
     EKQIRDVHVI SYAMYPKVTD DFLTFVEKYG PVDKLPTHAF FMGLSNGEEI DVELEKGKSM
     RIKMLAKSSL NAVGEREVFL ELNGQLRSFI VKDKEASKDD TSHPKADPTV IGSVGAPMPG
     EVLQIKVKEG DVVKMKTPLI VITAMKMEMI IESPLDGVVK TVFAKPAMKC NAGDLLVLIE
     IMNTNVRSAG CLSSSSSSSS SFPSSLIQST DFDRLNRLMD GCCTSKEPLE CGSSREIARR
     SLE
//
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