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
//