ID A0A183KDH7_9TREM Unreviewed; 694 AA.
AC A0A183KDH7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Propionyl-CoA carboxylase alpha chain, mitochondrial {ECO:0000313|WBParaSite:SCUD_0001307201-mRNA-1};
GN ORFNames=SCUD_LOCUS13069 {ECO:0000313|EMBL:VDP51184.1};
OS Schistosoma curassoni.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6186 {ECO:0000313|Proteomes:UP000050789, ECO:0000313|WBParaSite:SCUD_0001307201-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SCUD_0001307201-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDP51184.1, ECO:0000313|Proteomes:UP000279833}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Dakar {ECO:0000313|EMBL:VDP51184.1}, and Dakar, Senegal
RC {ECO:0000313|Proteomes:UP000279833};
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; UZAK01035579; VDP51184.1; -; Genomic_DNA.
DR STRING; 6186.A0A183KDH7; -.
DR WBParaSite; SCUD_0001307201-mRNA-1; SCUD_0001307201-mRNA-1; SCUD_0001307201.
DR Proteomes; UP000050789; Unplaced.
DR Proteomes; UP000279833; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.700.30; -; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 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 SMART; SM00878; Biotin_carb_C; 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 SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 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}; Reference proteome {ECO:0000313|Proteomes:UP000279833}.
FT DOMAIN 8..455
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 127..324
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 694 AA; 76746 MW; B20B135EFDF40964 CRC64;
MPVPRPWKFD KVLIANRGEI ACRIIQSCKR LGIRTVAIHS EVDYISRFVS MADEAVCVGP
PPSAQSYLNM PAILNAVKST GAQAVHPGYG FLSENTLFAA ELEKMNVVFL GPNSRAIKAM
GDKIESKRIA NQAKVNCIPG YDGEVDGPDE AARIAAEIGY PVMIKASAGG GGKGMRIAWN
EKEAREGYRL SKSEAKASFG DDRMLIEKFI DNPRHIEIQV LCDRHGNAIY LNERECSIQR
RNQKVIEEAP STFLDPASRK AMGEQAVSLA KAVGYDSAGT VEFLVDSKRN FYFLEMNTRL
QVEHPITECI TGVDVVHQML RVGKGHPLML SQSDIPVNGW AFECRVYAED PYKAFGLPSI
GRLRTYSEPL HIPNVRCDSG INEGSEISIY YDPMICKLVT YGPDRQTALN TMAKALDSYI
IRGVTHNIPL LRDIVTEKRF VSGNISTKYL SEVYPDGFKG KVLDQKELDT LISVSASIFA
KNDARIRNCS GESQWDLVAS VHENSANSDP KSRSYIRCIV TRDCSGFQVR MSSWEPPKHI
NQQDVNATSQ SSKSQETVVR VADNFKLSDK IINHSYDGNE ATSAPIDRLV TLQLLDKSIN
TVCLQYLGTA FPIEIMNTTA AWFRAAYMPP PRVIDYGSIC IAPMPGLVRS VAVKLGDRVS
EGQELCVLEA MKMQNSMTAS RSGVVSFIIS EFCT
//
