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Database: UniProt
Entry: A0A0W8D5P6_PHYNI
LinkDB: A0A0W8D5P6_PHYNI
Original site: A0A0W8D5P6_PHYNI 
ID   A0A0W8D5P6_PHYNI        Unreviewed;       702 AA.
AC   A0A0W8D5P6;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Methylcrotonoyl-CoA carboxylase subunit alpha {ECO:0000313|EMBL:KUF78882.1};
GN   ORFNames=AM587_10004588 {ECO:0000313|EMBL:KUF78882.1}, AM588_10003657
GN   {ECO:0000313|EMBL:KUF91468.1};
OS   Phytophthora nicotianae (Buckeye rot agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4790 {ECO:0000313|EMBL:KUF91468.1, ECO:0000313|Proteomes:UP000054636};
RN   [1] {ECO:0000313|Proteomes:UP000052943, ECO:0000313|Proteomes:UP000054636}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 0 {ECO:0000313|Proteomes:UP000052943}, Race 0
RC   {ECO:0000313|EMBL:KUF78882.1}, Race 1 {ECO:0000313|EMBL:KUF91468.1},
RC   and race 1 {ECO:0000313|Proteomes:UP000054636};
RA   Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT   "Genomes and virulence difference between two physiological races of
RT   Phytophthora nicotianae.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
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:KUF91468.1}.
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DR   EMBL; LNFO01005122; KUF78882.1; -; Genomic_DNA.
DR   EMBL; LNFP01000576; KUF91468.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0W8D5P6; -.
DR   STRING; 4790.A0A0W8D5P6; -.
DR   EnsemblProtists; KUF78882; KUF78882; AM587_10004588.
DR   EnsemblProtists; KUF91468; KUF91468; AM588_10003657.
DR   OMA; FINKPKH; -.
DR   OrthoDB; 1129179at2759; -.
DR   Proteomes; UP000052943; Unassembled WGS sequence.
DR   Proteomes; UP000054636; 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; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
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   SMART; SM01209; GARS_A; 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; PS50968; BIOTINYL_LIPOYL; 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:UP000052943}.
FT   DOMAIN          26..472
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          145..342
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          625..702
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   702 AA;  77364 MW;  0C5971D2008A15AD CRC64;
     MLRLRLLQPA LLGPTSRRAL SSTPRSFRKI LVANRGEIAL RVLRSAQKLN IETVAVYSDA
     DANSQHVKLA TEAYRLGPAP AAESYLNYPK ILEICRESGV EAVHPGYGFL SENAAFARAC
     EEAGVEFIGP PVKAIEDMGS KSASKDIMIK AGVPVTPGYH GADQSFETLQ REAKKIGYPV
     LIKAVLGGGG KGMRIVDEEK DFQDALDACV REGQASFGDG RVLIEKYLRK PRHVELQIFG
     DKHGNVIHLF ERDCSVQRRH QKVLEEAPAP NMSEALRKKM GDAAVAAAKA VGYVGAGTVE
     FLLDEDESFY FMEMNTRLQV EHPVTEMITK QDLVELQLKV AAGQELPIRQ EDLKIHGHAV
     EARIYAENPY NDFLPGSGKL QHLRLPSRSK DVRVDTGIIE GDEVSIFYDP MIAKLIVHGD
     NRQAALDKMI KALHEYQIVG LPTNIEFVAR TADHAAFRKG GVDTSFLNKF GDEVLGSLGT
     YPTYAKALGA VSLLLLEQVK RRPAGNYNGE LQSPWSDDSL AHFRSLETLE RKLSLSHDDD
     EASVSVKCLA KDTYAVILDG DAGQETHEVS GAIDKRGDFK FRVGNRTFKG TAVIHQQELH
     LFCDDNSQRY DYKFHVPLPS FEPAEGSAGA AAHSKIAAPM PGKIIKVLVK NGDTITADQP
     LLIMEAMKME HMIRAPKDGK VQELFCEKDD FVTDGHVLVE LD
//
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