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Database: UniProt
Entry: A0A2U1M8I6_ARTAN
LinkDB: A0A2U1M8I6_ARTAN
Original site: A0A2U1M8I6_ARTAN 
ID   A0A2U1M8I6_ARTAN        Unreviewed;       742 AA.
AC   A0A2U1M8I6;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   08-NOV-2023, entry version 18.
DE   SubName: Full=Methylcrotonyl-CoA carboxylase alpha chain {ECO:0000313|EMBL:PWA57557.1};
GN   ORFNames=CTI12_AA406440 {ECO:0000313|EMBL:PWA57557.1};
OS   Artemisia annua (Sweet wormwood).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae; Anthemideae;
OC   Artemisiinae; Artemisia.
OX   NCBI_TaxID=35608 {ECO:0000313|EMBL:PWA57557.1, ECO:0000313|Proteomes:UP000245207};
RN   [1] {ECO:0000313|EMBL:PWA57557.1, ECO:0000313|Proteomes:UP000245207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Huhao1 {ECO:0000313|Proteomes:UP000245207};
RC   TISSUE=Leaf {ECO:0000313|EMBL:PWA57557.1};
RX   PubMed=29703587; DOI=10.1016/j.molp.2018.03.015;
RA   Shen Q., Zhang L., Liao Z., Wang S., Yan T., Shi P., Liu M., Fu X., Pan Q.,
RA   Wang Y., Lv Z., Lu X., Zhang F., Jiang W., Ma Y., Chen M., Hao X., Li L.,
RA   Tang Y., Lv G., Zhou Y., Sun X., Brodelius P.E., Rose J.K.C., Tang K.;
RT   "The genome of Artemisia annua provides insight into the evolution of
RT   Asteraceae family and artemisinin biosynthesis.";
RL   Mol. Plant 11:776-788(2018).
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:PWA57557.1}.
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DR   EMBL; PKPP01006131; PWA57557.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U1M8I6; -.
DR   STRING; 35608.A0A2U1M8I6; -.
DR   Proteomes; UP000245207; 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; IPR045774; MCCA_BT_dom.
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   Pfam; PF19331; MCCA_BT; 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; PS50968; BIOTINYL_LIPOYL; 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   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000245207}.
FT   DOMAIN          45..492
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          164..362
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          664..740
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   742 AA;  82372 MW;  145FAA4468FBBE4C CRC64;
     MSLTTLIYRY KLNRNKLTHI RSLTTTTSSS TNLPNRQNNN NDNRKIEKIL IANRGEIACR
     IIRTAKKLGI KTVAVYSDAD RYSLHVKSAD EAVRIGPASA RLSYLNKEVI VDAAQRTGAQ
     AIHPGYGFLS ENADFAQLCE NEGFTFVGPP ASAIREMGDK SASKRIMGAA GVPLVPGYHG
     HEQDIDVMKS EAEKIGYPLL IKPTHGGGGK GMRIVESPKE FVDSFLGAQR EAAASFGVNT
     ILLEKYITRP RHIEVQVFGD KQGNVVYLYE RDCSVQRRHQ KIIEEAPAPD IISDFRSRLG
     QAAVSAAKAV GYHNAGTVEF IVDTLSGEFY FMEMNTRLQV EHPVTEMIVG QDLVEWQIRV
     ANGESLPLGQ EQIPLSGHAF EARIYAENVP KGFLPATGVL QYYRPIPVSE SVRVETGVEE
     GDTVSMHYDP MIAKLVVWGE NRSAALVKLK DSLSKFQVAG LPTNIEFLYK LANHRAFENA
     ELETHFIDQF KDDLFVKQND SVSAEAAYDA AKHSAVLLAA CICEKEHTLV KKSPPGGLSV
     WFTHPPFRLN HYATRTIELE WENEYRENNS EHLTLSISHL PNGNYLIKME ENDFPATEVA
     ITHLGDHDFR VEADGISKSV NLASYFTDKT QHIHIWHGSD HHHFKQKVGL DLLDNLETHQ
     HRNHESASHP PGTVIAPMAG LVVKVLVKDG MKVEEGQPLL VMEAMKMEHV IKAPISGLVS
     GLQLTPGQQV NDNSVLFKVE AA
//
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