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
//