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Database: UniProt
Entry: W7TSL4_9STRA
LinkDB: W7TSL4_9STRA
Original site: W7TSL4_9STRA 
ID   W7TSL4_9STRA            Unreviewed;       746 AA.
AC   W7TSL4;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   22-FEB-2023, entry version 34.
DE   SubName: Full=Methylcrotonoyl-carboxylase {ECO:0000313|EMBL:EWM23339.1};
GN   ORFNames=Naga_100053g29 {ECO:0000313|EMBL:EWM23339.1};
OS   Nannochloropsis gaditana.
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Eustigmatophyceae;
OC   Eustigmatales; Monodopsidaceae; Nannochloropsis.
OX   NCBI_TaxID=72520 {ECO:0000313|EMBL:EWM23339.1, ECO:0000313|Proteomes:UP000019335};
RN   [1] {ECO:0000313|EMBL:EWM23339.1, ECO:0000313|Proteomes:UP000019335}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-31 {ECO:0000313|EMBL:EWM23339.1,
RC   ECO:0000313|Proteomes:UP000019335};
RX   PubMed=23966634; DOI=10.1093/mp/sst120;
RA   Corteggiani Carpinelli E., Telatin A., Vitulo N., Forcato C., D'Angelo M.,
RA   Schiavon R., Vezzi A., Giacometti G.M., Morosinotto T., Valle G.;
RT   "Chromosome Scale Genome Assembly and Transcriptome Profiling of
RT   Nannochloropsis gaditana in Nitrogen Depletion.";
RL   Mol. Plant 7:323-335(2014).
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:EWM23339.1}.
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DR   EMBL; AZIL01001690; EWM23339.1; -; Genomic_DNA.
DR   AlphaFoldDB; W7TSL4; -.
DR   EnsemblProtists; EWM23339; EWM23339; Naga_100053g29.
DR   OrthoDB; 1129179at2759; -.
DR   Proteomes; UP000019335; Chromosome 17.
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   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.
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:UP000019335}.
FT   DOMAIN          48..497
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          167..365
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          670..744
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   746 AA;  80769 MW;  00A9DCFFBCF9152B CRC64;
     MWNCGRLVKI HISLPWRTSG SVLYSRSLMS HGSTSATPVE GSPPSSKPFT KLLIANRGEI
     ACRIIRTARK MGIKTVAVYS DADARSQFVR MADEAHWIGP SPTTESYLVK EKILEVAKRA
     GVQALHPGYG FLSENPDFAE MCQSAGVVFV GPPVPALRSM GSKAAAKRIM TEAGVPVTPA
     YYGEEQDDAR LLAEAEKVGY PVMIKAVTGG GGKGMRRVMA AADFLPALEA CRREALKSFG
     RDRMLIEKYL VDPRHIELQV FGDRHGNAVH LHERDCSVQR RHQKVLEESP APGLGEALRE
     EMGRAAVLAA KAVGYTGAGT VEFLLDPASQ RFYFCEMNTR LQVEHCVTEM VTGVDLVEWQ
     LRVAAGEPLP VREQADIRAR GHAIEARIYA ENPAKGFLPA TGSLKRLRTP VSEEGAVRVE
     TGVVEGDEVS MYYDPMIAKL LTWAPSRPEA LRRMARGLRD YQIAGLPNNL EFLERCVGHP
     AFERGGVTTG FLVEYEADVS IPPPSPPSPH LLALAAYALT QQREAPRGST PWLGGAWRGV
     GRRRLPVEFV VDGLEESFAL KAGVMDGGVQ EGGGGGRHAW GLRVEMPDGQ AYRVSGSRCE
     GERASGAHGD EWEATVEGVT YKYSAWIEDG GMRGGARVQL WLRSGGLVDD PLQRTTFSLR
     VPAAALGHEL AGGVMPRILA PMPGKLVKVL VKAGEAVRKG QSLLILEAMK MEHVITAPQD
     ATVDSVARAV GDVVQEGIPL VSLKAA
//
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