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Database: UniProt
Entry: A0A1I6MS38_9GAMM
LinkDB: A0A1I6MS38_9GAMM
Original site: A0A1I6MS38_9GAMM 
ID   A0A1I6MS38_9GAMM        Unreviewed;       665 AA.
AC   A0A1I6MS38;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=3-methylcrotonyl-CoA carboxylase alpha subunit {ECO:0000313|EMBL:SFS18540.1};
GN   ORFNames=SAMN05216570_3751 {ECO:0000313|EMBL:SFS18540.1};
OS   Dyella sp. OK004.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Dyella.
OX   NCBI_TaxID=1855292 {ECO:0000313|EMBL:SFS18540.1, ECO:0000313|Proteomes:UP000198834};
RN   [1] {ECO:0000313|EMBL:SFS18540.1, ECO:0000313|Proteomes:UP000198834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK004 {ECO:0000313|EMBL:SFS18540.1,
RC   ECO:0000313|Proteomes:UP000198834};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FOZI01000005; SFS18540.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6MS38; -.
DR   STRING; 1855292.SAMN05216570_3751; -.
DR   OrthoDB; 9763189at2; -.
DR   Proteomes; UP000198834; 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; 3.30.700.40; -; 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; 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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000198834}.
FT   DOMAIN          1..447
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          120..317
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          588..664
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   665 AA;  72578 MW;  A7A124DD5372ABA0 CRC64;
     MFNRVLIANR GEIACRVIRT CRRLGIHTIA VYSEADADAQ HVRLADEAWP IGGARPADSY
     LRSDAILDVA KRSGAQAIHP GYGFLSENTA FARACTEAGI AFIGPRPESI DAMGSKAAAK
     ALMEQHAVPL VPGYHGENQD AGFLAEQARH TGFPLMIKAA AGGGGKGMRI VRSEKEFADA
     LASAQREAAN AFGDTRVILE RYVEHPRHIE FQVFGDSHGN MIHLNERECS AQRRYQKVLE
     ETPSPFLTPE RRKAMGDAAV AAAQAVNYVG AGTVEFIVAQ DGEFFFMEMN TRLQVEHPVT
     EETLGLDLVE WQLRIAFGEP LPLRQEQVHA HGHAIEVRLY AEDPDQNFLP GSGKLLRLQL
     PTPSRHVRID GGVIEGDTVT IFYDPMIAKL IVYDRDRTQA LQRLREALAA CEIAGPKSNI
     AFLERLASHP AVVEGRIDTG YLDRHLDEFL AGDAAPSNTV LFAAATAALL HDECAVVTGT
     RHSTDPFSPW GSADAWRVGH AGKRIIALSL REQRYEIEAH GHDGRYQLHH GDATCDVHGA
     RHDGETLSAR FNGEALRLPL HADAQRVLLH DANGHRHSFA RATAFAWESK QGSGGNQIIA
     PMPGRIVLVK AKPGDAVEEG QELLVMEAMK MELALKAPRA GTIETVSAAQ GDFVEADTVL
     VRFAQ
//
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