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Database: UniProt
Entry: A0A2A4W2F7_9PROT
LinkDB: A0A2A4W2F7_9PROT
Original site: A0A2A4W2F7_9PROT 
ID   A0A2A4W2F7_9PROT        Unreviewed;       659 AA.
AC   A0A2A4W2F7;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   03-MAY-2023, entry version 13.
DE   SubName: Full=3-methylcrotonyl-CoA carboxylase {ECO:0000313|EMBL:PCI64530.1};
GN   ORFNames=COB37_01465 {ECO:0000313|EMBL:PCI64530.1};
OS   Kordiimonadales bacterium.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Kordiimonadales.
OX   NCBI_TaxID=2030814 {ECO:0000313|EMBL:PCI64530.1, ECO:0000313|Proteomes:UP000217879};
RN   [1] {ECO:0000313|Proteomes:UP000217879}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT   "A dynamic microbial community with high functional redundancy inhabits the
RT   cold, oxic subseafloor aquifer.";
RL   Submitted (AUG-2017) 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:PCI64530.1}.
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DR   EMBL; NVTU01000003; PCI64530.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A4W2F7; -.
DR   Proteomes; UP000217879; 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   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}.
FT   DOMAIN          3..448
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          122..319
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          574..651
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   659 AA;  70949 MW;  68A6CBA206B6CD88 CRC64;
     MTEFRKILIA SRGEIALRVM RTAQRLGYRT VAVYSDTDAQ ALHVSAADEA FALGGTTLQE
     SYLVIEKILE AAKATGADAI HPCYGFLSEN ADFARACADA GVVFIGPSAD AIELMGDKAR
     AKDAMLAAGV PCIPGYQGLD QNEDALQREA AAIGYPLMVK AAAGGGGRGI RLVSRPEDFS
     AALSSARSEA ENAFGNGDLI LEKAILQPRH IEFQVFADQH GNIIHLGERD CSIQRRHQKI
     VEEAPSPFLD EHLRAEMGAV AVEAAKACDY QGAGTVEFLV DADKNFYFLE MNTRLQVEHP
     VTEMITGLDL VEWQLIVAAG GKLPLKQDEV ELKGCAVEVR LYAEDPRNGF MPQTGEVLYW
     NSPEREGVRT DHAVAAGQSV SVYFDPMLAK LIAHGASRAE ALRRLSSLIQ DTKLLGINNN
     LCFLRNVLNH EVFRRGGANT GFLEDHFSGD VSLQSVNPGA ETLARAALCF YLQGHFEGQR
     KPSWRSSAAY EAHFKLHDGD ASHDVALIGQ NGTFTAKFSD SSVSIELAGN EANECTAIIG
     GVRSAFAVAV DGTELFLDDG TGHYHFRDIT HLPAETAKGT GSGLVKAPMD GAIVDIKVAE
     GDKVEAGQAL IIMEAMKMQH SLKAAVSGEV RKLNLEIGQQ VKGQQILVVI DLATEEEAS
//
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