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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//