ID A0A096AM17_9BURK Unreviewed; 678 AA.
AC A0A096AM17;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=3-methylcrotonyl-CoA carboxylase {ECO:0000313|EMBL:KGF31702.1};
GN ORFNames=HMPREF2130_02900 {ECO:0000313|EMBL:KGF31702.1};
OS Oligella urethralis DNF00040.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Oligella.
OX NCBI_TaxID=1401065 {ECO:0000313|EMBL:KGF31702.1, ECO:0000313|Proteomes:UP000029629};
RN [1] {ECO:0000313|EMBL:KGF31702.1, ECO:0000313|Proteomes:UP000029629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DNF00040 {ECO:0000313|EMBL:KGF31702.1,
RC ECO:0000313|Proteomes:UP000029629};
RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JUL-2014) 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:KGF31702.1}.
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DR EMBL; JRNI01000011; KGF31702.1; -; Genomic_DNA.
DR RefSeq; WP_036557902.1; NZ_JRNI01000011.1.
DR AlphaFoldDB; A0A096AM17; -.
DR eggNOG; COG4770; Bacteria.
DR OrthoDB; 9803706at2; -.
DR Proteomes; UP000029629; 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 GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.700.40; -; 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}; Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000029629}.
FT DOMAIN 1..451
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 597..675
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 678 AA; 73837 MW; 5E421F77FDAA4658 CRC64;
MFKKILIANR GEIACRVART ARAMGIATVA VYSDADRHAA HVQACDEAVY IGGSEPANSY
LRIDAIIEAA KQTGAEAIHP GYGFLAENGH FVEACNQAGI KFIGPSAAAM EAMGSKSAAK
ALMEKAGVPL VPGYHGDNQD PAFLHAQADA ISYPVLIKAS AGGGGKGMRI VNSSDEFISM
LESCQREARS SFSNDHVLIE RYVNKPRHIE IQIFGDEHGN YVYLFERDCS VQRRHQKVIE
EAPAPGMTEE RRRAMGEAAV NAARAVNYVG AGTVEFIAEQ DGTFYFMEMN TRLQVEHPVT
EMITGYDLVE WQLRIANNEA IPVQQADLAI QGHAIEVRIY AENPDNDFLP SIGQLNHLSF
PPHQSFVNAP VRVDSGIREG DSISPFYDPM IAKLIVWGDD REQAIARMRQ ALLATHIIGL
HTNVDFLYRL MCNDAFVNAD LDTGLIEKNQ ASLFPPARPT SSKALATAAV AYLAKHGLKH
SRAAKNTATR YVDPWAAADY WRVRQGDGTS ITINDGHQDY VLQLQQTAKD QWTLMIDGTA
QRLEWEASTL DSATQFDIKL GLDGVLSHAK AVFDGEDLYL YAQEGQLRLQ LPDSLAHAAD
GAEVGGGGLT APMPGKVINI LVKVGDEVKA GDVLLVMEAM KMEHSITADE GGVVEELFFD
VGEQVTEGAE LIKLSTAD
//
