ID A0A0R0MHY0_9BURK Unreviewed; 667 AA.
AC A0A0R0MHY0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=3-methylcrotonyl-CoA carboxylase {ECO:0000313|EMBL:KRH98932.1};
GN ORFNames=AO057_05545 {ECO:0000313|EMBL:KRH98932.1};
OS Curvibacter sp. PAE-UM.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Curvibacter.
OX NCBI_TaxID=1714344 {ECO:0000313|EMBL:KRH98932.1, ECO:0000313|Proteomes:UP000051912};
RN [1] {ECO:0000313|EMBL:KRH98932.1, ECO:0000313|Proteomes:UP000051912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAE-UM {ECO:0000313|EMBL:KRH98932.1,
RC ECO:0000313|Proteomes:UP000051912};
RA Ma D.;
RT "The whole genome sequence of a typical ultramicrobacteria PAE-UM from
RT river sediment.";
RL Submitted (SEP-2015) 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:KRH98932.1}.
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; LKCX01000031; KRH98932.1; -; Genomic_DNA.
DR RefSeq; WP_057674684.1; NZ_KQ483358.1.
DR AlphaFoldDB; A0A0R0MHY0; -.
DR STRING; 1714344.AO057_05545; -.
DR OrthoDB; 9803706at2; -.
DR Proteomes; UP000051912; 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:UP000051912}.
FT DOMAIN 1..454
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..320
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 589..665
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 667 AA; 71894 MW; 86E9645DF7881E67 CRC64;
MFKKILIANR GEIACRVAAT ARRLGIQTVA VYSDADANAK HVAVCDEAVH IGGSAPAESY
LRWERIIEAA QATGAQAIHP GYGFLSENEA FAQACAKAGL VFIGPPAAAI QAMGLKAESK
RLMEKAGVPL VPGYHGADQD TRLLQHEADR IGYPVLIKAS AGGGGKGMRV VEKREDFESS
LASCQREAIN SFGDAAVLIE KYVLRPRHIE IQVFGDTQGN CVYLFERDCS VQRRHQKVLE
EAPAPGMTPE LRQQMGQAAV AAARAVNYVG AGTVEFIVEQ REGRMSFFFM EMNTRLQVEH
PVTEAITGLD LVEWQLRVAA GQPLPLKQEQ IKIQGHAIEA RICAENPDRH FLPATGMLQV
YALPACSTFE RADVRVDSGV REGDAISPFY DSMVAKLIVH GDTREQALAR LDAALAATRI
VGLQTNVQFL RHVVGSRSFA QADLDTALIV REAAVLFEQE KVGLPLAAAA VVAHTLLQEQ
GTAPSVGWVD PWARRDGWRS HGLTQRYFDL AFHGEQHTAV LTYLHDGALQ LRVEEAGATL
QFKRHGDDIV LHYAGLRVLA QVLRSGEVAH VFMPQGATQI TVLDALAHAG EAQAEGGRLT
APMPGKVVSF AVKAGDTVSK GQVLAVMEAM KMEHTIAAPA AGVVAELLYA PGDQVGEGAE
LLKLSAM
//
