ID Q124J3_POLSJ Unreviewed; 663 AA.
AC Q124J3;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 24-JAN-2024, entry version 100.
DE SubName: Full=3-methylcrotonoyl-CoA carboxylase, alpha subunit {ECO:0000313|EMBL:ABE46049.1};
DE EC=6.4.1.4 {ECO:0000313|EMBL:ABE46049.1};
GN OrderedLocusNames=Bpro_4157 {ECO:0000313|EMBL:ABE46049.1};
OS Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=296591 {ECO:0000313|EMBL:ABE46049.1, ECO:0000313|Proteomes:UP000001983};
RN [1] {ECO:0000313|Proteomes:UP000001983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS666 / ATCC BAA-500 {ECO:0000313|Proteomes:UP000001983};
RX PubMed=18723656; DOI=10.1128/AEM.00197-08;
RA Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA Stothard P., Coleman N.V.;
RT "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT relevance to biotechnology.";
RL Appl. Environ. Microbiol. 74:6405-6416(2008).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; CP000316; ABE46049.1; -; Genomic_DNA.
DR RefSeq; WP_011485038.1; NC_007948.1.
DR AlphaFoldDB; Q124J3; -.
DR STRING; 296591.Bpro_4157; -.
DR KEGG; pol:Bpro_4157; -.
DR eggNOG; COG4770; Bacteria.
DR HOGENOM; CLU_000395_3_1_4; -.
DR OMA; LVKWQLM; -.
DR OrthoDB; 9803706at2; -.
DR Proteomes; UP000001983; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004485; F:methylcrotonoyl-CoA carboxylase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:ABE46049.1};
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:UP000001983}.
FT DOMAIN 1..455
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..321
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 585..662
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 663 AA; 71519 MW; DBB5C5B2E74F05BF CRC64;
MFKKILIANR GEIACRVAAT ARRMAIKTVA VYSDADANAK HVGVCDEAIH IGGSAPKDSY
LRWERIIEAA KATGAQAIHP GYGFLSENEE FAQACARAGL VFIGPPASAI KAMGLKAESK
QLMEKAGVPL VPGYHGSDQD PVMLKHEADR IGYPVLIKAS AGGGGKGMRA VDKAEDFDAA
LASCKREAIN SFGDDAVLVE KYAQRPRHIE IQVFGDTHGN YVYLFERDCS VQRRHQKVLE
EAPAPGMTPE MRQQMGLAAV AAARAVNYVG AGTVEFIVEQ RADGSMNFFF MEMNTRLQVE
HPVTEAITGL DLVEWQLRVA SGEKLPLAQE QLRINGHAIE ARICAENPDN NFLPATGTLH
VYQKPNCSSF ERGPVRVDDG VREGDAISPF YDSMVAKLIV HGQTREEALA RLDEALAQTH
IVGLNTNMQF LRYVLRSPSF AQANLDTALI PREEAVLFKQ EPVGLAMAAA CAIAQTLLQE
KASEDSDPFS RRDGWQTHGV TQRPFEFDFR GEHSKAALTY LHDGALQLKV GNVSGPLVFA
GSAQGIDIQF AGQRLTAAVY TQGEVDYVFT ARGATQITAI DLLAHAGESH TEGGRLTAPM
PGKVVSFGVK AGDKVSKGQA LAVMEAMKME HTIAAPADGV VQELLYAPGD QVAEGAELLK
IAV
//