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Database: UniProt
Entry: Q124J3_POLSJ
LinkDB: Q124J3_POLSJ
Original site: Q124J3_POLSJ 
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
//
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