ID F4CVG4_PSEUX Unreviewed; 465 AA.
AC F4CVG4;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Biotin carboxylase {ECO:0000313|EMBL:AEA23784.1};
DE EC=6.3.4.14 {ECO:0000313|EMBL:AEA23784.1};
GN OrderedLocusNames=Psed_1546 {ECO:0000313|EMBL:AEA23784.1};
OS Pseudonocardia dioxanivorans (strain ATCC 55486 / DSM 44775 / JCM 13855 /
OS CB1190).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=675635 {ECO:0000313|EMBL:AEA23784.1, ECO:0000313|Proteomes:UP000007809};
RN [1] {ECO:0000313|EMBL:AEA23784.1, ECO:0000313|Proteomes:UP000007809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55486 / DSM 44775 / JCM 13855 / CB1190
RC {ECO:0000313|Proteomes:UP000007809};
RX PubMed=21725009; DOI=10.1128/JB.00415-11;
RA Sales C.M., Mahendra S., Grostern A., Parales R.E., Goodwin L.A., Woyke T.,
RA Nolan M., Lapidus A., Chertkov O., Ovchinnikova G., Sczyrba A.,
RA Alvarez-Cohen L.;
RT "Genome sequence of the 1,4-dioxane-degrading Pseudonocardia dioxanivorans
RT strain CB1190.";
RL J. Bacteriol. 193:4549-4550(2011).
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DR EMBL; CP002593; AEA23784.1; -; Genomic_DNA.
DR AlphaFoldDB; F4CVG4; -.
DR STRING; 675635.Psed_1546; -.
DR KEGG; pdx:Psed_1546; -.
DR eggNOG; COG0439; Bacteria.
DR HOGENOM; CLU_000395_3_2_11; -.
DR Proteomes; UP000007809; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR PANTHER; PTHR48095:SF2; BIOTIN CARBOXYLASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR48095; PYRUVATE CARBOXYLASE SUBUNIT A; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 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 PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 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};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AEA23784.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000007809}.
FT DOMAIN 1..446
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..317
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 465 AA; 50092 MW; 4EA4F3882646BFC8 CRC64;
MVQRVLVANR GEIAMRVVRA CFDEGVTSVL AASEADLDSL PARVADEVVQ IGPASATASY
LDVGAVISAA LLTGCDAVHP GYGFLSEQPE LVEQCARHGI TFVGPSAESI RRGGDKIAAR
ELARGLDIPL GAGSDAIDTV EEAADLAARV GYPVLLKAAA GGGGRGMRRV DAPAQLADAV
VRARAEAQSA FGDGRLYIEH YVEHARHVEV QVLADALGTT VHLGDRDCSY QRRYQKLVEE
APASAVPEEL RRRIGEAAVA LISALDYVGA GTVEFLVDVD RDTFSFLEVN TRVQVEHPVT
EMVTGVDIVR EQLRIAAGKP LSFAQGDVRV SGHAIEFRIN AESPDRGFVP SPGELRVWRP
PVGTDVRVDS HCFAGYRVPP HYDSLLGKLI CRGDTRDEAL DLAARALDAF DVAGVDTTLP
LHRELVRHPD VRGHRITTRW VEESFLPLWT ADRARTARAE RAATP
//
