ID D2NP12_ROTMD Unreviewed; 606 AA.
AC D2NP12;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 24-JAN-2024, entry version 75.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN OrderedLocusNames=RMDY18_15480 {ECO:0000313|EMBL:BAI65380.1};
OS Rothia mucilaginosa (strain DY-18) (Stomatococcus mucilaginosus).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Rothia.
OX NCBI_TaxID=680646 {ECO:0000313|EMBL:BAI65380.1, ECO:0000313|Proteomes:UP000001883};
RN [1] {ECO:0000313|Proteomes:UP000001883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY-18 {ECO:0000313|Proteomes:UP000001883};
RA Yamane K., Nambu T., Mashimo C., Sugimori C., Yamanaka T., Leung K.,
RA Fukushima H.;
RT "Complete genome sequence of Rothia mucilaginosa DJ.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAI65380.1, ECO:0000313|Proteomes:UP000001883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY-18 {ECO:0000313|EMBL:BAI65380.1,
RC ECO:0000313|Proteomes:UP000001883};
RA Yamane K., Yoshida M., Fujihira T., Baba T., Tsuji N., Hayashi H.,
RA Sugimori C., Yamanaka T., Mashimo C., Nambu T., Kawai H., Fukushima H.;
RT "Isolation and identification of Rothia mucilaginosa from persistent apical
RT periodontitis lesions.";
RL J Osaka Dent Univ 44:93-98(2010).
RN [3] {ECO:0000313|EMBL:BAI65380.1, ECO:0000313|Proteomes:UP000001883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY-18 {ECO:0000313|EMBL:BAI65380.1,
RC ECO:0000313|Proteomes:UP000001883};
RA Yamane K., Nambu T., Yamanaka T., Mashimo C., Sugimori C., Leung K.-P.,
RA Fukushima H.;
RT "Complete Genome Sequence of Rothia mucilaginosa DY-18: A Clinical Isolate
RT with Dense Meshwork-Like Structures from a Persistent Apical Periodontitis
RT Lesion.";
RL Sequencing 2010:457236-457236(2010).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; AP011540; BAI65380.1; -; Genomic_DNA.
DR RefSeq; WP_012903991.1; NC_013715.1.
DR AlphaFoldDB; D2NP12; -.
DR STRING; 680646.RMDY18_15480; -.
DR KEGG; rmu:RMDY18_15480; -.
DR eggNOG; COG4770; Bacteria.
DR HOGENOM; CLU_000395_3_1_11; -.
DR OMA; KGDAWSI; -.
DR Proteomes; UP000001883; 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 CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000001883}.
FT DOMAIN 22..465
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 141..338
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 530..606
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 504..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 606 AA; 64924 MW; 94711FEEC64DC318 CRC64;
MTQHQAEAAK KFTAVPGRHT GPVSKILIAN RGEIAVRVIR AARDEGLQTV AVYADPDRDS
LHVKLADEAY ALGGSTAAQS YLVMDKLIEV AIRSGADAVH PGYGFLSENA QFAQKCIDAG
LTWIGPSPQS ITRLGDKVAA RHIAQKVGAP LVPGTKDPVK SADEVVAFAD EHGLPIAVKA
AFGGGGRGIK VARDRESIVE MYESAVREAT AAFGRGECFI ERFLDSPRHV ETQCLADAHG
NVVVVSTRDC SLQRRNQKLV EEAPAPYLSE EQTKRLYEAS RAILREAGYQ GAGTCEFLVG
TDGTISFLEV NTRLQVEHPV SEEISGLDLV REQFRIARGE KIEEKDPVLR GHSFEFRING
EDPGRSFMPA PGTIEKLNVP TGPGVRWDSG FVAGDVIGGN FDSMLAKLIV TGADREQALQ
RARRALSELS IEGMPTVVPF HRVVLEDPAF VPAEGEDFKV HTRWIETEFN NTIPMYDGAP
GSVDSDEDER TTVVVEVNGK RMEVSLPEMG GAAKPAAKPA SKSRKSRSSR TSAKAGGDEL
TSPMQGTIVK VAVSDGDTVA EGDLVLVLEA MKMEQPITAH KAGKVSGLSA KPGDTVTSGA
VLATIK
//