ID A0A1G6V2D6_9ACTN Unreviewed; 604 AA.
AC A0A1G6V2D6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN ORFNames=SAMN05216270_104144 {ECO:0000313|EMBL:SDD47075.1};
OS Glycomyces harbinensis.
OC Bacteria; Actinomycetota; Actinomycetes; Glycomycetales; Glycomycetaceae;
OC Glycomyces.
OX NCBI_TaxID=58114 {ECO:0000313|EMBL:SDD47075.1, ECO:0000313|Proteomes:UP000198949};
RN [1] {ECO:0000313|EMBL:SDD47075.1, ECO:0000313|Proteomes:UP000198949}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.3516 {ECO:0000313|EMBL:SDD47075.1,
RC ECO:0000313|Proteomes:UP000198949};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; FNAD01000004; SDD47075.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6V2D6; -.
DR STRING; 58114.SAMN05216270_104144; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000198949; Unassembled WGS sequence.
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}.
FT DOMAIN 1..444
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 119..316
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 501..579
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 487..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 604 AA; 64271 MW; 8722536B4AA30859 CRC64;
MRKVLIANRG EIAVRVIRAC RDAGYESVAV YADGDRDAPH TLLADEAFAL DGLTAADTYL
RIDKLLKIAQ RSEADAVHPG YGFLSENADF AQAVIDAGLT WIGPTPQSIR DLGDKVTARH
LAMKADVPLV PGTKDPVKDA SEILAFADEH GLPVAIKAAF GGGGRGLKVA RERDEIPDLF
ESAVREAEAA FGRGECFVER YLDRPRHVEA QVLADTHGNV IVVGTRDCSL QRRHQKLVEE
APAPFLTDDQ RAVIHNAAKA ICKAADYHGA GTVEFLVAVD GTISFLEVNT RLQVEHPVSE
ETSGLDLVRE QFRIASGEAV PITEDPEPRG HSIEFRINGE DPGRGFLPAP GTVTKLRLPA
GPGVRVDTGI EEGSVIDGNF DSLLAKVIVT GATRDEALRR SRRALAEMEV EGLATVLPFH
RAVIEDPAFA EDFTVHTRWI ETEFDNTLEP YGAGAGGGAE AEERTSLVVE VGGKRLEVSI
PAGLLNPVAS SKPKKRGPKK KADAGPAIGG DSLPSPMQGT IVKVAVADGQ SVVKGDTIVV
LEAMKMEQPI EAHKSGTVSG LEVGIGDVVA AGAPICHISD LQAGPRREMM EVAVRSTTST
APAD
//