ID A0A1C4GZ81_9BIFI Unreviewed; 644 AA.
AC A0A1C4GZ81;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN ORFNames=GA0061077_0015 {ECO:0000313|EMBL:SCC77945.1};
OS Bifidobacterium commune.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1505727 {ECO:0000313|EMBL:SCC77945.1, ECO:0000313|Proteomes:UP000242610};
RN [1] {ECO:0000313|Proteomes:UP000242610}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R-52791 {ECO:0000313|Proteomes:UP000242610};
RA Varghese N., Submissions Spin;
RL Submitted (AUG-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; FMBL01000001; SCC77945.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C4GZ81; -.
DR STRING; 1505727.GA0061077_0015; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000242610; 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; 3.30.470.20; 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; 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; 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}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000242610}.
FT DOMAIN 4..443
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 122..317
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 527..602
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 501..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..644
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 644 AA; 70887 MW; 47F57E9D318EF91B CRC64;
MVNNVNKLLV ANRGEIALRV IRTAHEMGIA TVAIYAEQDR DAQYVQMADE AYLLHGDSYR
SYMDEDLIID VLRRSGADAV HPGYGYLSEI ASFADKVMKA GATWIGPSPT ALTDLGDKIT
ARRVAKRAHV PPVPGISEPV SNMRELLTFA QINGYPVMMK RTDGGGGKGI TLIHDDDELR
SFYMNHDALE GGDLDEYFVE VFIDKARHVE TQSGRDSHGN FTVYSTRDCT VQRRNQKLIE
EAPAPFLTDD EREQLERYSR NLFSAVDYIG LGTCEFMVTE QHKVYFLEVN PRLQVEHTVS
EQVCGLDLVR EQINIARGDE LTKAPQSHGH AFELRITSED PEKNLTPSGG TLIRLDWPSG
PGIRIDSGVK IGDVVSPKFD SMMGKLVVTA QDRPTAVARV RRALKEFNLE GVPTPKSLFE
TVFNDQEFTA EDHPYSVYTK WLEHKYLNRK PNAAGSGQPA SMSGSDEQIR KQETDSFVIE
VDGKRVKLTV PRDIVDNFTG SARARGVRRP TQPLRGSSSG AVQERTKGND GKSGVIDSPM
QAIVTRVNVA EGQEVSKGDL LAVLESMKME NYVYTPVNGT VCKILVGPSD SVDAGTTLMN
IDVEGASNRE KSGANNVDGS EKKSHDGDSQ TASLADEADE KGRG
//
