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Database: UniProt
Entry: E0Q8W4_9BIFI
LinkDB: E0Q8W4_9BIFI
Original site: E0Q8W4_9BIFI 
ID   E0Q8W4_9BIFI            Unreviewed;       647 AA.
AC   E0Q8W4;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE            EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN   Name=accA {ECO:0000313|EMBL:EFM41256.1};
GN   ORFNames=HMPREF0168_1572 {ECO:0000313|EMBL:EFM41256.1};
OS   Bifidobacterium dentium ATCC 27679.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=871562 {ECO:0000313|EMBL:EFM41256.1, ECO:0000313|Proteomes:UP000003323};
RN   [1] {ECO:0000313|EMBL:EFM41256.1, ECO:0000313|Proteomes:UP000003323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27679 {ECO:0000313|EMBL:EFM41256.1,
RC   ECO:0000313|Proteomes:UP000003323};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EFM41256.1}.
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DR   EMBL; AEEQ01000010; EFM41256.1; -; Genomic_DNA.
DR   AlphaFoldDB; E0Q8W4; -.
DR   HOGENOM; CLU_000395_3_1_11; -.
DR   Proteomes; UP000003323; 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};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EFM41256.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}.
FT   DOMAIN          31..471
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          150..345
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          557..632
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   647 AA;  70615 MW;  C935DD2FD4D6ED3D CRC64;
     MEPYKKTASL LWKTSVRAAA KASNVDNMPK NVNTLLVANR GEIALRVVRT AREMGIPTVA
     VYAEQDRHAQ YVQMADDAYL LSGDTYKDTY LNEDLLIDIL HRSGADAVHP GYGFLSEVAS
     FAQKVIDAGA TWVGPNPKAL VDLGDKITAR RVATFAKVPP VPGISHSISD MRLLLDFAHT
     HGYPLMLKRT DGGGGRGITL VRNDDELRGF YMNHDALQGG DLNEYFVERF IDKGRHVETQ
     CGRDTHGNFT VYSTRDCSVQ RRNQKLVEEA PAPFLPDTVM EQLARYSRNL FEAVGYVGLG
     TCEFMVTEQG KVYFLEVNPR LQVEHTVSEE VCGLDLVREQ LTIANDGELT VEHPIRGHSF
     ELRLTCEDPA KNLTPSSGTL TALRWPSGPG IRVDSGVLEG DTISPKFDSM MGKLVVTASD
     RANAVARVRR ALEELNIEGV PTPVSLFERI FNDDEFTAEH GAAYDVSTKW LERKYLNKEA
     ASSHGGQPAS LSGAADEGKD IESSETFVIE VNNHRVSLTV PTDIVANLTG SAKARDAKRA
     IQPLRGQGLH HVKRGPQASE GQSGIIASPM QAVVTRINVA EGQEVAKGDL LVVLESMKME
     NYVYAPVKGT VTKIFVGPAN GVEAGETLLT INVAGATPES KDEEAEQ
//
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