ID A1UCG0_MYCSK Unreviewed; 602 AA.
AC A1UCG0;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN OrderedLocusNames=Mkms_1306 {ECO:0000313|EMBL:ABL90518.1};
OS Mycobacterium sp. (strain KMS).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=189918 {ECO:0000313|EMBL:ABL90518.1};
RN [1] {ECO:0000313|EMBL:ABL90518.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KMS {ECO:0000313|EMBL:ABL90518.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D.,
RA Richardson P.;
RT "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] =
CC ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate;
CC Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145,
CC ChEBI:CHEBI:456216; EC=6.3.4.14;
CC Evidence={ECO:0000256|ARBA:ARBA00024172};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13502;
CC Evidence={ECO:0000256|ARBA:ARBA00024172};
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; CP000518; ABL90518.1; -; Genomic_DNA.
DR AlphaFoldDB; A1UCG0; -.
DR STRING; 189918.Mkms_1306; -.
DR KEGG; mkm:Mkms_1306; -.
DR HOGENOM; CLU_000395_3_1_11; -.
DR OrthoDB; 9760256at2; -.
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; 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}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ABL90518.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 8..452
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 127..324
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 525..598
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 511..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 602 AA; 63670 MW; 1754B62AECE5149E CRC64;
MASHASSKIS KVLVANRGEI AVRVIRAAKD AGLQSVAVYA EPDADAPHVR LADEAFALGG
QTSAESYLVF EKLLDAAEKS GANAIHPGYG FLSENADFAQ AVIDAGLIWI GPSPQSIRDL
GDKVTARHIA ARAQAPLVPG TPDPVKDADE VVAFAEEYGV PVAIKAAFGG GGRGMKVART
IQEIPELFDS ATREAVAAFG RGECFVERYL DKPRHVEAQV IADQHGNVVV AGTRDCSLQR
RFQKLVEEAP APFLTDAQRK EIHESAKRIC KEAGYYGAGT VEYLVGQDGL ISFLEVNTRL
QVEHPVTEET SGIDLVRQQF RIANGEPLDI TEDPTPRGHS IEFRINGEDA GRGFLPAPGP
VTTFEPPTGP GVRLDSGVES GSVIGGQFDS MLAKLIVTGA TREEALERSR RALAEFKVEG
LATVIPFHRA VVSDPAFIGD ENGFTVHTRW IETEWDNTIE PFTGGDPIDE EDTAPRQTVV
VEVGGRRLEV SLPGDLVLGN GGGAAPAGVI RKKPKPRKRG AHGGAATSGD SVTAPMQGTV
VKVAVEEGQQ VSAGDLVVVL EAMKMENPVT AHKDGTITGL AVEAGAAVTQ GTVLAEIKSD
GE
//
