ID A0A448I0E4_MYCCI Unreviewed; 657 AA.
AC A0A448I0E4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Acetyl-/propionyl-coenzyme A carboxylase alpha chain, AccA2 {ECO:0000313|EMBL:VEG45958.1};
GN Name=accA2 {ECO:0000313|EMBL:VEG45958.1};
GN ORFNames=NCTC10485_00854 {ECO:0000313|EMBL:VEG45958.1};
OS Mycolicibacterium chitae (Mycobacterium chitae).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1792 {ECO:0000313|EMBL:VEG45958.1, ECO:0000313|Proteomes:UP000282551};
RN [1] {ECO:0000313|EMBL:VEG45958.1, ECO:0000313|Proteomes:UP000282551}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10485 {ECO:0000313|EMBL:VEG45958.1,
RC ECO:0000313|Proteomes:UP000282551};
RG Pathogen Informatics;
RL Submitted (DEC-2018) 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; LR134355; VEG45958.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A448I0E4; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000282551; Chromosome 1.
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; 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:SF126; BIOTIN CARBOXYLASE; 1.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 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:UP000282551}.
FT DOMAIN 1..440
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 109..304
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 572..647
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 657 AA; 69240 MW; 83922CE80FB57261 CRC64;
MITKVLVANR GEISRRVFAT CRRLGIGTVA VYTDPDAEAP HVTDADTRVR VDSYLDAEAL
VAATRAAGAD AVHPGYGFLS ENAAFAEAVT AAGLVWIGPP AAAIAAMGSK VEAKKTMAAA
GVPILDELDP AGLTAEQLPV LVKASAGGGG RGMRVVSDLA ALPDAVASAR REAESAFGDP
TVFCERYLPT GHHVEVQILA DHHGTVWAVG ERECSIQRRH QKIIEEAPSP LVERVAGMRG
RLFDAARLAA EAIGYTGAGT VEFLADGHGE FYFLEMNTRL QVEHPVTEAT TGLDLVELQL
RVAEGDRLPP EPPAAQGYSI EARLYAEDPA KNWQPQAGTV RHFAVPTARS EFESSGRPEI
RLDSGVVDRT TVSIHYDPML AKIISFAPTR RRAAAMLADA LVRTRLHGLR TNRDLLVNVL
GHPAFLAGDT DTAFFDTHGL AALAAPRVGA AGLRLSAVAA AVADAEHNRA AAPVALGAPI
GWRNVPSANQ SKTYRDGAGD EHRVAYRFGR TGLILPDDDG LRLVSSAPAR VVLADPSGVE
TAYEISRYGD TVCVDSPRGG VEFTVVPRFV EPGTAVAEGS LVAPMPGVVT RTGAEVGQAV
TAGQPLVWLE AMKMEHTLAA PGDGILTELH VTAGQQVEMG AVLALVADPT TEEESSR
//
