ID A0A221W9R1_9PSEU Unreviewed; 602 AA.
AC A0A221W9R1;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN Name=accC2 {ECO:0000313|EMBL:ASO22575.1};
GN ORFNames=AHOG_24850 {ECO:0000313|EMBL:ASO22575.1}, FHR81_004067
GN {ECO:0000313|EMBL:MBB5923000.1};
OS Actinoalloteichus hoggarensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinoalloteichus.
OX NCBI_TaxID=1470176 {ECO:0000313|EMBL:ASO22575.1, ECO:0000313|Proteomes:UP000204221};
RN [1] {ECO:0000313|EMBL:ASO22575.1, ECO:0000313|Proteomes:UP000204221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45943 {ECO:0000313|EMBL:ASO22575.1,
RC ECO:0000313|Proteomes:UP000204221};
RA Ruckert C., Nouioui I., Willmese J., van Wezel G., Klenk H.-P.,
RA Kalinowski J., Zotchev S.B.;
RT "Complete genome sequence of Actinoalloteichus hoggarensis DSM 45943, type
RT strain of Actinoalloteichus hoggarensis.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBB5923000.1, ECO:0000313|Proteomes:UP000541573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8639 {ECO:0000313|EMBL:MBB5923000.1,
RC ECO:0000313|Proteomes:UP000541573};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (AUG-2020) 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; CP022521; ASO22575.1; -; Genomic_DNA.
DR EMBL; JACHJM010000007; MBB5923000.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A221W9R1; -.
DR KEGG; ahg:AHOG_24850; -.
DR OrthoDB; 4435847at2; -.
DR Proteomes; UP000204221; Chromosome.
DR Proteomes; UP000541573; 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, ECO:0000313|EMBL:ASO22575.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000204221}.
FT DOMAIN 20..464
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 139..336
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 525..601
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 509..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 602 AA; 63449 MW; D8A8A56EC73C3092 CRC64;
MPDPVAEKTH KVSEQVRAQP LRKVLVANRG EIAVRVVRAC RDAGLASVAV YADSDRDAPF
VRLADEAFAL GGDTASTSYL DIDRIIDAAR RSGADAVHPG YGFLSENADF AQAVLDAGLT
WIGPSPAAIR DLGDKVTARH IAMRAGAPLA PGTKEPVSGP AEILAFTAEH GLPVAIKAAF
GGGGRGLKVA RTVEEIPEMF DSAVREAQSA FGRGECFVER YLDRPRHVEA QVLADQHGTV
IVVGTRDCSL QRRHQKLVEE APAPFLTDEQ RKTIHEAARA ICLEAGYHGA GTVEFLVGTD
GTISFLEVNT RLQVEHPVSE ETAGIDLVLE QFRIAAGERL PYDGDPAPRG HSIEFRVNGE
DAGRGFLPAP GTVTRFVPPA GPGVRVDAGV ESGSVVGGRF DSLLAKLIVT GSTREQALRR
ARRALDEFVV EGMATVLPFH RAVVTDPAFT AAAGFAVHTR WIETEFDNTI PPFTGPAGAE
DEEAERQTMV VEVGGRRLEV SLPAGHAVGA PTRQKAAPRK RGRGGTKAAV SGDAVTAPMQ
GTVVKLAVAD GAVVAAGDLL VVLEAMKMEN PVVAHKAGTV HGLSAVPGAT VAQGSQLCEI
KD
//
