ID A0A512DG49_9CELL Unreviewed; 1226 AA.
AC A0A512DG49;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 13-SEP-2023, entry version 16.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN ORFNames=CAE01nite_31990 {ECO:0000313|EMBL:GEO35474.1};
OS Cellulomonas aerilata.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=515326 {ECO:0000313|EMBL:GEO35474.1, ECO:0000313|Proteomes:UP000321181};
RN [1] {ECO:0000313|EMBL:GEO35474.1, ECO:0000313|Proteomes:UP000321181}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 106308 {ECO:0000313|EMBL:GEO35474.1,
RC ECO:0000313|Proteomes:UP000321181};
RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT "Whole genome shotgun sequence of Cellulomonas aerilata NBRC 106308.";
RL Submitted (JUL-2019) 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:GEO35474.1}.
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DR EMBL; BJYY01000020; GEO35474.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A512DG49; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000321181; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; 3.30.1360.40; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 2.
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; IPR003778; CT_A_B.
DR InterPro; IPR003833; CT_C_D.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR InterPro; IPR014084; Urea_COase.
DR NCBIfam; TIGR00724; urea_amlyse_rel; 1.
DR NCBIfam; TIGR02712; urea_carbox; 1.
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 Pfam; PF02626; CT_A_B; 1.
DR Pfam; PF02682; CT_C_D; 1.
DR SMART; SM00796; AHS1; 1.
DR SMART; SM00797; AHS2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF50891; Cyclophilin-like; 2.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF160467; PH0987 N-terminal 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000321181}.
FT DOMAIN 2..467
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 121..318
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1143..1221
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 343..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1226 AA; 128073 MW; 9C85DAC4D5392BDF CRC64;
MSFDTLLVAN RGEIAVRILR TARAMGLRTV AVHSAADAGA PHTRLADTSV LLGPAPAAQS
YLLGDRIVEA ALASGAGAIH PGYGFLSENA GFARAAEAAG VAFVGPSPEH LELFGSKHTA
RDAARAVGVP MLAGTGLLET LDEALVAADA IGYPVMLKAT AGGGGIGMRA CRSAAELSAA
WESVRRTAGA SFGTAGVFLE RLITAARHVE VQVFGDGAGT VVTLGDRDCS LQRRHQKVCE
EAPAPGLPDA VRTGIADAAR DLCASVAYRS AGTVEYVYDA EREEAAFLEV NTRLQVEHPV
TEAVYRVDLV EWMLRLAQGD TSVVDTPLEP RGHAVEARVY AENPDRDHLP SAGTVTGFAS
PATGVSTGST SGGPAGSPAG GSTGTAARVD TWIEAGTEVT THYDPLLAKV ITAGADRDAA
WAALGDALAG TRVDGIATNL GLLRSITTTA DVLAATHHTG TLAGVVDGDP RVEVVRPGML
TTVQDWPGRT GLWHVGIPPS GPMDDLSFRL GNRALGNDEG APGLECTLAG PALRFRTAAT
VLVAGAPTPV TVDGDPVPQW QPVHVPAGSV LDIGTPTAGM RSYLLVRGGL DVTPVLGSAA
TFDLGRIGGV TGSALRAGDT LRLPAAAAEG DPIAPGAGVP VADRPTITDA WEIGALEGPH
AAPEFFTPGD VEEFYAATWS VHFNSARTGV RLVGPKPTWA RPDGGEAGLH PSNIHDTPYA
VGAVDYTGDL PILLGPDGPS LGGFTCPATV AVGQMWKLGQ LRPGDAVRFV PVDEAQAGTL
RARPQSRPVA SRPAHDDGGI LARLEAQAHR PEVTMRRSGD DNLLVEYGPM QLDLASRMRV
HALAEAVRER LAADGGRAAR GLVDLTPGIR SLQLHLDPDV LPLRTALDLV RQVEDTLPAT
SELVVPSRTV HLPLSWDDPA TREAIERYMA GVRDDAPWCP WNIEFIRRIN GLGSVDDVYR
TVFDADYLVM GLGDVYLGAP VATPLDPRHR LVTTKYNPAR TWTPENAVGI GGAYLCIYGM
EGPGGYQFVG RTVPVWSTHT QRGAFEPGTP WLLRFFDVIK WHPVGADELL DLRADAKAGQ
LDLRIDQGTF ALADHERFLA DNAGSIEAFR AAQAAAFGTE RDAWEAAGEF DRRAEAEPPA
SSGDGVVVPE GSEGVGAPFV GTVFRIDVRP GDVVTAGQTL LALEAMKMEA PVVASVSGTV
TAVSVTPGDQ VSPGQVLVVV EQRAAA
//
