ID A0A495X3T2_9PSEU Unreviewed; 621 AA.
AC A0A495X3T2;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN ORFNames=DFJ66_2104 {ECO:0000313|EMBL:RKT68911.1};
OS Saccharothrix variisporea.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=543527 {ECO:0000313|EMBL:RKT68911.1, ECO:0000313|Proteomes:UP000272729};
RN [1] {ECO:0000313|EMBL:RKT68911.1, ECO:0000313|Proteomes:UP000272729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43911 {ECO:0000313|EMBL:RKT68911.1,
RC ECO:0000313|Proteomes:UP000272729};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
CC -!- SIMILARITY: Belongs to the asparaginase 1 family.
CC {ECO:0000256|ARBA:ARBA00010518}.
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:RKT68911.1}.
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DR EMBL; RBXR01000001; RKT68911.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A495X3T2; -.
DR OrthoDB; 4435847at2; -.
DR Proteomes; UP000272729; 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 GO; GO:0006520; P:amino acid metabolic process; 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; IPR020827; Asparaginase/glutaminase_AS1.
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; 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; PS00144; ASN_GLN_ASE_1; 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 3: Inferred from homology;
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:UP000272729}.
FT DOMAIN 1..431
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 107..306
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 547..619
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT ACT_SITE 597
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10099"
SQ SEQUENCE 621 AA; 66389 MW; 9004F850D6D29336 CRC64;
MISKLLIANR GEIARRVART CRAVGVSPVA VFSDPDADAP HVREADVAVR LPGAAPAETY
LRIDALVAAA KAAGADAVHP GYGFLSENAE FARAVQRAGL TWVGPDPEVI EAMGSKVAAK
KRMADAGVPV LPELDPETAT EFPLLVKASA GGGGRGMRVV RTREELAEAV AAARREAESA
FGDGTVFCEP LLENARHVEV QILADTHGTV WALGERECSI QRRHQKIIEE TPSPAVRSEA
RQRLFDAATK AAHAIGYVGA GTVEFLFTDD QEFHFLEVNT RLQVEHPVTE EVFGLDLVAW
QLAIAEGARL PAEPPTPHGH AIEARLYAED PAHDWRPASG TLHRFRVPDG VRVDSGVEDG
SVVGVHYDPM LAKVVAWGET RAAAVRKLAN ALDRAELHGL VTNRELLVRT LRHPAFAAGD
THTGFLAQHG LTKRPDVDVR PAALAAALAL AENRRTALPL GWRNVPSQPQ KVGFEFDGES
VEISYRHTRD GVICSPEVEV VRAAKDFVVL AQDGVQVTYP VAVYGDRVEV GGLSLRVLPR
FPEPTSRVAE GATVAPMPGT VVRVSVEAGQ HVEAGTELLV LEAMKMEHRV LAATGGTVAE
VLVQPGHQVD AGDVLAVVEG S
//
