ID A0A2N3Y0U0_SACSN Unreviewed; 452 AA.
AC A0A2N3Y0U0;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Acetyl-CoA carboxylase biotin carboxylase subunit {ECO:0000313|EMBL:PKW16520.1};
GN ORFNames=A8926_4360 {ECO:0000313|EMBL:PKW16520.1};
OS Saccharopolyspora spinosa.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharopolyspora.
OX NCBI_TaxID=60894 {ECO:0000313|EMBL:PKW16520.1, ECO:0000313|Proteomes:UP000233786};
RN [1] {ECO:0000313|EMBL:PKW16520.1, ECO:0000313|Proteomes:UP000233786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44228 {ECO:0000313|EMBL:PKW16520.1,
RC ECO:0000313|Proteomes:UP000233786};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 Actinobacteria strains.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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:PKW16520.1}.
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DR EMBL; PJNB01000001; PKW16520.1; -; Genomic_DNA.
DR RefSeq; WP_010314925.1; NZ_PJNB01000001.1.
DR AlphaFoldDB; A0A2N3Y0U0; -.
DR STRING; 994479.GCA_000194155_07307; -.
DR OrthoDB; 4435847at2; -.
DR Proteomes; UP000233786; 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 Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR PANTHER; PTHR48095:SF2; BIOTIN CARBOXYLASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR48095; PYRUVATE CARBOXYLASE SUBUNIT A; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 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 PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 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}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 1..446
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 119..317
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 452 AA; 48962 MW; F827AC49F19AF25C CRC64;
MRSLLIANRG EIAVRIVRAC FDEGIESVLA VSAADTDSLA ARLADRVVVI GPASAAESYL
SVNRVVAAAL YAGCDALHPG YGFLSERPEL VNACEENKIT YVGPPADIMR RSGSKLGARA
VAEKAGIPAG KGTPGLRDVE DAVRAAEALD NFPLLLKASA GGGGRGMTIV RDVADLREGF
ARSSTEAQRA FGDGTVYLEP YIEKARHVEV QILADTHGTV CHLGERDCST QRRYQKIIEE
APGAGLPEEL AEAVRTSAVE LCRALGYVGA GTVEFLVDAK THRYVFLEVN ARVQVEHPIT
EMVTGVDIVR EQLRIARGER LSFRQEDVRL DGHAIECRIN AEDPRTDFRP TPGRIDRWTV
PQGAGVRVDT YAHDGAVVAP WYDSLVAKVI VHAPDRPAAI DLMRRTLDRT RAEGISTTVD
VHRAILGDPA FAAGPVTTRW LEEQFLPSWL AD
//
