ID A0A2L0EQ14_SORCE Unreviewed; 499 AA.
AC A0A2L0EQ14;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Biotin carboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=SOCE26_028090 {ECO:0000313|EMBL:AUX41397.1};
OS Sorangium cellulosum (Polyangium cellulosum).
OC Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae; Sorangium.
OX NCBI_TaxID=56 {ECO:0000313|EMBL:AUX41397.1, ECO:0000313|Proteomes:UP000238348};
RN [1] {ECO:0000313|EMBL:AUX41397.1, ECO:0000313|Proteomes:UP000238348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=So ce26 {ECO:0000313|EMBL:AUX41397.1,
RC ECO:0000313|Proteomes:UP000238348};
RA Zaburannyi N., Bunk B., Overmann J., Mueller R.;
RT "Sorangium comparison.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP012673; AUX41397.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2L0EQ14; -.
DR OrthoDB; 9769961at2; -.
DR Proteomes; UP000238348; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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; 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; 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..444
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..315
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 499 AA; 53592 MW; BCF6D0454AE94135 CRC64;
MIRKVLIANR GEIAVRILRS LHEAGIQGVA VYSDVDRGSL HVRLADESYP IGPAPAAESY
LRIDRILDVA RRSGADAIHP GYGFLSENRE FAEACERAGI TFIGPPSSAM AAMGSKPAAR
AKMAAAGVPI VPGGEPASVA EAQALAARLG YPVMLKAAFG GGGKGMRLVH RPEDLLAAYE
RAQSEAARAF GNATVYLEKA ILRPRHVEIQ VLGDREGNLV HLFERDCSIQ RRHQKVVEEA
PCPVATPELV QRMGEVAVRG ALAVGYHSAG TFEFLLAEDG AFYFLEMNTR LQVEHPITEW
TTGVDLVAEM VKIAGGERLS LQQHAISRRG ASIECRIYAE DPSSGFLPSP GTLATLRPPA
GPWVRDDSGF YEGAVVPSHY DPLISKLSVW APDRRAAIAR MRRALAEYAV TGIRTNLSFH
ENLLAHPDFQ AGRYDTGFIA EHTAALCGPT AVAAEEETTL AAALAVAAAQ AERRPASGGA
PEPGAPRLSP WVIQHRAFR
//
