ID A0A161VRN9_9NOCA Unreviewed; 664 AA.
AC A0A161VRN9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN ORFNames=A2J03_24635 {ECO:0000313|EMBL:KZF06563.1};
OS Rhodococcus sp. EPR-157.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1813677 {ECO:0000313|EMBL:KZF06563.1, ECO:0000313|Proteomes:UP000077673};
RN [1] {ECO:0000313|EMBL:KZF06563.1, ECO:0000313|Proteomes:UP000077673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPR-157 {ECO:0000313|EMBL:KZF06563.1,
RC ECO:0000313|Proteomes:UP000077673};
RA Ploux O.;
RL Submitted (MAR-2016) 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:KZF06563.1}.
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DR EMBL; LVCV01000300; KZF06563.1; -; Genomic_DNA.
DR RefSeq; WP_068374823.1; NZ_LVCV01000300.1.
DR AlphaFoldDB; A0A161VRN9; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000077673; 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; 3.30.700.40; -; 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; 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; 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 Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000077673}.
FT DOMAIN 4..451
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 123..322
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 578..656
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 664 AA; 70340 MW; 58DC06362F5F102D CRC64;
MNKQIDTVLI ANRGEIAVRV ARTLRRMGIR SVAVYSDADA GARHVAEADT AIRLGPANAR
DSYLSIPKVI EAAQRTGAQA IHPGYGFLSE NADFAAACAA ADIAFLGPPA RAIEVMGDKI
AAKAAVSEFG VPVVPGISRP GLTDADLIAG AEDVGFPVLV KPSAGGGGKG MRLVERTEDL
PAALASARRE AASSFGDDTI FLERFVLRPR HIEVQILADE HGNVIHLGER ECSLQRRHQK
VIEEAPSPLL DEATRARIGA AACNTARSVD YAGAGTVEFI VSADNPDEFF FMEMNTRLQV
EHPVTELVTG LDLVEWQVRV AAGEALTIAQ DDITLTGHAI EARVYAEDPG RGFLPTGGTV
VGLREPVGDG IRVDSGLAVG TEVGSNYDPM LSKVIAYGPD RSSALRTLDR ALSQTAVLGV
VTNIEFARFL LADNDVRAGR LDTGLLDRRV EDFTASAATD EALIAAAAVE WTQTWQNAGN
DIWAMPSGWR VGAQAPFVRR LTSGDRSVHV AIVGTPDAAT VAIDDHPAST LHAHTTADTI
TVVVDGRRET MTFARSDSAT WISSAQGTWQ LRTVAEPSVR DDDAHSGDAE ILSPMPGSVI
AVGTSTGELI TAGTAVVVVE AMKMEHTLTT PIDGTVELVV AVGDQVRVDQ LLARIVPKED
KDQS
//
