ID A0A196LDC0_9MICO Unreviewed; 636 AA.
AC A0A196LDC0;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-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=A4X16_01710 {ECO:0000313|EMBL:OAN40881.1};
OS Microbacterium sp. H83.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1827324 {ECO:0000313|EMBL:OAN40881.1, ECO:0000313|Proteomes:UP000078289};
RN [1] {ECO:0000313|EMBL:OAN40881.1, ECO:0000313|Proteomes:UP000078289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H83 {ECO:0000313|EMBL:OAN40881.1,
RC ECO:0000313|Proteomes:UP000078289};
RA Lymperopoulou D., Adams R.I., Lindow S., Coil D.A., Jospin G., Eisen J.A.;
RT "Draft Genome Sequences of Staphylococcus capitis Strain H36, S. capitis
RT Strain H65, S. cohnii Strain H62, S. hominis Strain H69, Mycobacterium
RT iranicum Strain H39, Plantibacter sp. Strain H53, Pseudomonas oryzihabitans
RT Strain H72, and Microbacterium sp. Strain H83, isolated from residential
RT settings.";
RL Submitted (APR-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:OAN40881.1}.
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DR EMBL; LWCU01000012; OAN40881.1; -; Genomic_DNA.
DR RefSeq; WP_067118017.1; NZ_LWCU01000012.1.
DR AlphaFoldDB; A0A196LDC0; -.
DR STRING; 1827324.A4X16_01710; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000078289; 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; 3.30.470.20; 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; 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}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 6..448
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 125..324
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 557..631
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 636 AA; 67069 MW; 625A8EF9AD0404CB CRC64;
MTDLTQLDTV LVANRGEIAR RIIRTLRASG IRSIAVYSDA DAHAPHVREA NQAVRIGAAA
ASSSYLDVDA VVAAARSTGS RAIHPGYGFL SESASLATAC AEAGIVFIGP SVAALQIMGD
KARARDHVSR SGVPVVPGFD ARGLSDAEIA EEAASVGFPL LIKPSAGGGG KGMEVVDDAS
DLPRALASAR RIAAAAFADD AVIVERLIRR PRHIEVQVFG DVHGSVIALG ERECTLQRRH
QKVIEEAPSA GIPEATRERL LEAAVDAARS VDYVGAGTVE FLVDADRPED FFFIEMNTRL
QVEHPVTEEV TGLDLVAMQI AVAAGDHLPP APRLHGHAVE ARVYAESPER GFLPSTGRVL
LFDAPTGVRV DAAVETDSVV TEFYDPMIAK VIAHADDRAT ALRRLDEALS RTVVLGVETN
IAFLRRLCRD ERVVSGDLDT GLIETLLPVS GEPPTPAALA AARAHVLASG AAGSSERAAA
RAGAVWQTLS DRESTSLAFE TDDGQVHDAP SSSVAARGRV ATDEDGAVWV GVDGSSVRLR
PLDRRRRMLR RLADRSGAAA GGGHEGLAPM PGSVVAVHVQ DGTDVTAGMP LVSIEAMKME
HPVLAPRDGR VRVLVAVGDQ VRRDQAVVRM TTEENG
//
