ID A0A0Q8P6V9_9BURK Unreviewed; 447 AA.
AC A0A0Q8P6V9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Biotin carboxylase {ECO:0000313|EMBL:KRB67985.1};
GN ORFNames=ASE07_10055 {ECO:0000313|EMBL:KRB67985.1};
OS Noviherbaspirillum sp. Root189.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Noviherbaspirillum.
OX NCBI_TaxID=1736487 {ECO:0000313|EMBL:KRB67985.1, ECO:0000313|Proteomes:UP000051303};
RN [1] {ECO:0000313|EMBL:KRB67985.1, ECO:0000313|Proteomes:UP000051303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root189 {ECO:0000313|EMBL:KRB67985.1,
RC ECO:0000313|Proteomes:UP000051303};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB67985.1, ECO:0000313|Proteomes:UP000051303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root189 {ECO:0000313|EMBL:KRB67985.1,
RC ECO:0000313|Proteomes:UP000051303};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KRB67985.1}.
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DR EMBL; LMHZ01000067; KRB67985.1; -; Genomic_DNA.
DR RefSeq; WP_057293721.1; NZ_LMHZ01000067.1.
DR AlphaFoldDB; A0A0Q8P6V9; -.
DR STRING; 1736487.ASE07_10055; -.
DR OrthoDB; 9803706at2; -.
DR Proteomes; UP000051303; Unassembled WGS sequence.
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 GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
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; 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}; Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000051303}.
FT DOMAIN 1..445
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 119..316
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 447 AA; 48479 MW; EBDC5F7B44BA0DB9 CRC64;
MRRILVANRG AVAARVIRAV HALGLQAVAV YSDADAGMPY LTDADAAMHI GEAAPMASYL
NQDAILAAAA KAGADAIHPG YGFLSENAGF AERVERAEMC FIGPSSHWIR DLGQKTHARE
LMAEYGMPMT RASRVLDDDP AAVAAVAREM GYPLLLKPGN GGGGIGMLPV RNEEEVEAVW
NRARSVASKS FGSAQLYFEH LLEQPRHIEF QFLADRYGGV RCLFERDCST QRRHQKVLEE
APAPALPREQ LDAMAAQLQD ILGRIGYDII GTVEMLYTPE RGFSFLEVNT RLQVEHAVTE
EVTGIDIVAA QIRLARGERI NDVLPATPAL SGHAIEARVY AEDPVRFFPS PGLLEQFDVP
SGLGIRIETG YAEGCRVSSY YDPMLAKVIA SGADRPQAIA RLVAALDACS VRGVKTNIPF
IQRVLASRDF RDGAVHTGLA ESVLRSA
//
