ID A0A1N7RTB5_9BURK Unreviewed; 675 AA.
AC A0A1N7RTB5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Acetyl-/propionyl-coenzyme A carboxylase alpha chain {ECO:0000313|EMBL:SIT38359.1};
DE EC=6.3.4.14 {ECO:0000313|EMBL:SIT38359.1};
GN Name=accA {ECO:0000313|EMBL:SIT38359.1};
GN ORFNames=BN2475_150051 {ECO:0000313|EMBL:SIT38359.1};
OS Paraburkholderia ribeironis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1247936 {ECO:0000313|EMBL:SIT38359.1, ECO:0000313|Proteomes:UP000187012};
RN [1] {ECO:0000313|EMBL:SIT38359.1, ECO:0000313|Proteomes:UP000187012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=STM7296 {ECO:0000313|EMBL:SIT38359.1,
RC ECO:0000313|Proteomes:UP000187012};
RA Song W.-J., Kurnit D.M.;
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; CYGX02000015; SIT38359.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1N7RTB5; -.
DR STRING; 1247936.BN2475_150051; -.
DR OrthoDB; 9803706at2; -.
DR Proteomes; UP000187012; 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 GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
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; IPR001882; Biotin_BS.
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 SMART; SM01209; GARS_A; 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; PS00188; BIOTIN; 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, ECO:0000313|EMBL:SIT38359.1};
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:UP000187012}.
FT DOMAIN 1..462
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..317
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 598..673
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 675 AA; 72145 MW; C75E74DC0D1CB884 CRC64;
MFNKILIANR GEIACRVAAT CKRLGIASVA VYSDADANAK HVAACDEAVH IGGSTAAESY
LRIERIIEAA RASGAQAVHP GYGFLSENED FAHACEAAGI VFIGPPVAAI AAMGSKAAAK
ALMHAAAVPL VPGYHGDDQD PELLHREADA IGYPVLLKAS AGGGGKGMRV VARSEVFAAA
LASCKREAAS SFGNDRVLIE KYLTRPRHVE VQVFADRHGG AVYLFDRDCS VQRRHQKVLE
EAPAPGLSAE IRRAMGEAAV AAARAVNYVG AGTVEFIMTG SGEFYFMEMN TRLQVEHPVT
EMVTGQDLVE WQLRVAADEP LPLTQQQLQL DGHAIEARIY AEHPARGFLP STGTLKHLRM
PEGVEFAIDA AGLGESGRKA PVRIDSGVRE GDTITPFYDP MIAKLIVHGA TREEALARLS
RALHACEVVG PHTNIEFLQR IVTSEPFATA DLDTGLIERH HDALFAPLKK PFKEALALAC
AALLTREGGT AHGASPWDAL SHWRLNGGYT QTLSWREVDN DNAFTVTFAR DGATQTLEHD
GVREAFSWSV GTGAHEFRAT IGDERVTGRV FVDVDTFHVF CFGHALAFEW QNLLAHAADA
EGGEGRLTAP MPGKVIAVLV EPGTVVEKGT PLLVMEAMKM EHTIGAPAAG TVSEVLYGVG
DQVADGAQLL VLDVQ
//
