ID A0A1C6LU08_9BURK Unreviewed; 494 AA.
AC A0A1C6LU08;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE SubName: Full=Acetyl-CoA/propionyl-CoA carboxylase, biotin carboxylase, biotin carboxyl carrier protein {ECO:0000313|EMBL:SCK09968.1};
GN ORFNames=VAR608DRAFT_0394 {ECO:0000313|EMBL:SCK09968.1};
OS Variovorax sp. HW608.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1034889 {ECO:0000313|EMBL:SCK09968.1, ECO:0000313|Proteomes:UP000198203};
RN [1] {ECO:0000313|Proteomes:UP000198203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HW608 {ECO:0000313|Proteomes:UP000198203};
RA Varghese N., Submissions Spin;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LT607803; SCK09968.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C6LU08; -.
DR Proteomes; UP000198203; Chromosome i.
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; 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}; Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}.
FT DOMAIN 6..449
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 125..320
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 494 AA; 53069 MW; 23B1F66B96BAD6FA CRC64;
MQINWPFQSV LIANRGEIAS RIVRTVQRLG LRAVVVHHAV DAQTPAVRQA DAAVEIHGTT
PVAAYLDGAQ IIDAARSAGA GAIHPGYGFL SENATFARQC AQAGLVFVGP SPEVIDLMGD
KVRARAFVAQ GGFPVAPSAI EDDDPDSFVE RALAVGFPLL IKPAAGGGGK GMRIVREAEQ
LRPELERARS EGQRYFGDGR LYVERFIENP RHIEVQVLGD HHGNVVHLFE RECSVQRRFQ
KIVEESPSPA LTPELRRDIC ATAAGIAKRA GYSNAGTVEF IFGSGEFYFL EMNTRLQVEH
PVTEEVLGID LVDQQLLVAA GNKLAFTQAS LLPRGHAIEF RIYAEDPARG YLPTTGPILA
LHEPRGPGIR VDSGIAAGQE VTAAFDPMLA KLIVSGATRT EAIAAAQRAL GDYVLLGCKT
NTGFLRRLLS HPAFVAGEIH TGFLDAQPEV AAEPPIPTDT LHRLLAIAAM ASRPVRAAAD
AVPDLHAAMG DWRN
//
