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Database: UniProt
Entry: F0GFV2_9BURK
LinkDB: F0GFV2_9BURK
Original site: F0GFV2_9BURK 
ID   F0GFV2_9BURK            Unreviewed;       558 AA.
AC   F0GFV2;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=Biotin carboxylation region {ECO:0000313|EMBL:EGC99631.1};
DE   Flags: Fragment;
GN   ORFNames=B1M_35646 {ECO:0000313|EMBL:EGC99631.1};
OS   Burkholderia sp. TJI49.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=987057 {ECO:0000313|EMBL:EGC99631.1, ECO:0000313|Proteomes:UP000003049};
RN   [1] {ECO:0000313|EMBL:EGC99631.1, ECO:0000313|Proteomes:UP000003049}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TJI49 {ECO:0000313|EMBL:EGC99631.1,
RC   ECO:0000313|Proteomes:UP000003049};
RX   PubMed=23653265; DOI=10.1007/s11274-013-1366-5;
RA   Khan A., Asif H., Studholme D.J., Khan I.A., Azim M.K.;
RT   "Genome characterization of a novel Burkholderia cepacia complex genomovar
RT   isolated from dieback affected mango orchards.";
RL   World J. Microbiol. Biotechnol. 29:2033-2044(2013).
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:EGC99631.1}.
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DR   EMBL; AEXE01002246; EGC99631.1; -; Genomic_DNA.
DR   AlphaFoldDB; F0GFV2; -.
DR   Proteomes; UP000003049; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; IPR003778; CT_A_B.
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   Pfam; PF02626; CT_A_B; 1.
DR   SMART; SM00797; AHS2; 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}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   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          2..445
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          121..318
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   NON_TER         558
FT                   /evidence="ECO:0000313|EMBL:EGC99631.1"
SQ   SEQUENCE   558 AA;  58637 MW;  30A3B81AFA9CDB88 CRC64;
     MRFAKVLVAN RGEIACRVIR TLKRLGIASV AIYSDADRDA RHVTLADEAV RVGAAPAADS
     YLNVAAILAA ARATGAQAVH PGYGFLSEHA GFADACEAAG LRFIGPRGDQ MRAFGLKHTA
     RALAAAQGVA LLPGTGLLDD VETALAEAAA IGYPVMLKST AGGGGIGMSL CRDAAQLEAA
     FESVVRLGNA NFAHAGVYLE KFVEHARHIE VQIFGDGRGN AIALGERDCS VQRRNQKVIE
     ETPAPDLTDA ERGALHASAV RLARAVGYAS AGTVEFVFDA STRQFYFLEV NTRLQVEHGV
     TEAVTGIDLV EWMILQAEGD LPPLDTLAVA PRGASIQVRL YAEDPHKQFL PSAGVLTHVA
     FPDDVRVDGW IEAGTEVSAH YDPLLAKLIV RGDTRREALA ALQAALAQTE LYGIETNLDY
     LRAIAGSDTF ARGAPTTAFL SRFAFAPHTI DVLDGGVQTT VQQAPGRVGY WSVGVPPSGP
     MDDRAFDLAN ALLGNARDAA GLEFTMVGAT LRFNTATLFV LGGAPLAATL DGEPAPFRQV
     LRARPGAVLK LGGVTGAG
//
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