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
//