ID A0A366I8F9_9GAMM Unreviewed; 424 AA.
AC A0A366I8F9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Biotin-dependent carboxylase-like uncharacterized protein {ECO:0000313|EMBL:RBP65815.1};
GN ORFNames=DES54_10479 {ECO:0000313|EMBL:RBP65815.1};
OS Brenneria salicis ATCC 15712 = DSM 30166.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Brenneria.
OX NCBI_TaxID=714314 {ECO:0000313|EMBL:RBP65815.1, ECO:0000313|Proteomes:UP000253046};
RN [1] {ECO:0000313|EMBL:RBP65815.1, ECO:0000313|Proteomes:UP000253046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 30166 {ECO:0000313|EMBL:RBP65815.1,
RC ECO:0000313|Proteomes:UP000253046};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (JUN-2018) 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:RBP65815.1}.
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DR EMBL; QNRY01000004; RBP65815.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A366I8F9; -.
DR Proteomes; UP000253046; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR003778; CT_A_B.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR NCBIfam; TIGR00724; urea_amlyse_rel; 1.
DR PANTHER; PTHR43309; 5-OXOPROLINASE SUBUNIT C; 1.
DR PANTHER; PTHR43309:SF3; 5-OXOPROLINASE SUBUNIT C; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF02626; CT_A_B; 1.
DR SMART; SM00797; AHS2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR PROSITE; PS50979; BC; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 1..108
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
SQ SEQUENCE 424 AA; 46163 MW; 105A406DD9E15EDF CRC64;
MRIYAEDPLK NFQPSPGVLT EVAFPADVRV DGWVSTGTEV SAYYDPMIAK LIVHADTRDQ
ALEKMRRALN ETRLHGIATN LDYLRQIIAT DAFRNGKVWT RLLDGFTPAA SVIEVVQPGT
WSSVQDYPGR LGYWDIGVPP SGPMDDFAFR LANRIVGNDA SAAGLEFTLQ GPTLRFHCDA
VIALTGAACP AELDGQAVGY WRPVAVKAGQ TLTLGRAQSG CRTYLAVRNG IDVPRYLGSR
STFALGAFGG HAGRTLRVAD MLAISQPDLP ACATPAPVSA PQAVDTALIP AYRDEWRIGV
LYGPHGAPDF FTHEAIDEFF AAEWQVHYNS NRLGVRLVGP KPRRTGRRAV CAAGGHYQPQ
RNVAHQLDRS RHLGRARRAG DAGRPVAGRR DCQRREKLVY RGFPGILTVF SGVDVHSCYA
VSAA
//