LOCUS VTR94794.1 265 aa PRT BCT 03-FEB-2020
DEFINITION Gemmata massiliana biotin--acetyl- -carboxylase ligase
: Biotin--acetyl-CoA-carboxylase ligase OS=Listeriaceae
bacterium FSL A5-0281 GN=EP57_08620 PE=4 SV=1: BPL_LplA_LipB
protein.
ACCESSION LR593886-4095
PROTEIN_ID VTR94794.1
SOURCE Gemmata massiliana
ORGANISM Gemmata massiliana
Bacteria; Planctomycetes; Planctomycetia; Gemmatales; Gemmataceae;
Gemmata.
REFERENCE 1
AUTHORS
CONSRTM Science for Life Laboratories
JOURNAL Submitted (14-MAY-2019) to the INSDC. DEPARTMENT OF CELL AND
MOLECULAR BIOLOGY, Uppsala University, Molecular Evolution,
Biomedicinskt centrum (BMC), Husargatan 3, 752 37 Uppsala, Sweden
FEATURES Qualifiers
source /organism="Gemmata massiliana"
/chromosome="1"
/isolate="Soil9"
/mol_type="genomic DNA"
/isolation_source="soil"
/db_xref="taxon:1210884"
protein /locus_tag="SOIL9_29200"
/note="BLAST_uniprot:hit_1 ;
ACCESSION=tr|A0A099W4B1|A0A099W4B1_9LIST ;
ALN/Q_length_ratio=0.898 ;
DESCRIPTION=Biotin--acetyl-CoA-carboxylase ligase
OS=Listeriaceae bacterium FSL A5-0281 GN=EP57_08620 PE=4
SV=1 ; EVALUE=5e-35 ; Q/S_length_ratio=0.818"
/note="BLAST_uniprot:hit_2 ;
ACCESSION=tr|W7D364|W7D364_9LIST ;
ALN/Q_length_ratio=0.898 ; DESCRIPTION=Bifunctional
protein BirA OS=Listeria riparia FSL S10-1204
GN=PRIP_11829 PE=4 SV=1 ; EVALUE=2e-33 ;
Q/S_length_ratio=0.818"
/note="BLAST_uniprot:hit_4 ;
ACCESSION=tr|U2SF00|U2SF00_9FIRM ;
ALN/Q_length_ratio=0.970 ;
DESCRIPTION=Biotin--[acetyl-CoA-carboxylase] ligase
OS=Oscillibacter sp. KLE 1728 GN=HMPREF1545_00666 PE=4
SV=1 ; EVALUE=2e-32 ; Q/S_length_ratio=0.793"
/note="BLAST_uniprot:hit_5 ;
ACCESSION=tr|W7CD47|W7CD47_9LIST ;
ALN/Q_length_ratio=0.906 ; DESCRIPTION=Bifunctional biotin
operon repressor/biotin-[acetyl-CoA-carboxylase]
synthetase OS=Listeria weihenstephanensis FSL R9-0317
GN=PWEIH_15728 PE=4 SV=1 ; EVALUE=2e-32 ;
Q/S_length_ratio=0.818"
/note="BLAST_uniprot:hit_3 ;
ACCESSION=tr|U2RGX2|U2RGX2_9FIRM ;
ALN/Q_length_ratio=0.970 ;
DESCRIPTION=Biotin--[acetyl-CoA-carboxylase] ligase
OS=Oscillibacter sp. KLE 1745 GN=HMPREF1546_00326 PE=4
SV=1 ; EVALUE=2e-32 ; Q/S_length_ratio=0.793"
/note="BLAST_uniprot:hit_6 ;
ACCESSION=tr|C7HBS2|C7HBS2_CLOTM ;
ALN/Q_length_ratio=0.819 ;
DESCRIPTION=Biotin/acetyl-CoA-carboxylase ligase
OS=Ruminiclostridium thermocellum DSM 2360
GN=ClothDRAFT_0237 PE=4 SV=1 ; EVALUE=3e-32 ;
Q/S_length_ratio=0.911"
/note="BLAST_uniprot:hit_7 ;
ACCESSION=tr|A3DIK6|A3DIK6_CLOTH ;
ALN/Q_length_ratio=0.819 ;
DESCRIPTION=Biotin/acetyl-CoA-carboxylase ligase
OS=Clostridium thermocellum (strain ATCC 27405 / DSM 1237
/ NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372)
GN=Cthe_2585 PE=4 SV=1 ; EVALUE=8e-32 ;
Q/S_length_ratio=0.784"
/note="BLAST_uniprot:hit_8 ;
ACCESSION=tr|D1NPH3|D1NPH3_CLOTM ;
ALN/Q_length_ratio=0.819 ;
DESCRIPTION=Biotin/acetyl-CoA-carboxylase ligase
OS=Ruminiclostridium thermocellum JW20 GN=Cther_0799 PE=4
SV=1 ; EVALUE=8e-32 ; Q/S_length_ratio=0.784"
/note="BLAST_uniprot:hit_10 ;
ACCESSION=tr|H8EF44|H8EF44_CLOTM ;
ALN/Q_length_ratio=0.819 ;
DESCRIPTION=Biotin/acetyl-CoA-carboxylase ligase
OS=Ruminiclostridium thermocellum AD2 GN=AD2_0381 PE=4
SV=1 ; EVALUE=9e-32 ; Q/S_length_ratio=0.784"
/note="BLAST_uniprot:hit_9 ;
ACCESSION=tr|E6UQA9|E6UQA9_CLOTL ;
ALN/Q_length_ratio=0.819 ;
DESCRIPTION=Biotin/acetyl-CoA-carboxylase ligase
OS=Clostridium thermocellum (strain DSM 1313 / LMG 6656 /
LQ8) GN=Clo1313_0172 PE=4 SV=1 ; EVALUE=9e-32 ;
Q/S_length_ratio=0.784"
/note="BLAST_uniprot:hit_11 ;
ACCESSION=tr|H8EPT0|H8EPT0_CLOTM ;
ALN/Q_length_ratio=0.819 ;
DESCRIPTION=Biotin/acetyl-CoA-carboxylase ligase
OS=Ruminiclostridium thermocellum YS GN=YSBL_2226 PE=4
SV=1 ; EVALUE=9e-32 ; Q/S_length_ratio=0.784"
/note="BLAST_uniprot:hit_12 ;
ACCESSION=tr|R9M5V6|R9M5V6_9FIRM ;
ALN/Q_length_ratio=0.913 ;
DESCRIPTION=Biotin-[acetyl-CoA-carboxylase] ligase
OS=Oscillibacter sp. 1-3 GN=C816_01487 PE=4 SV=1 ;
EVALUE=1e-31 ; Q/S_length_ratio=0.793"
/note="BLAST_uniprot:hit_13 ;
ACCESSION=tr|W7BIC7|W7BIC7_9LIST ;
ALN/Q_length_ratio=0.864 ; DESCRIPTION=BirA bifunctional
protein OS=Listeria grandensis FSL F6-971 GN=PGRAN_01460
PE=4 SV=1 ; EVALUE=2e-31 ; Q/S_length_ratio=0.818"
/note="BLAST_uniprot:hit_14 ;
ACCESSION=tr|A0A087LEI1|A0A087LEI1_GEOSE ;
ALN/Q_length_ratio=0.864 ;
DESCRIPTION=Biotin--acetyl-CoA-carboxylase ligase
OS=Geobacillus stearothermophilus GN=ET31_08875 PE=4 SV=1
; EVALUE=3e-31 ; Q/S_length_ratio=0.805"
/note="BLAST_uniprot:hit_15 ;
ACCESSION=tr|G2TGS8|G2TGS8_RHORU ;
ALN/Q_length_ratio=0.887 ;
DESCRIPTION=Biotin--acetyl-CoA-carboxylase ligase
OS=Rhodospirillum rubrum F11 GN=F11_06835 PE=4 SV=1 ;
EVALUE=4e-31 ; Q/S_length_ratio=0.957"
/note="Pfam_scan:hit_1 (24..150);
Pfam:PF03099.14:BPL_LplA_LipB;
Pfam_type:Domain;HMM_aln_Length:120; HMM_Length:125;
EVALUE:2.7e-18; BITSCORE: 66.2"
/note="GO_domain:GO:0044281"
/note="GO_domain:GO:0006790"
/note="GO_domain:GO:0051186"
/note="GO_domain:GO:0006464"
/note="GO_domain:GO:0034641"
/note="GO_domain:GO:0016874"
/note="Enzyme_Code:EC:6.3.4.15"
/note="Enzyme_Code:EC:6.3.4"
BEGIN
1 MSDSFTPRET WHFDTELIGR RVLVYDSVDS TLSLGATLAA SEEDTDGLVL IADHQSAGRG
61 QYGRTWTSRP GSSLLMSVIV RPPAGLRRPV ILTAWVAVAI ADAVQTLTGA QARLKWPNDL
121 LVSEKKICGI LIEQSSSAGA LTTIAGTGLN LTQTAEEFAQ ANLPSATSLG IISGGAIDTR
181 AAAGVVIRKL DREYSRLCAG ERGAVETEWK RRTGLLGRQV VIEHLGGAST TGRLRDMSFD
241 GLELEDPGGF VSVVAPESVA HVRAV
//