LOCUS VTR94544.1 545 aa PRT BCT 03-FEB-2020
DEFINITION Gemmata massiliana dihydrolipoamide acetyltransferase
: Pyruvate dehydrogenase E2 component OS=Melioribacter
roseus (strain JCM 17771 / P3M-2) GN=MROS_0858 PE=3 SV=
1: Biotin_lipoyl: Biotin_lipoyl: E3_binding: 2-oxoacid_dh
protein.
ACCESSION LR593886-3845
PROTEIN_ID VTR94544.1
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_31700"
/note="BLAST_uniprot:hit_1 ;
ACCESSION=tr|I6ZPW5|I6ZPW5_MELRP ;
ALN/Q_length_ratio=0.983 ; DESCRIPTION=Pyruvate
dehydrogenase E2 component OS=Melioribacter roseus (strain
JCM 17771 / P3M-2) GN=MROS_0858 PE=3 SV=1 ; EVALUE=1e-142
; Q/S_length_ratio=1.011"
/note="BLAST_uniprot:hit_2 ;
ACCESSION=tr|U7FSW9|U7FSW9_9GAMM ;
ALN/Q_length_ratio=0.982 ; DESCRIPTION=Acetyltransferase
component of pyruvate dehydrogenase complex OS=Alcanivorax
sp. P2S70 GN=Q670_15350 PE=3 SV=1 ; EVALUE=1e-134 ;
Q/S_length_ratio=0.987"
/note="BLAST_uniprot:hit_3 ;
ACCESSION=tr|A0A095USD8|A0A095USD8_9GAMM ;
ALN/Q_length_ratio=0.963 ; DESCRIPTION=Pyruvate
dehydrogenase, E2 component OS=Alcanivorax sp. 19-m-6
GN=Y5S_01338 PE=4 SV=1 ; EVALUE=1e-132 ;
Q/S_length_ratio=1.006"
/note="BLAST_uniprot:hit_4 ;
ACCESSION=tr|D5SV60|D5SV60_PLAL2 ;
ALN/Q_length_ratio=0.778 ; DESCRIPTION=Catalytic domain of
components of various dehydrogenase complexes
OS=Planctomyces limnophilus (strain ATCC 43296 / DSM 3776
/ IFAM 1008 / 290) GN=Plim_3533 PE=3 SV=1 ; EVALUE=1e-116
; Q/S_length_ratio=1.282"
/note="BLAST_uniprot:hit_5 ;
ACCESSION=tr|L1NYE4|L1NYE4_9NEIS ;
ALN/Q_length_ratio=0.976 ; DESCRIPTION=Acetyltransferase
component of pyruvate dehydrogenase complex OS=Neisseria
sp. oral taxon 020 str. F0370 GN=HMPREF9120_00774 PE=3
SV=1 ; EVALUE=1e-108 ; Q/S_length_ratio=1.002"
/note="BLAST_uniprot:hit_6 ;
ACCESSION=tr|D0W0E3|D0W0E3_NEICI ;
ALN/Q_length_ratio=0.972 ; DESCRIPTION=Acetyltransferase
component of pyruvate dehydrogenase complex OS=Neisseria
cinerea ATCC 14685 GN=aceF PE=3 SV=1 ; EVALUE=1e-107 ;
Q/S_length_ratio=0.975"
/note="BLAST_uniprot:hit_7 ;
ACCESSION=tr|C5TJL1|C5TJL1_NEIFL ;
ALN/Q_length_ratio=0.954 ; DESCRIPTION=Acetyltransferase
component of pyruvate dehydrogenase complex OS=Neisseria
flavescens SK114 GN=aceF PE=3 SV=1 ; EVALUE=1e-106 ;
Q/S_length_ratio=1.024"
/note="BLAST_uniprot:hit_8 ;
ACCESSION=tr|E5UJ13|E5UJ13_NEIMU ;
ALN/Q_length_ratio=0.960 ; DESCRIPTION=Acetyltransferase
component of pyruvate dehydrogenase complex OS=Neisseria
mucosa C102 GN=HMPREF0604_00709 PE=3 SV=1 ; EVALUE=1e-106
; Q/S_length_ratio=1.019"
/note="BLAST_uniprot:hit_9 ;
ACCESSION=tr|C0EK62|C0EK62_NEIFL ;
ALN/Q_length_ratio=0.960 ; DESCRIPTION=Acetyltransferase
component of pyruvate dehydrogenase complex OS=Neisseria
flavescens NRL30031/H210 GN=aceF PE=3 SV=1 ; EVALUE=1e-105
; Q/S_length_ratio=1.019"
/note="BLAST_uniprot:hit_12 ;
ACCESSION=tr|H8DX84|H8DX84_9NEIS ;
ALN/Q_length_ratio=0.974 ; DESCRIPTION=Acetyltransferase
component of pyruvate dehydrogenase complex OS=Kingella
kingae PYKK081 GN=KKB_04037 PE=3 SV=1 ; EVALUE=1e-104 ;
Q/S_length_ratio=1.004"
/note="BLAST_uniprot:hit_10 ;
ACCESSION=tr|L5UET0|L5UET0_NEIME ;
ALN/Q_length_ratio=0.960 ; DESCRIPTION=Acetyltransferase
component of pyruvate dehydrogenase complex OS=Neisseria
meningitidis NM3642 GN=aceF PE=3 SV=1 ; EVALUE=1e-104 ;
Q/S_length_ratio=1.019"
/note="BLAST_uniprot:hit_11 ;
ACCESSION=tr|L5U8D2|L5U8D2_NEIME ;
ALN/Q_length_ratio=0.960 ; DESCRIPTION=Acetyltransferase
component of pyruvate dehydrogenase complex OS=Neisseria
meningitidis NM3652 GN=aceF PE=3 SV=1 ; EVALUE=1e-104 ;
Q/S_length_ratio=1.019"
/note="BLAST_uniprot:hit_13 ;
ACCESSION=tr|V7IF42|V7IF42_EIKCO ;
ALN/Q_length_ratio=0.963 ; DESCRIPTION=Acetyltransferase
component of pyruvate dehydrogenase complex OS=Eikenella
corrodens CC92I GN=HMPREF1177_01101 PE=3 SV=1 ;
EVALUE=1e-102 ; Q/S_length_ratio=1.011"
/note="BLAST_uniprot:hit_14 ;
ACCESSION=tr|A0A072NBX0|A0A072NBX0_9DEIO ;
ALN/Q_length_ratio=0.837 ; DESCRIPTION=Acetyltransferase
component of pyruvate dehydrogenase complex OS=Deinococcus
sp. RL GN=RDMS_05355 PE=3 SV=1 ; EVALUE=1e-101 ;
Q/S_length_ratio=0.899"
/note="BLAST_uniprot:hit_15 ;
ACCESSION=tr|A0A031BW92|A0A031BW92_PSEAI ;
ALN/Q_length_ratio=0.978 ; DESCRIPTION=Acetyltransferase
component of pyruvate dehydrogenase complex OS=Pseudomonas
aeruginosa BWH056 GN=V557_03076 PE=3 SV=1 ; EVALUE=1e-100
; Q/S_length_ratio=0.996"
/note="Pfam_scan:hit_1 (1..74);
Pfam:PF00364.17:Biotin_lipoyl;
Pfam_type:Domain;HMM_aln_Length:70; HMM_Length:74;
EVALUE:3.6e-20; BITSCORE: 71.3"
/note="Pfam_scan:hit_2 (115..188);
Pfam:PF00364.17:Biotin_lipoyl;
Pfam_type:Domain;HMM_aln_Length:71; HMM_Length:74;
EVALUE:3e-20; BITSCORE: 71.6"
/note="Pfam_scan:hit_3 (237..274);
Pfam:PF02817.12:E3_binding;
Pfam_type:Family;HMM_aln_Length:33; HMM_Length:39;
EVALUE:5.1e-09; BITSCORE: 35.6"
/note="Pfam_scan:hit_4 (312..543);
Pfam:PF00198.18:2-oxoacid_dh;
Pfam_type:Domain;HMM_aln_Length:227; HMM_Length:231;
EVALUE:1.1e-77; BITSCORE: 260.3"
/note="GO_domain:GO:0016746"
BEGIN
1 MDIVLANPGE GIEGGTVTAV FVKVGDAVKS GQALVEVSTD KASMEVTAES DGTVEAVHVK
61 PGDKVSVGGK LIRVSGGAKP SEAPAPKNQP QQKAEAPAAP APHAKTEAPT AAASVDVVLA
121 NPGEGIEGGT VTAVFVKVGD AVKSGQALVE VSTDKASMEV TAESDGTVEA VHVKPGDKVS
181 VGGKLVTLKA AGATSNAPKA STPVPAQQTA PKSAPAASQP QAQPASNNGS ANGTKTLVPA
241 GPATRKLARE LGVALGELKG SGREGRVTLD DLKGFVRTER QRVKESGGVV APASGIIVNA
301 FALPPLPDFA KFGPVEVTEV ATIRQTIAKN LTVGWRTMPM VTQHELADIT DLEAGRKRIV
361 DALPKGSPKI TMTVLAIKAC IAALKEFPRF NSSYDMNAGK LVLKKYFHIG IAVDTDAGLK
421 VPVIRDADKK SIRDLAAEVS TIAEKARTNK LTIDEMRGGT FTITNLGGIG GTGFTPLVNY
481 PEVAILGLSK SSLQPIVRDG QIVARLMMPL SLTYDHRVID GADGCRFTVR LAQLFSDPLR
541 LLMET
//