LOCUS VTR97181.1 337 aa PRT BCT 03-FEB-2020
DEFINITION Gemmata massiliana n-acetyl-gamma-glutamyl-phosphate reductase
: N-acetyl-gamma-glutamyl-phosphate reductase OS=Planctomyces
maris DSM 8797 GN=argC PE=3 SV=1: Semialdhyde_dh: Semialdhyde_dhC
protein.
ACCESSION LR593886-6166
PROTEIN_ID VTR97181.1
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_08490"
/note="BLAST_uniprot:hit_2 ;
ACCESSION=tr|D5SPT5|D5SPT5_PLAL2 ;
ALN/Q_length_ratio=0.988 ;
DESCRIPTION=N-acetyl-gamma-glutamyl-phosphate reductase
OS=Planctomyces limnophilus (strain ATCC 43296 / DSM 3776
/ IFAM 1008 / 290) GN=argC PE=3 SV=1 ; EVALUE=1e-135 ;
Q/S_length_ratio=1.006"
/note="BLAST_uniprot:hit_1 ;
ACCESSION=tr|A6CAM9|A6CAM9_9PLAN ;
ALN/Q_length_ratio=0.991 ;
DESCRIPTION=N-acetyl-gamma-glutamyl-phosphate reductase
OS=Planctomyces maris DSM 8797 GN=argC PE=3 SV=1 ;
EVALUE=1e-135 ; Q/S_length_ratio=1.000"
/note="BLAST_uniprot:hit_3 ;
ACCESSION=tr|F0SFK9|F0SFK9_PLABD ;
ALN/Q_length_ratio=0.997 ;
DESCRIPTION=N-acetyl-gamma-glutamyl-phosphate reductase
OS=Planctomyces brasiliensis (strain ATCC 49424 / DSM 5305
/ JCM 21570 / NBRC 103401 / IFAM 1448) GN=argC PE=3 SV=1 ;
EVALUE=1e-134 ; Q/S_length_ratio=0.983"
/note="BLAST_uniprot:hit_4 ;
ACCESSION=tr|L0DKW7|L0DKW7_SINAD ;
ALN/Q_length_ratio=0.994 ;
DESCRIPTION=N-acetyl-gamma-glutamyl-phosphate reductase
OS=Singulisphaera acidiphila (strain ATCC BAA-1392 / DSM
18658 / VKM B-2454 / MOB10) GN=argC PE=3 SV=1 ;
EVALUE=1e-133 ; Q/S_length_ratio=0.991"
/note="BLAST_uniprot:hit_5 ;
ACCESSION=tr|A4A2L3|A4A2L3_9PLAN ;
ALN/Q_length_ratio=0.991 ;
DESCRIPTION=N-acetyl-gamma-glutamyl-phosphate reductase
OS=Blastopirellula marina DSM 3645 GN=argC PE=3 SV=1 ;
EVALUE=1e-132 ; Q/S_length_ratio=0.997"
/note="BLAST_uniprot:hit_6 ;
ACCESSION=tr|E8R0G0|E8R0G0_ISOPI ;
ALN/Q_length_ratio=1.003 ;
DESCRIPTION=N-acetyl-gamma-glutamyl-phosphate reductase
OS=Isosphaera pallida (strain ATCC 43644 / DSM 9630 /
IS1B) GN=argC PE=3 SV=1 ; EVALUE=1e-128 ;
Q/S_length_ratio=0.988"
/note="BLAST_uniprot:hit_7 ;
ACCESSION=tr|D2QWM3|D2QWM3_PIRSD ;
ALN/Q_length_ratio=0.991 ;
DESCRIPTION=N-acetyl-gamma-glutamyl-phosphate reductase
OS=Pirellula staleyi (strain ATCC 27377 / DSM 6068 / ICPB
4128) GN=argC PE=3 SV=1 ; EVALUE=1e-124 ;
Q/S_length_ratio=1.006"
/note="BLAST_uniprot:hit_8 ;
ACCESSION=tr|L7CDM1|L7CDM1_RHOBT ;
ALN/Q_length_ratio=1.012 ;
DESCRIPTION=N-acetyl-gamma-glutamyl-phosphate reductase
OS=Rhodopirellula baltica SWK14 GN=argC PE=3 SV=1 ;
EVALUE=1e-112 ; Q/S_length_ratio=0.974"
/note="BLAST_uniprot:hit_10 ;
ACCESSION=tr|K5DCX2|K5DCX2_RHOBT ;
ALN/Q_length_ratio=1.012 ;
DESCRIPTION=N-acetyl-gamma-glutamyl-phosphate reductase
OS=Rhodopirellula baltica SH28 GN=argC PE=3 SV=1 ;
EVALUE=1e-111 ; Q/S_length_ratio=0.974"
/note="BLAST_uniprot:hit_9 ;
ACCESSION=tr|M2B689|M2B689_9PLAN ;
ALN/Q_length_ratio=1.012 ;
DESCRIPTION=N-acetyl-gamma-glutamyl-phosphate reductase
OS=Rhodopirellula europaea 6C GN=argC PE=3 SV=1 ;
EVALUE=1e-111 ; Q/S_length_ratio=0.974"
/note="BLAST_uniprot:hit_12 ; ACCESSION=Q7UVL4 ;
ALN/Q_length_ratio=1.012 ;
DESCRIPTION=N-acetyl-gamma-glutamyl-phosphate reductase
OS=Rhodopirellula baltica (strain SH1) GN=argC PE=3 SV=1 ;
EVALUE=1e-110 ; Q/S_length_ratio=0.974"
/note="BLAST_uniprot:hit_14 ;
ACCESSION=tr|B3EA19|B3EA19_GEOLS ;
ALN/Q_length_ratio=1.003 ;
DESCRIPTION=N-acetyl-gamma-glutamyl-phosphate reductase
OS=Geobacter lovleyi (strain ATCC BAA-1151 / DSM 17278 /
SZ) GN=argC PE=3 SV=1 ; EVALUE=1e-110 ;
Q/S_length_ratio=0.949"
/note="BLAST_uniprot:hit_13 ;
ACCESSION=tr|M5S030|M5S030_9PLAN ;
ALN/Q_length_ratio=1.012 ;
DESCRIPTION=N-acetyl-gamma-glutamyl-phosphate reductase
OS=Rhodopirellula europaea SH398 GN=argC PE=3 SV=1 ;
EVALUE=1e-110 ; Q/S_length_ratio=0.974"
/note="BLAST_uniprot:hit_11 ;
ACCESSION=tr|F2AL50|F2AL50_RHOBT ;
ALN/Q_length_ratio=1.012 ;
DESCRIPTION=N-acetyl-gamma-glutamyl-phosphate reductase
OS=Rhodopirellula baltica WH47 GN=argC PE=3 SV=1 ;
EVALUE=1e-110 ; Q/S_length_ratio=0.974"
/note="BLAST_uniprot:hit_15 ;
ACCESSION=tr|R6MLI8|R6MLI8_9FIRM ;
ALN/Q_length_ratio=1.000 ;
DESCRIPTION=N-acetyl-gamma-glutamyl-phosphate reductase
OS=Firmicutes bacterium CAG:41 GN=argC PE=3 SV=1 ;
EVALUE=1e-107 ; Q/S_length_ratio=0.977"
/note="Pfam_scan:hit_1 (5..143);
Pfam:PF01118.19:Semialdhyde_dh;
Pfam_type:Domain;HMM_aln_Length:119; HMM_Length:121;
EVALUE:1.2e-29; BITSCORE: 103.0"
/note="Pfam_scan:hit_2 (160..314);
Pfam:PF02774.13:Semialdhyde_dhC;
Pfam_type:Domain;HMM_aln_Length:182; HMM_Length:184;
EVALUE:2.1e-16; BITSCORE: 60.3"
/note="GO_domain:GO:0005737"
/note="GO_domain:GO:0016491"
/note="GO_domain:GO:0006520"
/note="GO_domain:GO:0009058"
/note="Enzyme_Code:EC:1.2.1.38"
BEGIN
1 MDKVKVAILG GSGYTAVELI KLLLRHPGAE IVAITSRQSE HIADLHPSLL GRLDLRCEPF
61 DPDALKSKGT QVVFGCLPHG TSMESIPPLL ERGMRVIDLS ADYRLRDVKV YEQWYKETHH
121 DQKNLAQAVY GLPEVYGDKI VGAKLVANPG CYPQTAILGL APLVANKLIE LTGIVIDSKS
181 GVSGGGRTPK LSFHFPECNE SVTAYAVGTH RHTPEIEQAL SDVAGAPVSV IFTPHLMPMD
241 RGIFSTIYAT LTRAVTEAEL VELYRSYFAD KPFVRVRTNP PATKDTTGTN FLDVCVKVVR
301 GKVLVLAAED NLVRGASGVA VQNFNRVFGF DERTGLM
//