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 //