ID A0A0S4LCJ4_9BACT Unreviewed; 435 AA.
AC A0A0S4LCJ4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Glutamate-1-semialdehyde aminotransferase {ECO:0000313|EMBL:CUS34911.1};
GN ORFNames=COMA1_20019 {ECO:0000313|EMBL:CUS34911.1};
OS Candidatus Nitrospira nitrosa.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Nitrospira.
OX NCBI_TaxID=1742972 {ECO:0000313|EMBL:CUS34911.1, ECO:0000313|Proteomes:UP000199032};
RN [1] {ECO:0000313|EMBL:CUS34911.1, ECO:0000313|Proteomes:UP000199032}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COMA1 {ECO:0000313|EMBL:CUS34911.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CZQA01000008; CUS34911.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S4LCJ4; -.
DR STRING; 1742972.COMA1_20019; -.
DR OrthoDB; 9807885at2; -.
DR Proteomes; UP000199032; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43713; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE; 1.
DR PANTHER; PTHR43713:SF3; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE 1, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:CUS34911.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000199032};
KW Transferase {ECO:0000313|EMBL:CUS34911.1}.
SQ SEQUENCE 435 AA; 48555 MW; 8F0DE84E6AC68DFC CRC64;
MRFDKSKALQ DRAHALIPGG CHTYARGDDQ YPEQAPGFLI KGRGCHVWDV DGNEFIEYNM
GLRSVTLGYA DERILGAARK YMQEGSSFTR PSPIEVECAE EMLSLIEGAE MVKFGKNGSD
VTSAAIRLSR AYTGRDLVAV CADHPFFSGD DWFIGSTPIS TGIPKVTQEL TVKFSYNSIE
SVQALFQQYP GRIACLILEP EKETAPVDGF LMKVQELCRK NGSVFILDEM ICGFRWHNGG
GQGYHRIIPD LSTFGKALAN GFSVSALVGK REIMRLGGLD HEHERVFLLS LTHGAETHSL
AAAMEVIRTY KREPVIETMW RAGERLERGV RKSIGEHHLQ EYFKVLGKPC CQIYATLDGE
KTPSQAFRTL FLQETIKGGV LAPSFVVSSS HTDTDIDRTI EVIDKALQVY RKALDEGLDR
YLVGRPVKPV FRRYA
//