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Database: UniProt
Entry: A0A0S4LCJ4_9BACT
LinkDB: A0A0S4LCJ4_9BACT
Original site: A0A0S4LCJ4_9BACT 
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}.
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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
//
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