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Database: UniProt
Entry: H5XM15_9PSEU
LinkDB: H5XM15_9PSEU
Original site: H5XM15_9PSEU 
ID   H5XM15_9PSEU            Unreviewed;       388 AA.
AC   H5XM15;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=Glutamate-1-semialdehyde aminotransferase {ECO:0000313|EMBL:EHR63094.1};
GN   ORFNames=SaccyDRAFT_4276 {ECO:0000313|EMBL:EHR63094.1};
OS   Saccharomonospora cyanea NA-134.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharomonospora.
OX   NCBI_TaxID=882082 {ECO:0000313|EMBL:EHR63094.1};
RN   [1] {ECO:0000313|EMBL:EHR63094.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA-134 {ECO:0000313|EMBL:EHR63094.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Pagani I., Brambilla E.-M.,
RA   Klenk H.-P., Woyke T.;
RT   "The Noncontiguous Finished sequence of Saccharomonospora cyanea NA-134.";
RL   Submitted (NOV-2011) 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; CM001440; EHR63094.1; -; Genomic_DNA.
DR   RefSeq; WP_005459195.1; NZ_CM001440.1.
DR   AlphaFoldDB; H5XM15; -.
DR   STRING; 882082.SaccyDRAFT_4276; -.
DR   eggNOG; COG0001; Bacteria.
DR   HOGENOM; CLU_016922_1_2_11; -.
DR   OrthoDB; 9801052at2; -.
DR   Proteomes; UP000002791; Chromosome.
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:EHR63094.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:EHR63094.1}.
SQ   SEQUENCE   388 AA;  41348 MW;  045F68141FF02D43 CRC64;
     MRIAPDELPE RARAVLPGGN TRSTVFVPPH PPYAVAGEGC VVTDAQGHRV YDCNNNYTSL
     LHGHARREIV EVATETLARG SAFGLPTESE IELAELLRDR TGLTRWRFCN SGTEAVMMAV
     RVARAVTERS RIIRFEASYH GTYDGVVAAS ATGVPGAVEE QSVILPQADG AAFDAAMRQH
     GHEVAAVLID LMPNRAGLRP VPRDFVDHVR ARTREYGSLL VVDEVITFRL GVGGLRQRYG
     VAADLTTLGK VIGGGFPVGA VGGSVDVMKA FDPLGDGVVS WGGTFSANPV SMRAGATALR
     LYGKSEVDRL NALGDRLRQE LADSGLPVSG FGSLIRLLVD DPTVTWWALY REGVLAGTNG
     LLALSTAMTD DDVTEIGTRV RAAARAST
//
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