ID B9L2L9_THERP Unreviewed; 472 AA.
AC B9L2L9;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Glutamate-1-semialdehyde 2,1-aminomutase {ECO:0000313|EMBL:ACM05425.1};
DE EC=5.4.3.8 {ECO:0000313|EMBL:ACM05425.1};
GN OrderedLocusNames=trd_1421 {ECO:0000313|EMBL:ACM05425.1};
OS Thermomicrobium roseum (strain ATCC 27502 / DSM 5159 / P-2).
OC Bacteria; Thermomicrobiota; Thermomicrobia; Thermomicrobiales;
OC Thermomicrobiaceae; Thermomicrobium.
OX NCBI_TaxID=309801 {ECO:0000313|EMBL:ACM05425.1, ECO:0000313|Proteomes:UP000000447};
RN [1] {ECO:0000313|EMBL:ACM05425.1, ECO:0000313|Proteomes:UP000000447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27502 / DSM 5159 / P-2
RC {ECO:0000313|Proteomes:UP000000447};
RX PubMed=19148287; DOI=10.1371/journal.pone.0004207;
RA Wu D., Raymond J., Wu M., Chatterji S., Ren Q., Graham J.E., Bryant D.A.,
RA Robb F., Colman A., Tallon L.J., Badger J.H., Madupu R., Ward N.L.,
RA Eisen J.A.;
RT "Complete genome sequence of the aerobic CO-oxidizing thermophile
RT Thermomicrobium roseum.";
RL PLoS ONE 4:E4207-E4207(2009).
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; CP001275; ACM05425.1; -; Genomic_DNA.
DR RefSeq; WP_015922370.1; NC_011959.1.
DR AlphaFoldDB; B9L2L9; -.
DR STRING; 309801.trd_1421; -.
DR KEGG; tro:trd_1421; -.
DR eggNOG; COG0001; Bacteria.
DR HOGENOM; CLU_016922_1_5_0; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000000447; Chromosome.
DR GO; GO:0042286; F:glutamate-1-semialdehyde 2,1-aminomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR CDD; cd00610; OAT_like; 1.
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; IPR049704; Aminotrans_3_PPA_site.
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.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000313|EMBL:ACM05425.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}.
SQ SEQUENCE 472 AA; 52353 MW; 9B92B10DB9C09B9E CRC64;
MSTDRLLGDA YFAQSRQLFE RISRTIAGGE SSYARLKKGL ELCFDHGEGS HFWDIDGHEY
IDYSLGYGPL IFGHKPKRVI QAVIEAIERY GTISTFPYEL DAEVGELFTE LVPGVDLLRF
ANSGTEATMA AARLARAYTG RPKIVQMEGA YHGWADTHLW SSHPDVWRPQ LRPYSPRPIP
GSRGIPEVYG EALLIAQYND RESLERLFAE HGNEIAAVLV EPVQCNSGVI LPEPGYLEFL
REITRSYGAL LIFDEVITGF RLAPGGAQER LGVIPDIATY AKALGAGFPI AAFGGSREVM
QLEATNQVMH GGTYTANVVA LAAARAVLTE MKTRRDELWA VLNGFGERVR EGLREACEAA
GLRCIVQGIG PVWHIFFAKP DAPALDRIRN YREAHAYTSI DIYDRFNRAM LRRGVYFHPY
HLERWFISTA HSESDVQATL QAAHEAALEV AQSLREQPAA DPASLAMPGI AQ
//
