ID I0AJS2_IGNAJ Unreviewed; 447 AA.
AC I0AJS2;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Glutamate-1-semialdehyde aminotransferase {ECO:0000313|EMBL:AFH49229.1};
GN Name=hemL {ECO:0000313|EMBL:AFH49229.1};
GN OrderedLocusNames=IALB_1521 {ECO:0000313|EMBL:AFH49229.1};
OS Ignavibacterium album (strain DSM 19864 / JCM 16511 / NBRC 101810 /
OS Mat9-16).
OC Bacteria; Ignavibacteriota; Ignavibacteria; Ignavibacteriales;
OC Ignavibacteriaceae; Ignavibacterium.
OX NCBI_TaxID=945713 {ECO:0000313|EMBL:AFH49229.1, ECO:0000313|Proteomes:UP000007394};
RN [1] {ECO:0000313|EMBL:AFH49229.1, ECO:0000313|Proteomes:UP000007394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19864 / JCM 16511 / NBRC 101810 / Mat9-16
RC {ECO:0000313|Proteomes:UP000007394};
RX PubMed=22661972; DOI=10.3389/fmicb.2012.00185;
RA Liu Z., Frigaard N.-U., Vogl K., Iino T., Ohkuma M., Overmann J.,
RA Bryant D.A.;
RT "Complete genome of Ignavibacterium album, a metabolically versatile,
RT flagellated, facultative anaerobe from the phylum Chlorobi.";
RL Front. Microbiol. 3:185-185(2012).
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; CP003418; AFH49229.1; -; Genomic_DNA.
DR RefSeq; WP_014560382.1; NC_017464.1.
DR AlphaFoldDB; I0AJS2; -.
DR STRING; 945713.IALB_1521; -.
DR GeneID; 78243191; -.
DR KEGG; ial:IALB_1521; -.
DR PATRIC; fig|945713.3.peg.1521; -.
DR eggNOG; COG0001; Bacteria.
DR HOGENOM; CLU_016922_1_4_10; -.
DR OrthoDB; 1286826at2; -.
DR Proteomes; UP000007394; 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:AFH49229.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000007394};
KW Transferase {ECO:0000313|EMBL:AFH49229.1}.
SQ SEQUENCE 447 AA; 50174 MW; 56DC3C21C3344691 CRC64;
MPNKVEFNKD YPVITKSDEY YKIALELIPA QTQTLAKGPG QNIKGVAPKY LQRGKGSHVW
DVDGNEYLDY TMAVGPLSLG YAYDKVDDAI REQLKDGITF SLMHPLEVEV AQLINKVVPN
AESIRYSKVG ADVTTAAVRL ARAYTGRNKV LCCGYHGWHD WYIAVTDRNK GIPQSIQDLS
YTFNYNDIQS VIDSIDEDTA CVILEPFVFE EPKDNFLHKL RDICTENGTL LIFDEMWTGF
RVAVGGAQEY FGVKADLACF SKAVANGMPI SILTGKKEIM QLLEKDVFFF TTFGGEALSL
AAVKATVTEI IEKNVPAYLA KQGRKLKDGY NTIANKLGMD YTKCSGFDCR TIITFDAEKS
GCNPLEMKSL VQQEMIKRGI LWGGFHNMSF SHTDDDIDYT LKAYEDVLPI LKKAVEEKNV
KAYLRGEPVE PVFRRVGNFN MKPKVKK
//
