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Database: UniProt
Entry: A0A094QCI3_9ACTN
LinkDB: A0A094QCI3_9ACTN
Original site: A0A094QCI3_9ACTN 
ID   A0A094QCI3_9ACTN        Unreviewed;       367 AA.
AC   A0A094QCI3;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Glutamate-1-semialdehyde 2,1-aminomutase {ECO:0000313|EMBL:KGA11976.1};
DE   Flags: Fragment;
GN   ORFNames=GM46_2520 {ECO:0000313|EMBL:KGA11976.1};
OS   actinobacterium acAcidi.
OC   Bacteria; Actinomycetota; Actinomycetes.
OX   NCBI_TaxID=1504320 {ECO:0000313|EMBL:KGA11976.1, ECO:0000313|Proteomes:UP000029305};
RN   [1] {ECO:0000313|EMBL:KGA11976.1, ECO:0000313|Proteomes:UP000029305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Ghai R., Mizuno C.M., Picazo A., Camacho A., Rodriguez-Valera F.;
RT   "Key roles for freshwater Actinobacteria revealed by deep metagenomic
RT   sequencing.";
RL   Submitted (MAY-2014) 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KGA11976.1}.
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DR   EMBL; JNSG01000020; KGA11976.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094QCI3; -.
DR   Proteomes; UP000029305; Unassembled WGS sequence.
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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}.
FT   NON_TER         367
FT                   /evidence="ECO:0000313|EMBL:KGA11976.1"
SQ   SEQUENCE   367 AA;  37343 MW;  5AE621197697EDB3 CRC64;
     MTIPLCDPNL CVSAGCTATV CIGKAIASNH TFYERSANVI PGGVNSSIRA FKSVGGEPYI
     VARGEGAHIV DVEGNRYIDL VQSYGAVILG HAHPAITAAL RDAAGDGTSF GAPTPREMKL
     AEAIRERVPS CERVRLMNSG TEATSTAVRL ARGATGRKRI ITFYGNFHGA TDALLAAGGS
     GIATLGIPGT AGVPEEAVAN TLVVPYNVVP EIGNDVAAVI VEPVAANMGV IAPAPGFLEG
     LRAACDKAGA LLIFDEVITG FRIGQGGAQA KYDVKPDITC FGKVIGGGLP IGAIGGSRAV
     MENLTPIGKV FHAGTLAGNP LATAAGLAAL NELTPDVYME LGARARALAT LLRDACSSAG
     IVAQFPV
//
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