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
//