ID A0A0S2JZZ2_9GAMM Unreviewed; 417 AA.
AC A0A0S2JZZ2;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase {ECO:0000256|ARBA:ARBA00015416};
DE AltName: Full=Glutamate-1-semialdehyde aminotransferase {ECO:0000256|ARBA:ARBA00031365};
GN ORFNames=PP2015_1096 {ECO:0000313|EMBL:ALO41612.1};
OS Pseudoalteromonas phenolica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=161398 {ECO:0000313|EMBL:ALO41612.1, ECO:0000313|Proteomes:UP000061457};
RN [1] {ECO:0000313|EMBL:ALO41612.1, ECO:0000313|Proteomes:UP000061457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 12086 {ECO:0000313|EMBL:ALO41612.1,
RC ECO:0000313|Proteomes:UP000061457};
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) 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; CP013187; ALO41612.1; -; Genomic_DNA.
DR RefSeq; WP_058029339.1; NZ_CP013187.1.
DR AlphaFoldDB; A0A0S2JZZ2; -.
DR STRING; 161398.PP2015_1096; -.
DR KEGG; pphe:PP2015_1096; -.
DR PATRIC; fig|161398.10.peg.1116; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000061457; Chromosome I.
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; 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 Aminotransferase {ECO:0000313|EMBL:ALO41612.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000061457};
KW Transferase {ECO:0000313|EMBL:ALO41612.1}.
SQ SEQUENCE 417 AA; 45460 MW; CF6D5AD502AF793E CRC64;
MNNQPLSFTQ SQKLQSQGEQ VIAGFTQSMM KKPEQFSPGA FPVYLAGGEG AVVTDVDGNQ
YIDFICGLAA NTLGHNHPVV TKAILDNLSN GLIHSLPTPV EVKTAQTLVD VIPGAEMVRF
FKTGADANSA AVRLARHVTG RDEIMTVGYN GWHDQYMFDT PGVPSAIASL THRMPLFTPA
DEPKIIEKIA NRKDQLAVVL LSVPYNRVLE KAFLQELRET CSEHGVVLVF DEVVTGFRLA
PGGAQEYFGV NADLVTLSKG IAAGMPLSAV AGCSKLMSRI NELQVSTTFG GEMLSLEVCD
AVIKEYKRTD FTSYIAKLGS ILKSEVNQIS EQLGTPLRVV GYDAIPMFLF AKNPEEHVKF
AIPFLAQMAK RGILMRREVN FISGAHTMEQ INDTITAVKA SLIEMQSEGV FDIKENT
//
