ID A0A0S9NG13_9BURK Unreviewed; 548 AA.
AC A0A0S9NG13;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Glutamate-1-semialdehyde 2,1-aminomutase {ECO:0000313|EMBL:KQP44214.1};
GN ORFNames=ASF44_28225 {ECO:0000313|EMBL:KQP44214.1};
OS Pseudorhodoferax sp. Leaf274.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=1736318 {ECO:0000313|EMBL:KQP44214.1, ECO:0000313|Proteomes:UP000051759};
RN [1] {ECO:0000313|EMBL:KQP44214.1, ECO:0000313|Proteomes:UP000051759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf274 {ECO:0000313|EMBL:KQP44214.1,
RC ECO:0000313|Proteomes:UP000051759};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQP44214.1, ECO:0000313|Proteomes:UP000051759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf274 {ECO:0000313|EMBL:KQP44214.1,
RC ECO:0000313|Proteomes:UP000051759};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
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}.
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:KQP44214.1}.
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DR EMBL; LMNA01000008; KQP44214.1; -; Genomic_DNA.
DR RefSeq; WP_056899523.1; NZ_LMNA01000008.1.
DR AlphaFoldDB; A0A0S9NG13; -.
DR STRING; 1736318.ASF44_28225; -.
DR OrthoDB; 5476440at2; -.
DR Proteomes; UP000051759; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 2.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 2.
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; 2.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000051759}.
SQ SEQUENCE 548 AA; 60424 MW; 77EB6571B573DC02 CRC64;
MNELTFLGGF GAAAVLALLP AASQRLALSR AKHRSLAGHS KLSRRVARKL PFYDFGRDRF
FDSDGAPAAV AAQREAGMAR LAAVFAQRFP KTLAMTEAAR EGIADLQFTS RYRVPFQYSR
VLRESLKMGA FVQESRGVQV TDLDGNAFYD LAGSYGVNLF GQDFYKSCIA EGSARVQDLG
PVLGSYHPAV LDNVRALRAI SGKDEVSFHM SGTEAVMQAV RLARYHTRRT HIVRFCGAYH
GWWDDVQPGI GNPVSAERTY TLRDMDERTL RVLASRRDIA CVLVNPLQAL HPNANAPSDS
ALVAGRAAPA FDRAAYTAWL HKLRAVCTAR GIVLVFDEVF LGFRLAPGGA QEYFGVQADM
VTYGKTLGGG LPVGVVCGPH RLMQRWREDR PADICFARGT FNAHPYVMGA MQVFLERLAT
PAVQAMYQDL DVTWEGRAAQ LNGLLEGAGL PVRVGGMSTV WAVGFTQASR YHWMLPYYLR
AQGLALSWVG TGRLIFSLNY GDAEFAEVAR RFVAGCQAMQ ADGWWWQDAG LSKKTIQRRI
LREMFGRA
//
