ID A0A0T2YGK7_9BURK Unreviewed; 553 AA.
AC A0A0T2YGK7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Glutamate-1-semialdehyde 2,1-aminomutase {ECO:0000313|EMBL:KRB98118.1};
GN ORFNames=ASE11_13890 {ECO:0000313|EMBL:KRB98118.1};
OS Hydrogenophaga sp. Root209.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Hydrogenophaga.
OX NCBI_TaxID=1736490 {ECO:0000313|EMBL:KRB98118.1, ECO:0000313|Proteomes:UP000050889};
RN [1] {ECO:0000313|Proteomes:UP000050889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root209 {ECO:0000313|Proteomes:UP000050889};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB98118.1, ECO:0000313|Proteomes:UP000050889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root209 {ECO:0000313|EMBL:KRB98118.1,
RC ECO:0000313|Proteomes:UP000050889};
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 -!- 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:KRB98118.1}.
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DR EMBL; LMIE01000031; KRB98118.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T2YGK7; -.
DR STRING; 1736490.ASE11_13890; -.
DR Proteomes; UP000050889; 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; 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 4: Predicted;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..553
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006662903"
SQ SEQUENCE 553 AA; 61552 MW; 07E3E684938B67CF CRC64;
MCQMSTAWVL SASALAASFP FVHQRIQLSR AKHRSLAGHS LMAKRLARWL PGYSYTEDRF
FAADGAPPGV AAQRKAAFHR LSAQLNAKAP QGLALTAQLR AGLPDLQFTG RYRVPFQFSE
LVRQHLALPA FWAHAEGVGL TDIDGNHCFD LTGSYGVNVF GVDFYKATMA EGSELGAALG
PVLGGYHPCV ADNVERLKAI SGLDAVSFHM SGTEAVMQAV RLARFHTGRK KLVRFCGAYH
GWWDDVQPGP GNPMPPGHTY TLKDMDERSL NVLRTRRDIA CVLVNPLQAL HPNRNAPGDS
TVMTARQSDP ADQKAYAQWL ARLREVCTAR GIALIFDEVF VGFRLARGGA QEHYGVQADL
VTYGKTLGGG LPVGVVCGKA AWMQRFRPER PADICFARGT FNAHPYVMGA MNAFLRRLET
PEVQAIYEGL DERWQNHLTR FNHALQQADV PVRVAGLSSI WTVNFTAPSR YHWMLQFYLR
EQGLALSWVG TGRMVFSLNY SEQDMAEVLR RLVLACQRMT EDGWWANPTG ATARDLQRQV
FKEMWRARWS GRA
//
