ID Q7D3V3_AGRFC Unreviewed; 444 AA.
AC Q7D3V3;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 2.
DT 27-MAR-2024, entry version 102.
DE SubName: Full=Glutamate-1-semialdehyde aminotransferase {ECO:0000313|EMBL:AAK90498.2};
GN Name=atrB {ECO:0000313|EMBL:AAK90498.2};
GN OrderedLocusNames=Atu5124 {ECO:0000313|EMBL:AAK90498.2};
OS Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS (strain C58)).
OG Plasmid At {ECO:0000313|EMBL:AAK90498.2,
OG ECO:0000313|Proteomes:UP000000813}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=176299 {ECO:0000313|EMBL:AAK90498.2, ECO:0000313|Proteomes:UP000000813};
RN [1] {ECO:0000313|EMBL:AAK90498.2, ECO:0000313|Proteomes:UP000000813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970 {ECO:0000313|Proteomes:UP000000813};
RC PLASMID=Plasmid At {ECO:0000313|Proteomes:UP000000813};
RX PubMed=11743194; DOI=10.1126/science.1066803;
RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT "Genome sequence of the plant pathogen and biotechnology agent
RT Agrobacterium tumefaciens C58.";
RL Science 294:2323-2328(2001).
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; AE007872; AAK90498.2; -; Genomic_DNA.
DR RefSeq; NP_396057.2; NC_003064.2.
DR RefSeq; WP_010974388.1; NC_003064.2.
DR AlphaFoldDB; Q7D3V3; -.
DR EnsemblBacteria; AAK90498; AAK90498; Atu5124.
DR KEGG; atu:Atu5124; -.
DR PATRIC; fig|176299.10.peg.4813; -.
DR eggNOG; COG0001; Bacteria.
DR HOGENOM; CLU_016922_1_2_5; -.
DR OrthoDB; 9801052at2; -.
DR PhylomeDB; Q7D3V3; -.
DR BioCyc; AGRO:ATU5124-MONOMER; -.
DR Proteomes; UP000000813; Plasmid At.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; 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.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:AAK90498.2};
KW Plasmid {ECO:0000313|EMBL:AAK90498.2};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000000813};
KW Transferase {ECO:0000313|EMBL:AAK90498.2}.
SQ SEQUENCE 444 AA; 47314 MW; 4827865D998EF656 CRC64;
MLSSSNTPLT GPNDRQTSIA FFERASTVFP GGVTRATIEL DPHPIFVAYG EGAFVTDVDG
HRMLDLNNNF TTLIHGHAYP PITEAIAGLL RTGSCFANPM NHEIDLAELL VGRIPAVEQV
RFVASGTEAV MFAIKAARAT TGRVAIARVE GAYHGAYDWA EAGQHASSNT PCAAYPGMPA
SVIDDVVLLQ FNCPAELEQQ IAMNAGRLAA ILIDPMPSRA GLIEPTEEFI ATINKVAKQH
GIVIIADEVL NLRQGFAGAS ARYGLKPDLV TMGKIIGGGF PIGAVGGRRE IMSAFGKQGS
KAPLTQGGTF AANPVSMVAG RLAMEALTQD AFQRLEHMGN LVREGLRSRI ERHGANLSVT
GAASLFRIHA KKVAPVSYQD SIPTASEDVV LKLLRRHFAN NGILMPYGAA ASLSTPMTDN
DMGDIVSVFD DFLVNLDRHA WEAA
//
