ID J2WSR9_9PSED Unreviewed; 449 AA.
AC J2WSR9;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Adenosylmethionine-8-amino-7-oxononanoate aminotransferase {ECO:0000313|EMBL:EJM19138.1};
GN ORFNames=PMI22_02980 {ECO:0000313|EMBL:EJM19138.1};
OS Pseudomonas sp. GM21.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1144325 {ECO:0000313|EMBL:EJM19138.1, ECO:0000313|Proteomes:UP000007292};
RN [1] {ECO:0000313|EMBL:EJM19138.1, ECO:0000313|Proteomes:UP000007292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM21 {ECO:0000313|EMBL:EJM19138.1,
RC ECO:0000313|Proteomes:UP000007292};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJM19138.1}.
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DR EMBL; AKJS01000087; EJM19138.1; -; Genomic_DNA.
DR RefSeq; WP_007945898.1; NZ_AKJS01000087.1.
DR AlphaFoldDB; J2WSR9; -.
DR PATRIC; fig|1144325.3.peg.2892; -.
DR eggNOG; COG0161; Bacteria.
DR Proteomes; UP000007292; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
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; PTHR42684; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42684:SF1; BETA-ALANINE--PYRUVATE AMINOTRANSFERASE; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW ECO:0000313|EMBL:EJM19138.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EJM19138.1}.
SQ SEQUENCE 449 AA; 48600 MW; 30537824D078CFFF CRC64;
MNLPENAPSS LASQLKLDAH WMPYTANRNF QRDPRLIVGA EGSWLIDDKG RKVYDSLSGL
WTCGAGHTRK EIQEAVSKQL GTLDYSPGFQ YGHPLSFQLA EKITDLTPGN LNHVFFTDSG
SECADTAVKM VRAYWRLKGQ ATKTKMIGRA RGYHGVNIAG TSLGGVNGNR KMFGQAMMDV
DHLPHTLLAS NAYSRGVPEL GGIALADELL KLIELHDASN IAAVFVEPLA GSAGVLVPPQ
GYLKRLREIC DQHNILLVFD EVITGFGRTG SMFGADSFGV TPDLMCIAKQ VTNGAIPMGA
VIASSEIYQT FMNQATPEYA VEFPHGYTYS AHPVACAAGL AALDLLQKEN LVQSVAEVAP
HFENALHGLK GSKNIIDIRN YGLAGAIQIA PRDGDAIVRP FEAGMALWKA GFYVRFGGDT
LQFGPTFNSK PQDLDRLFDA VGEVLNKID
//
