ID A0A2N7XAX1_9BURK Unreviewed; 469 AA.
AC A0A2N7XAX1;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Aspartate aminotransferase family protein {ECO:0000313|EMBL:PMS38757.1};
GN ORFNames=C0Z20_02620 {ECO:0000313|EMBL:PMS38757.1};
OS Trinickia symbiotica.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Trinickia.
OX NCBI_TaxID=863227 {ECO:0000313|EMBL:PMS38757.1, ECO:0000313|Proteomes:UP000235777};
RN [1] {ECO:0000313|EMBL:PMS38757.1, ECO:0000313|Proteomes:UP000235777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPY 581 {ECO:0000313|EMBL:PMS38757.1,
RC ECO:0000313|Proteomes:UP000235777};
RA Estrada-de los Santos P., Palmer M., Chavez-Ramirez B., Beukes C.,
RA Steenkamp E.T., Hirsch A.M., Manyaka P., Maluk M., Lafos M., Crook M.,
RA Gross E., Simon M.F., Bueno dos Reis Junior F., Poole P.S., Venter S.N.,
RA James E.K.;
RT "Whole genome analyses suggest that Burkholderia sensu lato contains two
RT further novel genera in the rhizoxinica-symbiotica group Mycetohabitans
RT gen. nov., and Trinickia gen. nov.: implications for the evolution of
RT diazotrophy and nodulation in the Burkholderiaceae.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC ECO:0000256|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|RuleBase:RU000382}.
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:PMS38757.1}.
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DR EMBL; PNYC01000001; PMS38757.1; -; Genomic_DNA.
DR RefSeq; WP_018439249.1; NZ_PTIR01000002.1.
DR AlphaFoldDB; A0A2N7XAX1; -.
DR STRING; 863227.GCA_000373005_00733; -.
DR OrthoDB; 9803665at2; -.
DR Proteomes; UP000235777; Unassembled WGS sequence.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProt.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0019752; P:carboxylic acid metabolic process; 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; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11999:SF70; AROMATIC-L-AMINO-ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:PMS38757.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000235777};
KW Transferase {ECO:0000313|EMBL:PMS38757.1}.
FT MOD_RES 295
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 469 AA; 50553 MW; C7DA123E6D5EAAF6 CRC64;
MSQSSPFRPA LEHALDHALA HLDNLSRHSV AANATLESLR ARLGKPLGEE GVAADRVIDE
LVADTAGGIV GSAGGRFFGW VIGGALPAAL GADWLTSAWD QNAASYACAP AEAVVEEVCG
AWLKDLLRLP HDASFALTSG CQMAHLTALA AARHALLERR GWQVESDGLF GAPKIRVLSS
DQFHGSVTQA LRLLGMGTSA IQPLPSNEAG QLEAVTLEAA LRESPDTPTV VLLQAGDLNI
GAFDAYLQLI PLAHRYGAWV HIDGAFGLWV NASARYRHLL EGVEQADSWA TDGHKWLNVP
YDSGFAFVAH PDAHRNAMSH HASYVSYNEQ VREQKDWTPV WSRRGRGFAA YAALRELGRN
GVASLIERNC DAARALAYGI SALPGVVVVR EPQINQGLVR FLDPRPGATE QDHDARTDAV
TQSVLQTGEA LFSNTTWRGK RYMRISVCNW QTNDDDVARA IAAVASVVR
//
