ID A0A2C6DK09_9GAMM Unreviewed; 490 AA.
AC A0A2C6DK09;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Aspartate aminotransferase family protein {ECO:0000313|EMBL:PHI29033.1};
GN ORFNames=CRN84_06740 {ECO:0000313|EMBL:PHI29033.1};
OS Budvicia aquatica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Budviciaceae; Budvicia.
OX NCBI_TaxID=82979 {ECO:0000313|EMBL:PHI29033.1, ECO:0000313|Proteomes:UP000224974};
RN [1] {ECO:0000313|Proteomes:UP000224974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FDAARGOS_387 {ECO:0000313|Proteomes:UP000224974};
RA Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Tallon L.,
RA Sadzewicz L., Ott S., Zhao X., Nagaraj S., Vavikolanu K., Aluvathingal J.,
RA Nadendla S., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR602129-50, 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:PHI29033.1}.
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DR EMBL; PDDX01000001; PHI29033.1; -; Genomic_DNA.
DR RefSeq; WP_029095295.1; NZ_PDDX01000001.1.
DR AlphaFoldDB; A0A2C6DK09; -.
DR STRING; 1111728.GCA_000427805_02897; -.
DR OrthoDB; 9803665at2; -.
DR Proteomes; UP000224974; 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 CDD; cd06450; DOPA_deC_like; 1.
DR Gene3D; 3.90.1150.170; -; 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 PANTHER; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:PHI29033.1};
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:UP000224974};
KW Transferase {ECO:0000313|EMBL:PHI29033.1}.
FT MOD_RES 307
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 490 AA; 53600 MW; E63CBF59FB997617 CRC64;
MSKLNPILAA SAHSTEAYQQ AIAQSSQAVV QWLQQPEMYQ GKTVAELRER ITLDFNPQGL
GNQAAIERAV EYFLKDSLSV HHPQCVAHLH CPSLVISQAA EVLINATNQS MDSWDQSPSA
TIIEMKLIEW LRTQVGYQPG DAGVFTSGGT QSNLMGLMLA RDAFFARQGH SVQQDGLVGN
LTKIKVLCSE NAHFSVQKNM ALMGLGYQSV TLVKTDYFGR LDFNDLSEKV AQAQANGEQI
LAIVATAGTT DAGAIDPLRA IATLAAQHQI WVHVDAAWGG ALLLSEKYRD YLDGIELVDS
ITLDFHKQFF QTISCGAFLL KEARHYELMR YQAAYLNSEF DEAQGVPNLV SKSLQTTRRF
DALKLWMGLE ALGQKQYAEI IDHGVTLAQQ VAHYISQQAS LELVMQPQLA SVLFRYRSQQ
LATGSDAAIG LLNQKIGDAL LASGLANVGV TEFNGITCLK MTLLNPTVTL DDIKALLALV
DSTAQRLLTV
//
