ID A0A1Q9LSL3_9PSEU Unreviewed; 450 AA.
AC A0A1Q9LSL3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Aspartate aminotransferase family protein {ECO:0000313|EMBL:OLR95008.1};
GN ORFNames=BJP25_08595 {ECO:0000313|EMBL:OLR95008.1};
OS Actinokineospora bangkokensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinokineospora.
OX NCBI_TaxID=1193682 {ECO:0000313|EMBL:OLR95008.1, ECO:0000313|Proteomes:UP000186040};
RN [1] {ECO:0000313|EMBL:OLR95008.1, ECO:0000313|Proteomes:UP000186040}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=44EHW {ECO:0000313|EMBL:OLR95008.1,
RC ECO:0000313|Proteomes:UP000186040};
RA Greule A., Intra B., Flemming S., Rommel M.G., Panbangred W., Bechthold A.;
RT "The Draft Genome Sequence of Actinokineospora bangkokensis 44EHWT reveals
RT the biosynthetic pathway of antifungal compounds Thailandins with unusual
RT extender unit butylmalonyl-CoA.";
RL Submitted (OCT-2016) 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:OLR95008.1}.
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DR EMBL; MKQR01000005; OLR95008.1; -; Genomic_DNA.
DR RefSeq; WP_075973241.1; NZ_MKQR01000005.1.
DR AlphaFoldDB; A0A1Q9LSL3; -.
DR STRING; 1193682.BJP25_08595; -.
DR OrthoDB; 3335676at2; -.
DR Proteomes; UP000186040; Unassembled WGS sequence.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
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 InterPro; IPR021115; Pyridoxal-P_BS.
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.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:OLR95008.1};
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:UP000186040};
KW Transferase {ECO:0000313|EMBL:OLR95008.1}.
FT MOD_RES 278
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 450 AA; 45569 MW; EBB2175085BFB132 CRC64;
MTRSPAALAA ADAVRPLVAI ALDAVAAGAA ARGGPLPPGG PGGLGAGADP VPERGVGAEA
ALRALVARFA AGAADPADPW CAAHLHCPPL AVAAAADLVA SVLNPSMDSW DQAPAASELE
AELTRGIARL CHPGAAAPDA LVTTGGTESN LLGLLLARES RGRVTVVCGR NAHHSVTRAA
WLLGLPAPVP VDCAGDRVDP ASLAAVLARV DGPAAVVATL GTTNTGALDP LPEIEAAAVA
AGAWLHVDAA YAGGLLFSGR RALPSLARAD SVALDLHKFG WQPIAAGLLV CRDAGVLRAL
HTTADYLSAD DDTEAGLPDL LGRSLRTSRR PDAFKIAVTL RALGRAGIGE LVDHCCDTAA
GVAAAARAHP ALRVWGEPSL STVLFRPADT PDAVVAQVRR DLLRSGRAVV GRADLDGELW
LKLTILHPHA TAETYAPLLD LVADAARRAA
//
