ID A0A0F0HJV7_9PSEU Unreviewed; 302 AA.
AC A0A0F0HJV7;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=1-aminocyclopropane-1-carboxylate deaminase {ECO:0000313|EMBL:KJK55096.1};
GN ORFNames=UK12_30755 {ECO:0000313|EMBL:KJK55096.1};
OS Saccharothrix sp. ST-888.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1427391 {ECO:0000313|EMBL:KJK55096.1, ECO:0000313|Proteomes:UP000033409};
RN [1] {ECO:0000313|EMBL:KJK55096.1, ECO:0000313|Proteomes:UP000033409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST-888 {ECO:0000313|EMBL:KJK55096.1,
RC ECO:0000313|Proteomes:UP000033409};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase
CC family. {ECO:0000256|ARBA:ARBA00008639}.
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:KJK55096.1}.
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DR EMBL; JYJF01000165; KJK55096.1; -; Genomic_DNA.
DR RefSeq; WP_045306487.1; NZ_JYJF01000165.1.
DR AlphaFoldDB; A0A0F0HJV7; -.
DR PATRIC; fig|1427391.3.peg.2319; -.
DR OrthoDB; 9801249at2; -.
DR Proteomes; UP000033409; Unassembled WGS sequence.
DR GO; GO:1901605; P:alpha-amino acid metabolic process; IEA:UniProt.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR027278; ACCD_DCysDesulf.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR PANTHER; PTHR43780; 1-AMINOCYCLOPROPANE-1-CARBOXYLATE DEAMINASE-RELATED; 1.
DR PANTHER; PTHR43780:SF2; 1-AMINOCYCLOPROPANE-1-CARBOXYLATE DEAMINASE-RELATED; 1.
DR Pfam; PF00291; PALP; 1.
DR PIRSF; PIRSF006278; ACCD_DCysDesulf; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR006278-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000033409}.
FT DOMAIN 3..295
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT ACT_SITE 69
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006278-1"
FT MOD_RES 42
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR006278-2"
SQ SEQUENCE 302 AA; 31187 MW; 9E63D26D794B94FD CRC64;
MLTPAALPTP LQVLADPALA RAGVELRLKR DDLAHPAVPG NKWRKLAPNL AQAVADGHAR
LLTFGGAYST HVRAVAAAAQ ALGLASVGVI RGEELAAAPR NWSLRAAEAA GMELEFVSRS
AYRGLVGGEH GEHGALLRRW GRCLVLPEGG SNALAVRGAA EIPAEIPALG ARDLLCCPVG
TGGTLAGIAA GLPDGARALG VAVLRGEGYL EGEVAGLHRA AYGREFGNWR IHHGHHGGGY
GKVPAEVESF AVEFERRHGV PVERRYVAKT LLAVHDLAAA GELAPGTRVT VVITGLPDPV
GG
//
