ID A0A0M8W5R5_9NOCA Unreviewed; 336 AA.
AC A0A0M8W5R5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=1-aminocyclopropane-1-carboxylate deaminase {ECO:0000313|EMBL:KOV79074.1};
DE EC=3.5.99.7 {ECO:0000313|EMBL:KOV79074.1};
GN ORFNames=ADL03_37915 {ECO:0000313|EMBL:KOV79074.1};
OS Nocardia sp. NRRL S-836.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=1519492 {ECO:0000313|EMBL:KOV79074.1, ECO:0000313|Proteomes:UP000037746};
RN [1] {ECO:0000313|Proteomes:UP000037746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL S-836 {ECO:0000313|Proteomes:UP000037746};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate +
CC NH4(+); Xref=Rhea:RHEA:16933, ChEBI:CHEBI:15377, ChEBI:CHEBI:16763,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:58360; EC=3.5.99.7;
CC Evidence={ECO:0000256|ARBA:ARBA00001132};
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:KOV79074.1}.
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DR EMBL; LGDY01000138; KOV79074.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8W5R5; -.
DR STRING; 1519492.ADL03_37915; -.
DR PATRIC; fig|1519492.3.peg.8094; -.
DR Proteomes; UP000037746; Unassembled WGS sequence.
DR GO; GO:0008660; F:1-aminocyclopropane-1-carboxylate deaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:1901605; P:alpha-amino acid metabolic process; IEA:UniProt.
DR GO; GO:0009310; P:amine catabolic process; IEA:InterPro.
DR CDD; cd06449; ACCD; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR027278; ACCD_DCysDesulf.
DR InterPro; IPR005965; ACP_carboxylate_deaminase.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR01274; ACC_deam; 1.
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 Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KOV79074.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR006278-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000037746}.
FT DOMAIN 15..320
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT ACT_SITE 80
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006278-1"
FT MOD_RES 53
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR006278-2"
SQ SEQUENCE 336 AA; 35588 MW; 1B846BB7FB59DBD0 CRC64;
MEHPPGGTVN RYPLLFGPSP IHRLDRLTTH LGGAAIWAKR EDCNSGLAYG GNKTRKLEYL
VADAIATGCD TLVSIGGIQS NHTRQVAAAA ARAGLKAVLV QESWVDWTDT GHDRVGNILL
SRMMGADVRL VSAEFGIGIK PAWEQAIADV RAAGGTPYPI PAGASDHPLG GMGFATWADE
VRQQEAQLGI FFDTIIVCSV TGSTQAGMVA GFAGDPHRRV LGIDASAKPA ETLAQITRIA
HNTAKLRNTT VSEEDILLDD RFHAGVYGLP DDTTLDAMRL GAQLEGMITD PVYEGKSLAG
LIHLVTSGEI DRNSTVLYAH LGGQPALNAY SSLFPA
//
