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Database: UniProt
Entry: A0A161XI68_9NOCA
LinkDB: A0A161XI68_9NOCA
Original site: A0A161XI68_9NOCA 
ID   A0A161XI68_9NOCA        Unreviewed;       553 AA.
AC   A0A161XI68;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Pyridoxal-dependent decarboxylase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AWN90_32285 {ECO:0000313|EMBL:KZM73338.1};
OS   Nocardia terpenica.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=455432 {ECO:0000313|EMBL:KZM73338.1, ECO:0000313|Proteomes:UP000076512};
RN   [1] {ECO:0000313|EMBL:KZM73338.1, ECO:0000313|Proteomes:UP000076512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 0406 {ECO:0000313|EMBL:KZM73338.1,
RC   ECO:0000313|Proteomes:UP000076512};
RA   Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA   Babar A., Rosenke K.;
RL   Submitted (APR-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:KZM73338.1}.
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DR   EMBL; LWGR01000007; KZM73338.1; -; Genomic_DNA.
DR   RefSeq; WP_067590510.1; NZ_KV411304.1.
DR   AlphaFoldDB; A0A161XI68; -.
DR   STRING; 455432.AWN90_32285; -.
DR   OrthoDB; 3335676at2; -.
DR   Proteomes; UP000076512; 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:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
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; PTHR42735; -; 1.
DR   PANTHER; PTHR42735:SF4; TYROSINE DECARBOXYLASE; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
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:UP000076512}.
FT   MOD_RES         349
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   553 AA;  59527 MW;  876FCCC51C671020 CRC64;
     MDTGERLRRI VADYRSWRQR CGAPTDGWGE GPLAGYTRPA VDELLTELSA NLSHESTPWA
     APLYLAHMTG EIPESVALAY FCAMLYNPNN VVPEASPVTT RLEDEVAADL CRLIGYRPGE
     GWAHLCSGGH AANYEAIWMA RNLRAIPYAV AETPVTHHLV RGRTAAELAN LPVQQVLALL
     SAATRLGADS QVLATARRLR RTGEIPAATL LASANAHYAW SKCADLLALR EFGTIPTDHR
     HAIDVAALRD EVVQLADAGR PIAAVVACVG SSGEGSVDDL PAIIELRDDL ERTRGIGFHL
     HVDAAYGGYF RSMWLDETGG FMPVDPSDPV AAALRSLPAA DTVTVDPHKN AHAPYPAGAI
     VIRDRALCVT VGTDIGSYFA DGQQDPRMPY APYTLEGGRP GAAAAGVWAL HRLYPLDRTG
     LGAVLAARRS AARRWSAHVD RLPAATTTTG QPVRLFSCFE PDLAIVNIGI AGPTVDDDNA
     GRLIRTLAGR PDPAWKSRLW LSTNRLIIDG RPQWTLRSCL MNDLTSAEIT EAGMSLLHAL
     QAVLVEQAVD PPE
//
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