ID V6K2K9_STRNV Unreviewed; 463 AA.
AC V6K2K9;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Pyridoxal-dependent decarboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=M877_19375 {ECO:0000313|EMBL:EST26357.1};
OS Streptomyces niveus NCIMB 11891.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1352941 {ECO:0000313|EMBL:EST26357.1, ECO:0000313|Proteomes:UP000017971};
RN [1] {ECO:0000313|EMBL:EST26357.1, ECO:0000313|Proteomes:UP000017971}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 11891 {ECO:0000313|EMBL:EST26357.1,
RC ECO:0000313|Proteomes:UP000017971};
RX PubMed=24407644;
RA Flinspach K., Ruckert C., Kalinowski J., Heide L., Apel A.K.;
RT "Draft Genome Sequence of Streptomyces niveus NCIMB 11891, Producer of the
RT Aminocoumarin Antibiotic Novobiocin.";
RL Genome Announc. 2:e01146-e01113(2014).
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:EST26357.1}.
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DR EMBL; AWQW01000136; EST26357.1; -; Genomic_DNA.
DR AlphaFoldDB; V6K2K9; -.
DR STRING; 193462.BBN63_16015; -.
DR PATRIC; fig|1352941.4.peg.3956; -.
DR eggNOG; COG0076; Bacteria.
DR HOGENOM; CLU_011856_0_4_11; -.
DR Proteomes; UP000017971; Chromosome.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProt.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
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 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 Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382}.
FT MOD_RES 267
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 463 AA; 47419 MW; A1380EC1F8C15AAA CRC64;
MADTFGAARG TEALGRLTEL LAHGSADPAD PACAAHLHCP PLAVAVAADL AVSALNPSQD
SWDQAPAATV LETLLLEEMA GLVGYDPAEA AGVLTSGGTE SNLMGLMLAR DRVLGAATGR
QIELTGVPRA GAGGSLGSAA GARPRILASA AAHFSVQRAA ALLGLGEDAV IPVAVDSQLR
MKTGALTAAL ERCVERGQLP VAIVATAGTT DTGAIDPLRE CAELAARYGA WLHVDAAYGG
GALLSDRLAP LLDGIELADS VSLDWHKLGW QPAAAGIFLV RKSETYASLA RRAVYLNPAD
DEEAGYPSLL GLSLRTTRRA DAFKIAVTLR TLGREGLGRL VDACHELAVA GARAVAAHPR
LELHGQAGAG EPVLTAILFR YVPAASAGAS ADAEAVRADE VNAALRRRLL REGGAVVGRT
ELPGEGPGRV RLKLTLLNPH TTVVEVERLL AAVVAAGVAE ESA
//
