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Database: UniProt
Entry: A0A430BCW4_9SPHN
LinkDB: A0A430BCW4_9SPHN
Original site: A0A430BCW4_9SPHN 
ID   A0A430BCW4_9SPHN        Unreviewed;       485 AA.
AC   A0A430BCW4;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 10.
DE   SubName: Full=Amino acid decarboxylase {ECO:0000313|EMBL:RSU46455.1};
GN   ORFNames=BRX43_15600 {ECO:0000313|EMBL:RSU46455.1};
OS   Sphingomonas sp. S-NIH.Pt15_0812.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1920129 {ECO:0000313|EMBL:RSU46455.1, ECO:0000313|Proteomes:UP000287772};
RN   [1] {ECO:0000313|EMBL:RSU46455.1, ECO:0000313|Proteomes:UP000287772}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S-NIH.Pt15_0812 {ECO:0000313|EMBL:RSU46455.1,
RC   ECO:0000313|Proteomes:UP000287772};
RA   Johnson R.C., Deming C., Conlan S., Zellmer C., Michelin A., Lee-Lin S.-Q.,
RA   Thomas P.J., Park M., Weingarten R.A., Less J., Dekker J.P., Frank K.M.,
RA   Musser K.A., Mcquiston J.R., Henderson D.K., Lau A.F., Palmore T.N.,
RA   Segre J.A.;
RT   "Genomic and Epidemiologic Investigation to Identify Sphingomonas koreensis
RT   Point Sources in an Indolent Hospital Outbreak.";
RL   Submitted (JUN-2018) 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 Orn/Lys/Arg decarboxylase class-I family.
CC       {ECO:0000256|ARBA:ARBA00010671}.
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:RSU46455.1}.
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DR   EMBL; QLJH01000028; RSU46455.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A430BCW4; -.
DR   OrthoDB; 9761189at2; -.
DR   Proteomes; UP000287772; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   Gene3D; 3.90.100.10; Orn/Lys/Arg decarboxylase, C-terminal domain; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR000310; Orn/Lys/Arg_deCO2ase_major_dom.
DR   InterPro; IPR008286; Prn/Lys/Arg_de-COase_C.
DR   InterPro; IPR036633; Prn/Lys/Arg_de-COase_C_sf.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR43277; ARGININE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43277:SF4; ARGININE DECARBOXYLASE; 1.
DR   Pfam; PF01276; OKR_DC_1; 1.
DR   Pfam; PF03711; OKR_DC_1_C; 1.
DR   SUPFAM; SSF55904; Ornithine decarboxylase C-terminal domain; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000287772}.
FT   DOMAIN          7..300
FT                   /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT                   attachment site"
FT                   /evidence="ECO:0000259|Pfam:PF01276"
FT   DOMAIN          406..465
FT                   /note="Orn/Lys/Arg decarboxylase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03711"
SQ   SEQUENCE   485 AA;  51034 MW;  16D698B13F6583A6 CRC64;
     MDQKSAPLVE ALAAIERKPL IGFGAPGHNQ GAVIPSGLRS LLGRRTFRAD VLTPKGLDDR
     TEGTLALQRA HEIAAEAWNA DFCRFVTGGS TQSLHTVMAA VAGPGDTILV AANAHKAERT
     YALAAGLDIG IVPVQVDQGW DIEHGVTPDA LRESLARHPA AKAFVLVSPT YYGVTSDVAA
     LATLCHEHGI PLIVDAAWGG AFAFCEALPD DPLTKGADAA VYSAHKTMGA LAQGSIIVAK
     GDLLDRQRLW MAYELFETTS PSVPILASLD ATRRDHALRG EQMWNDVLAL ADHARGTIAA
     IAPLRVLGRE DMPAGADLDR TKVLIDVSAL GVSGYAIDDW LFAEHRISVG LSDARHLLAV
     ISLGTTRSDI RALQRGLADL VARLTADPAM LPTLATTPGV GTLSVEMAMA GPDAIAGPVE
     MVRYEEAGGR IAAEMIAPAP PGVPRLVPGQ RISKAHVAWL VAQREAGAFI MDPVDPTDAT
     IRVVA
//
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