ID   E3I3F0_RHOVT            Unreviewed;       516 AA.
AC   E3I3F0;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:ADP72598.1};
GN   OrderedLocusNames=Rvan_3416 {ECO:0000313|EMBL:ADP72598.1};
OS   Rhodomicrobium vannielii (strain ATCC 17100 / ATH 3.1.1 / DSM 162 / LMG
OS   4299).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Hyphomicrobiaceae; Rhodomicrobium.
OX   NCBI_TaxID=648757 {ECO:0000313|EMBL:ADP72598.1, ECO:0000313|Proteomes:UP000001399};
RN   [1] {ECO:0000313|Proteomes:UP000001399}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17100 / ATH 3.1.1 / DSM 162 / LMG 4299
RC   {ECO:0000313|Proteomes:UP000001399};
RX   PubMed=21705585; DOI=10.1128/JB.05453-11;
RG   US DOE Joint Genome Institute;
RA   Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT   "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL   J. Bacteriol. 193:4567-4568(2011).
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}.
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DR   EMBL; CP002292; ADP72598.1; -; Genomic_DNA.
DR   RefSeq; WP_013420956.1; NC_014664.1.
DR   AlphaFoldDB; E3I3F0; -.
DR   STRING; 648757.Rvan_3416; -.
DR   KEGG; rva:Rvan_3416; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_011856_0_4_5; -.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000001399; Chromosome.
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; 3.90.1150.10; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001399}.
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         321
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   516 AA;  56792 MW;  E28006950D92412C CRC64;
     MASEKLTEIS QHPSPSEDAG ADVADYLLGS DLSKLRGWVE ARSASFLRSA DAGERSPIRR
     VREKFRSCEV PDTAMALDDY LSLLDQDVLP HCSSLASPRY LGHMTSPIPG FLPELGRLVQ
     TLNQNVVKME TSGSLTFVER QVLGMLHKET YGFDTAFYDR RVQDRDSTLG LFASGGTIAN
     LTALRAAKQR ASVHAGGGAR MAVIGSELMH YSFAKGADLM GLELRRVPVD EQNRMLPAAL
     EREIEACEAE GVTVAALIAI AGTTEFGSVD PLASICRLGQ ARNIHVHVDA AWGGGFLLSP
     RNRHILAGIE LADTVTIDGH KQLMVPLGCG MLFFRDPEVS KTIMHHAPYA VRPNSEDQGR
     FTLEGTRPAT AIYVHAALHL IGKSVYDALF SASLERTRIM ARHIEGMPEF ELTSRPDMNI
     LTYRYIPEAM RGTTPGPADN HRISRFNVAL QRAQRDKGDS FVSRTFRPVS RHGDEPLALL
     RAVLLNPRTT EDDILFLLRD QVGIARELEN SPAFHE
//