ID B3PSH7_RHIE6 Unreviewed; 447 AA.
AC B3PSH7;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=L-2,4-diaminobutyrate decarboxylase protein {ECO:0000313|EMBL:ACE91675.1};
DE EC=4.1.1.- {ECO:0000313|EMBL:ACE91675.1};
GN Name=rhbB {ECO:0000313|EMBL:ACE91675.1};
GN OrderedLocusNames=RHECIAT_CH0002723 {ECO:0000313|EMBL:ACE91675.1};
OS Rhizobium etli (strain CIAT 652).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=491916 {ECO:0000313|EMBL:ACE91675.1, ECO:0000313|Proteomes:UP000008817};
RN [1] {ECO:0000313|EMBL:ACE91675.1, ECO:0000313|Proteomes:UP000008817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIAT 652 {ECO:0000313|EMBL:ACE91675.1,
RC ECO:0000313|Proteomes:UP000008817};
RA Gonzalez V., Acosta J.L., Santamaria R.I., Bustos P.,
RA Hernandez-Gonzalez I.L., Fernandez J.L., Diaz R., Flores M., Mora J.,
RA Palacios R., Davila G.;
RT "Genome diversity and DNA divergence of Rhizobium etli.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC ECO:0000256|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|RuleBase:RU000382}.
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DR EMBL; CP001074; ACE91675.1; -; Genomic_DNA.
DR AlphaFoldDB; B3PSH7; -.
DR KEGG; rec:RHECIAT_CH0002723; -.
DR eggNOG; COG0076; Bacteria.
DR HOGENOM; CLU_011856_0_4_5; -.
DR Proteomes; UP000008817; 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; PTHR11999:SF70; AROMATIC-L-AMINO-ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE 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}.
FT MOD_RES 264
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 447 AA; 47286 MW; F5A67C62D474DC26 CRC64;
MPSSDYAASL AVFDEPLSAA GSDMLDVIRQ LSDGAEPGLH ATTGPRFFGW VIGGSHPVGV
AADFLTSAWG QNAGNHVAAP AAAAVETIAA RWLLDLLKLP AESSVGFVTG ATVANFTCLA
AARGEVLRMV GWNADADGLF GAPEITVLIG DDAHTTVFSA LQFLGLGHDR VLRLPTDAMG
RIDPAALPGA LDAITGPLIA ILQAGQINTG AFDDFDRLIP PLKAKGAWVH VDGAFGLWAQ
ASAKVSHLSR GIEGADSWAT DGHKWLQTPY DCGYAIVRDE LAHRRAMTIA ASYLPLAGEG
ERDPSHYVPE LSRRARGFAT WAMLKHFGRN GVEALIDQCC ASARLMADRL AREPGIAILN
EVALNQLVVR FGVDCPDDEG DALTRKAIEK IQSDGILFAG GAKWRRRDVL RLSVTNFQTT
SDQARLAAES IIAAYKSVSD SAGHDSG
//
