ID A0A0E9MP64_9SPHN Unreviewed; 472 AA.
AC A0A0E9MP64;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Putative aromatic L-amino acid decarboxylase {ECO:0000313|EMBL:GAO39552.1};
GN ORFNames=SCH01S_34_00050 {ECO:0000313|EMBL:GAO39552.1};
OS Sphingomonas changbaiensis NBRC 104936.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1219043 {ECO:0000313|EMBL:GAO39552.1, ECO:0000313|Proteomes:UP000033202};
RN [1] {ECO:0000313|EMBL:GAO39552.1, ECO:0000313|Proteomes:UP000033202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 104936 {ECO:0000313|EMBL:GAO39552.1,
RC ECO:0000313|Proteomes:UP000033202};
RA Katano-Makiyama Y., Hosoyama A., Hashimoto M., Noguchi M., Tsuchikane K.,
RA Ohji S., Yamazoe A., Ichikawa N., Kimura A., Fujita N.;
RT "Whole genome shotgun sequence of Sphingomonas changbaiensis NBRC 104936.";
RL Submitted (APR-2015) 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|ARBA:ARBA00009533, 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:GAO39552.1}.
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DR EMBL; BBWU01000034; GAO39552.1; -; Genomic_DNA.
DR RefSeq; WP_046348377.1; NZ_BBWU01000034.1.
DR AlphaFoldDB; A0A0E9MP64; -.
DR STRING; 1219043.SCH01S_34_00050; -.
DR OrthoDB; 9803665at2; -.
DR Proteomes; UP000033202; Unassembled WGS sequence.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006520; P:amino 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; IPR010977; Aromatic_deC.
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; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR PANTHER; PTHR11999:SF177; MIP05841P; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR PRINTS; PR00800; YHDCRBOXLASE.
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:UP000033202}.
FT MOD_RES 296
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 472 AA; 50032 MW; 04EB45C85123D354 CRC64;
MSDRARLQAL AAAARPLEPD HAERAALMAA VQAHAERYLD ALPDAPTYRV GPVAAPGFPD
APAGIEEALA FISDQIEQRG IATASGRFMG YIPGGGLFHS ALGDFLADVS NKYAGFASAA
PGAVRLENAC VRWLADAIGY PAEAAGALTS GGSIANLSAI VAARDALDQD GGGAVYVAPT
AHHCVDKALK IAGRGAAPRR TLALDANHRI ALESLEAALE QDRRDGVRPW LVVASAGTVD
TGSVDPLTGI AELCARYGAW MHVDGAYGGL FMLCPEGRAV LGGIERADTL AVDPHKTLFL
PYGTGAVLAR DGRTLRASFS AAADYLTPFA ALEDISPADL SPELTRHFRA LRLWLPIQLA
GLDAFRAAQS EKIGLARYMH ARLSELPGWE TGAAPDLSVF AFRYRPGKGD IDAFNERLTK
RIQDDGRVFL SSTRIYGRLH LRAAILSFRA HLEHVDEAID ALQSAARALE AE
//
