ID H1G0Z8_9GAMM Unreviewed; 462 AA.
AC H1G0Z8;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Aromatic-L-amino-acid decarboxylase {ECO:0000313|EMBL:EHQ51485.1};
GN ORFNames=ECTPHS_02264 {ECO:0000313|EMBL:EHQ51485.1};
OS Ectothiorhodospira sp. PHS-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Ectothiorhodospira.
OX NCBI_TaxID=519989 {ECO:0000313|EMBL:EHQ51485.1, ECO:0000313|Proteomes:UP000005314};
RN [1] {ECO:0000313|EMBL:EHQ51485.1, ECO:0000313|Proteomes:UP000005314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHS-1 {ECO:0000313|EMBL:EHQ51485.1,
RC ECO:0000313|Proteomes:UP000005314};
RA Saltikov C.W., Zargar K., Conrad A., Bernick D., Lowe T.M., Stolc V.,
RA Hoeft S., Oremland R.S., Stolz J.;
RT "ArxA, a new clade of arsenite oxidase within the DMSO family of molybdenum
RT oxidoreductases.";
RL Submitted (JAN-2012) 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:EHQ51485.1}.
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DR EMBL; AGBG01000003; EHQ51485.1; -; Genomic_DNA.
DR RefSeq; WP_008931052.1; NZ_AGBG01000003.1.
DR AlphaFoldDB; H1G0Z8; -.
DR STRING; 519989.ECTPHS_02264; -.
DR PATRIC; fig|519989.5.peg.454; -.
DR eggNOG; COG0076; Bacteria.
DR OrthoDB; 9803665at2; -.
DR Proteomes; UP000005314; 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; 1.20.1340.10; dopa decarboxylase, N-terminal domain; 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:SF70; AROMATIC-L-AMINO-ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 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}.
FT MOD_RES 294
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 462 AA; 51059 MW; B4FA5A5BB9A5EC51 CRC64;
MNHDDLRQWS KRAADWTHEY HNSLRDRPVR AQTRPGDIAA RLPETAPEQP DPLETIFEDF
TRIVPEGMTH WQHPRFFAYF PGNAAPASML AEQLANGMAA QAMLWQTSPA ATEMETVMIG
WLRDALGLAP HFTGTIHDTA TIATLSAILT MREKALAWKG NSAGLAAQPR LRLYASTQVH
SSIDKAVRIA GIGQDNLVKI PTDAHHAMDT AALDSAIRAD LAAGRRPAGV ILCVGATGIG
ASDRLQDAIT VAKTHGLTTH VDAAWAGSAM ICPEFRHLWA GIDGADSIVF NPHKWLGMQM
DCSIQFLADP VPQVRTLGLR PDYLETLGQS EITNYNEWTV PLGRRFRALK IWFTLRAYGL
EGLRRRIRNH IAWSEALATA IASLPDVEII TPPALSLFSF ALKDGNAATE ALLTRINDHG
QVYLTQTRHQ DRFVIRVQVG QFDCTREDVM TVYQVVRDLL SG
//
