ID Q6LL34_PHOPR Unreviewed; 489 AA.
AC Q6LL34;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=Hypothetical amino acid decarboxylase {ECO:0000313|EMBL:CAG22150.1};
GN Name=SMB21414 {ECO:0000313|EMBL:CAG22150.1};
GN OrderedLocusNames=PBPRB0277 {ECO:0000313|EMBL:CAG22150.1};
OS Photobacterium profundum (strain SS9).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=298386 {ECO:0000313|EMBL:CAG22150.1, ECO:0000313|Proteomes:UP000000593};
RN [1] {ECO:0000313|Proteomes:UP000000593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1253 / SS9 {ECO:0000313|Proteomes:UP000000593};
RX PubMed=15746425; DOI=10.1126/science.1103341;
RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA Bartlett D.H., Valle G.;
RT "Life at depth: Photobacterium profundum genome sequence and expression
RT analysis.";
RL Science 307:1459-1461(2005).
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; CR378675; CAG22150.1; -; Genomic_DNA.
DR RefSeq; WP_011220367.1; NC_006371.1.
DR AlphaFoldDB; Q6LL34; -.
DR STRING; 298386.PBPRB0277; -.
DR KEGG; ppr:PBPRB0277; -.
DR eggNOG; COG0076; Bacteria.
DR HOGENOM; CLU_011856_0_4_6; -.
DR Proteomes; UP000000593; Chromosome 2.
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; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000000593}.
FT MOD_RES 296
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 489 AA; 53028 MW; 0E3A2731ACFD638C CRC64;
MSHKFNQYRQ LLNSSLDHAV DYLESLPERP IDKQSNSESL RKAIGGTLPI TGTAPDQVIQ
KLVTDVEEGL IGSGGPRYFG YAIGGSFPVA LAADWLVSAW DQNVPYYVSS PATSIVEETA
AEWMLDLLHL PKTAGVGFTS GAQEAIYTAL ITARNSLLEK AGWDVAANGL YGAPRIHVVM
SDQIHSTIKR ALSMIGIGLK DIKTIPTDQN LRIIPDTLPA ILAECDGPTL VCAQAGCIDS
GAFDPFDEIA SSIEAHPNAW LHVDGAIGLW SAASDTQKHL LKGIEKADSW DTDGHKWFNM
PYDSGMVIVK DASLLAKAMG GNNMGDYLTD AIAKPDRNAI NFGISASRRA RGVPVYATIK
SLGKEGIQAH LDNCCTLAKR MADKLRNVDG ITILNDVVSN RFSAQFGKGD DAFRDQLTAR
IVYQLQQDGF CYPSTSGYKG LKTMLFSVLS CHTTAQDIDA SAEKIIEIYH MELEKIQEEH
TQSDATLCS
//
