ID A0A090WAG4_9FLAO Unreviewed; 377 AA.
AC A0A090WAG4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Histidine decarboxylase {ECO:0000313|EMBL:GAL64497.1};
GN ORFNames=JCM19300_4592 {ECO:0000313|EMBL:GAL64497.1};
OS Algibacter lectus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Algibacter.
OX NCBI_TaxID=221126 {ECO:0000313|EMBL:GAL64497.1, ECO:0000313|Proteomes:UP000029644};
RN [1] {ECO:0000313|EMBL:GAL64497.1, ECO:0000313|Proteomes:UP000029644}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 19300 {ECO:0000313|EMBL:GAL64497.1,
RC ECO:0000313|Proteomes:UP000029644};
RA Takatani N., Nakanishi M., Meirelles P., Mino S., Suda W., Oshima K.,
RA Hattori M., Ohkuma M., Hosokawa M., Miyashita K., Thompson F.L., Niwa A.,
RA Sawabe T., Sawabe T.;
RT "Draft Genome Sequences of Marine Flavobacterium Algibacter lectus Strains
RT SS8 and NR4.";
RL Genome Announc. 2:e01168-14(2014).
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|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:GAL64497.1}.
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DR EMBL; BBNQ01000019; GAL64497.1; -; Genomic_DNA.
DR RefSeq; WP_042506313.1; NZ_FOLN01000014.1.
DR AlphaFoldDB; A0A090WAG4; -.
DR OrthoDB; 9803665at2; -.
DR Proteomes; UP000029644; Unassembled WGS sequence.
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; PTHR46101; -; 1.
DR PANTHER; PTHR46101:SF2; SERINE 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:UP000029644}.
FT MOD_RES 229
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 377 AA; 42728 MW; 1FFDA96010913A8D CRC64;
MNTNPDLIID SLLTQLVKDK EKVLGYPVAQ DFDYSRLNEF LKYPINNVGD PFEENTYKVQ
THEMECEVVE FFAELFRADP KNHWGYVTNG GSESNLYGLY LARELYPKAM VYFSESTHYS
VKKNIHLLNI PSITIRSQEN GEIDYEDLEN TLQFNRHKPA IILTTFGTTM MEAKDDVSKV
KKILKKLAIQ DHYIHCDAAL SGSYGAFIEP RIPFDFKDGA DSISISGHKF IGSPFPSGVI
ITKRSLRDRI ARGISYIGSL DTTITGSRNG HSPLFLWYAI KKMGIEGLAK RFQHSLETAE
YCKNELIKQG IKAWTNPGSI TVVFPKVSDA IKGKWQLATD DDITHIICMP NVTKSQIDEF
VKDIVLEKST KEEVAVF
//
