ID F3B902_9FIRM Unreviewed; 477 AA.
AC F3B902;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGG84852.1};
GN ORFNames=HMPREF9477_00579 {ECO:0000313|EMBL:EGG84852.1};
OS Lachnospiraceae bacterium 2_1_46FAA.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=742723 {ECO:0000313|EMBL:EGG84852.1, ECO:0000313|Proteomes:UP000018451};
RN [1] {ECO:0000313|EMBL:EGG84852.1, ECO:0000313|Proteomes:UP000018451}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2_1_46FAA {ECO:0000313|EMBL:EGG84852.1,
RC ECO:0000313|Proteomes:UP000018451};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA Ambrose C., Allen-Vercoe E., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Lachnospiraceae bacterium 2_1_46FAA.";
RL Submitted (DEC-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|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:EGG84852.1}.
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DR EMBL; ADLB02000007; EGG84852.1; -; Genomic_DNA.
DR AlphaFoldDB; F3B902; -.
DR STRING; 742723.HMPREF9477_00579; -.
DR eggNOG; COG0076; Bacteria.
DR HOGENOM; CLU_011856_0_4_9; -.
DR OrthoDB; 9803665at2; -.
DR Proteomes; UP000018451; Unassembled WGS sequence.
DR GO; GO:0004058; F:aromatic-L-amino-acid decarboxylase 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; 3.90.1150.170; -; 1.
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 InterPro; IPR021115; Pyridoxal-P_BS.
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.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 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:UP000018451}.
FT MOD_RES 294
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 477 AA; 53360 MW; 0E44638441E7364D CRC64;
MINSENILNS AQLEEAIENF VHEFCAEKHD IHSQKVTWYT SEGQIEKIKQ IGISKDGRPV
DEVIAEMSKE VYRYRGDANH PRFFGFVPGP ASSVSWLGDI MTSAYNIHAG GSKLAPMVNC
IEQEVLRWLC EQVGFTKNPG GVFVSGGSMA NITALTAARD CKLNDENLHL GVAYVSDQTH
SSVAKGLRII GIPNSRIRSV ATNSAFQMDT DMLKEMIAKD KENGLIPFVV IGTAGTTNTG
SIDPLEEIAD ICANNNMWFH IDGAYGASVL LSPKYKHLLK GTELADSISW DAHKWLFQTY
GCAMVLVKDI KHLFHSFHVN PEYLKDVEGD MEHINTWDIG MELTRPARGL KLWLTLQVLG
TRLIGSAIEH GFQLAEWAEE ALNELDNWEV ISKAQLAMLN FRYAADDLTD EQMDLLNEKV
SEKIVESGYA AVFTTILNGK KVLRICALHP ETTRDDMRTT IHLLDTYARE LHEKMKK
//