ID H3NJP1_9LACT Unreviewed; 455 AA.
AC H3NJP1;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EHR36854.1};
GN ORFNames=HMPREF9708_01080 {ECO:0000313|EMBL:EHR36854.1};
OS Facklamia languida CCUG 37842.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Facklamia.
OX NCBI_TaxID=883113 {ECO:0000313|EMBL:EHR36854.1, ECO:0000313|Proteomes:UP000006190};
RN [1] {ECO:0000313|EMBL:EHR36854.1, ECO:0000313|Proteomes:UP000006190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 37842 {ECO:0000313|EMBL:EHR36854.1,
RC ECO:0000313|Proteomes:UP000006190};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Heiman D., Howarth C., Larimer J., Lui A.,
RA MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Facklamia languida CCUG 37842.";
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:EHR36854.1}.
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DR EMBL; AGEG01000013; EHR36854.1; -; Genomic_DNA.
DR RefSeq; WP_006309260.1; NZ_JH601133.1.
DR AlphaFoldDB; H3NJP1; -.
DR STRING; 883113.HMPREF9708_01080; -.
DR PATRIC; fig|883113.3.peg.1073; -.
DR eggNOG; COG0076; Bacteria.
DR HOGENOM; CLU_011856_0_4_9; -.
DR OrthoDB; 9803665at2; -.
DR Proteomes; UP000006190; 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: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: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};
KW Reference proteome {ECO:0000313|Proteomes:UP000006190}.
FT MOD_RES 291
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 455 AA; 50471 MW; 431278E1F528E9B7 CRC64;
MDNKFWNYED EAVELTLDWA KNRTVTGSDS KTTALSANEL RNKVGDTITE DGIGPKKALD
IFETLNKATR SSDDPMNFAY IPCAPTKAAV AFDEVVSAAN VFGGIWENGA GAIYAENQVV
DWLKENLNWP EEAIGTFVSG GTHGNLSALA CARENAKNKW KTEERYPKGR PSDGYKLIIS
KDTHSSVRTI AKVLDVDVLV AETDENGRMT GEAVRTLIDE NEGVFAVVAT TGTTNTGTID
DVQSISKVCQ EYDIWLHIDG AYGGAGILAP SARDLYNGIE NADSFIVDPH KWLFAPYDSC
CLIYRNPKNV YQTFSQHAEY LEGVDHSQSN PSDMAIHLSR RTRGLPLWYS LVTYGSKKYS
DAIEKCLDNA KKCAQAIKES EHLELVMEPT LSVVAFKRKT WELKDYQKWS NELALEGRIL
CLPSSIDGEV ILRLAFLNPN TDIDKVINII LETTK
//
