ID   B9Y425_9FIRM            Unreviewed;       402 AA.
AC   B9Y425;
DT   14-APR-2009, integrated into UniProtKB/TrEMBL.
DT   14-APR-2009, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   SubName: Full=Putative diaminopropionate ammonia-lyase {ECO:0000313|EMBL:EEF69283.1};
GN   ORFNames=HOLDEFILI_00556 {ECO:0000313|EMBL:EEF69283.1};
OS   Holdemania filiformis DSM 12042.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Erysipelotrichaceae; Holdemania.
OX   NCBI_TaxID=545696 {ECO:0000313|EMBL:EEF69283.1, ECO:0000313|Proteomes:UP000005950};
RN   [1] {ECO:0000313|EMBL:EEF69283.1, ECO:0000313|Proteomes:UP000005950}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12042 {ECO:0000313|EMBL:EEF69283.1,
RC   ECO:0000313|Proteomes:UP000005950};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEF69283.1, ECO:0000313|Proteomes:UP000005950}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12042 {ECO:0000313|EMBL:EEF69283.1,
RC   ECO:0000313|Proteomes:UP000005950};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Holdemania filiformis DSM 12042.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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:EEF69283.1}.
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DR   EMBL; ACCF01000040; EEF69283.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9Y425; -.
DR   STRING; 545696.HOLDEFILI_00556; -.
DR   eggNOG; COG1171; Bacteria.
DR   HOGENOM; CLU_021802_8_0_9; -.
DR   OrthoDB; 34584at2; -.
DR   Proteomes; UP000005950; Unassembled WGS sequence.
DR   GO; GO:0008838; F:diaminopropionate ammonia-lyase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   CDD; cd00640; Trp-synth-beta_II; 1.
DR   Gene3D; 3.40.50.1100; -; 3.
DR   InterPro; IPR010081; DiNH2opropionate_NH3_lyase.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   NCBIfam; TIGR01747; diampropi_NH3ly; 1.
DR   PANTHER; PTHR42937; -; 1.
DR   PANTHER; PTHR42937:SF1; DIAMINOPROPIONATE AMMONIA-LYASE; 1.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000313|EMBL:EEF69283.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT   DOMAIN          59..359
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   402 AA;  43896 MW;  E5F00A5D56407630 CRC64;
     MAADEAERRS GINWKNGKRR KHMDKIQMAK GKLARGPLPA MFNSEQYRQV EAFHQTLKQY
     APTPLINLSK LAEKLGIQAI LVKDESHRFG LNAFKALGAS YAVHRYLEQH PHTQPVFVTT
     TDGNHGKGVA WAALQVGCRS EIFMPKGTVA SRVQAIEALG NAKVTVTEWG YDDTVRWTRD
     YAQRNGYVLV QDTVLEDYHE IPQNIVLGYT TMIREVVQQI EEQALAKPTH VFLQAGVGSM
     AGGVLGWLAD TLKAEMPVAS IIEATDSACV FASCPQGKLV SKAGITPTIM AGLNCGEVNP
     DLFPVLRDYA AFYFACADEV TEAGMRQYAD PLAGDTAIVA GESGAVGLGL LLSLCQDRQY
     EAMKQALGLD EHSVVLLLNT EGATDPDDYR RVVGRDPQTV GQ
//