ID   G7ZBA9_AZOL4            Unreviewed;       419 AA.
AC   G7ZBA9;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=2,3-diaminopropionate ammonia-lyase {ECO:0000313|EMBL:CBS88562.1};
DE            EC=4.3.1.15 {ECO:0000313|EMBL:CBS88562.1};
GN   Name=dpaL {ECO:0000313|EMBL:CBS88562.1};
GN   OrderedLocusNames=AZOLI_p10273 {ECO:0000313|EMBL:CBS88562.1};
OS   Azospirillum lipoferum (strain 4B).
OG   Plasmid AZO_p1 {ECO:0000313|EMBL:CBS88562.1,
OG   ECO:0000313|Proteomes:UP000005667}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=862719 {ECO:0000313|EMBL:CBS88562.1, ECO:0000313|Proteomes:UP000005667};
RN   [1] {ECO:0000313|Proteomes:UP000005667}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4B {ECO:0000313|Proteomes:UP000005667};
RC   PLASMID=Plasmid AZO_p1 {ECO:0000313|Proteomes:UP000005667};
RX   PubMed=22216014; DOI=10.1371/journal.pgen.1002430;
RA   Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G.,
RA   Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H., Robertson J.S.,
RA   Barbe V., Calteau A., Rouy Z., Mangenot S., Prigent-Combaret C.,
RA   Normand P., Boyer M., Siguier P., Dessaux Y., Elmerich C., Condemine G.,
RA   Krishnen G., Kennedy I., Paterson A.H., Gonzalez V., Mavingui P.,
RA   Zhulin I.B.;
RT   "Azospirillum genomes reveal transition of bacteria from aquatic to
RT   terrestrial environments.";
RL   PLoS Genet. 7:E1002430-E1002430(2011).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR   EMBL; FQ311869; CBS88562.1; -; Genomic_DNA.
DR   RefSeq; WP_014188020.1; NC_016585.1.
DR   AlphaFoldDB; G7ZBA9; -.
DR   KEGG; ali:AZOLI_p10273; -.
DR   HOGENOM; CLU_021802_8_0_5; -.
DR   OrthoDB; 34584at2; -.
DR   Proteomes; UP000005667; Plasmid AZO_p1.
DR   GO; GO:0008838; F:diaminopropionate ammonia-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   CDD; cd00640; Trp-synth-beta_II; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
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:CBS88562.1}; Plasmid {ECO:0000313|EMBL:CBS88562.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT   DOMAIN          51..386
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   419 AA;  44406 MW;  DF5EABF4B5B70A09 CRC64;
     MPHQAVSPSS CLPRLHSNPR ADHERAYGPS ERAILSRAAF EEAMAEIGAW PGYAPTPLRS
     LPGLAREAGI DRIWYKDESA RFALGSFKAL GGAYAVLRLL AREVTARVPG VPVTALDLVV
     GRYARVTRTL TVTTATDGNH GRSVAWGAQV FGCNCVVYVP AACSPGRRAA IEAYGARVVV
     IDGSYDDAVR RAAADAAEQG WFVVSDTSYT GYMDVPRDVM QGYTVMVEEA ISQLPASERP
     THVFVQGGVG SLPAAVCGHL WESWGRQRPR FVVVEPHNAD CLYQSAVAGR PMRSEGDLDT
     VMAGLACGEV SLLAWAILER GADDFLTIPD EGAVTAMRKL AEGKHGGRPI VAGESGVAGL
     AGLLCAAAHE DVRLALGLAP DARVLVFGTE GATDPEVYER IVGRSPEMVA EDPVSAAGR
//