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Database: UniProt
Entry: A0A4R3KBR3_9BACI
LinkDB: A0A4R3KBR3_9BACI
Original site: A0A4R3KBR3_9BACI 
ID   A0A4R3KBR3_9BACI        Unreviewed;       266 AA.
AC   A0A4R3KBR3;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   27-MAR-2024, entry version 10.
DE   SubName: Full=4-amino-4-deoxychorismate lyase {ECO:0000313|EMBL:TCS80339.1};
GN   ORFNames=EDD72_1175 {ECO:0000313|EMBL:TCS80339.1};
OS   Tepidibacillus fermentans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Tepidibacillus.
OX   NCBI_TaxID=1281767 {ECO:0000313|EMBL:TCS80339.1, ECO:0000313|Proteomes:UP000295788};
RN   [1] {ECO:0000313|EMBL:TCS80339.1, ECO:0000313|Proteomes:UP000295788}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23802 {ECO:0000313|EMBL:TCS80339.1,
RC   ECO:0000313|Proteomes:UP000295788};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (MAR-2019) 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|RuleBase:RU004516};
CC   -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00009320,
CC       ECO:0000256|RuleBase:RU004106}.
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:TCS80339.1}.
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DR   EMBL; SMAB01000017; TCS80339.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4R3KBR3; -.
DR   OrthoDB; 9805628at2; -.
DR   Proteomes; UP000295788; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046394; P:carboxylic acid biosynthetic process; IEA:UniProt.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   CDD; cd00449; PLPDE_IV; 1.
DR   Gene3D; 3.30.470.10; -; 1.
DR   Gene3D; 3.20.10.10; D-amino Acid Aminotransferase, subunit A, domain 2; 1.
DR   InterPro; IPR001544; Aminotrans_IV.
DR   InterPro; IPR018300; Aminotrans_IV_CS.
DR   InterPro; IPR036038; Aminotransferase-like.
DR   InterPro; IPR043132; BCAT-like_C.
DR   InterPro; IPR043131; BCAT-like_N.
DR   PANTHER; PTHR42743; AMINO-ACID AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR42743:SF24; AMINODEOXYCHORISMATE LYASE; 1.
DR   Pfam; PF01063; Aminotran_4; 1.
DR   SUPFAM; SSF56752; D-aminoacid aminotransferase-like PLP-dependent enzymes; 1.
DR   PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:TCS80339.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU004516};
KW   Reference proteome {ECO:0000313|Proteomes:UP000295788}.
SQ   SEQUENCE   266 AA;  30521 MW;  E97234B89C580153 CRC64;
     MILYNGQMMN NNSSLFSSNV ILGTGIFETL TVYHKKAIDL NSHIDRLFFS LKFFNLYVEI
     SKQELISQVE YFIKHIDEKK VALRITVIQS TKNEPADIII SANHFPYQKE DYERGFKISR
     SSVIRHRSNP LLYHKTTNYL LNKLELEKAQ RKGYDEVIFL NEIGAITEGT RSNIFLVCNG
     NIYTPKTSCG LLEGVTRNKI INIAKKLGFN VIIDTIPNNF LETCDEAFLT SSLLGIMPIS
     QIENRKLNRS TFVITPILLN EINIEM
//
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