ID A0A1I2FEN0_9BACI Unreviewed; 294 AA.
AC A0A1I2FEN0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=4-amino-4-deoxychorismate lyase {ECO:0000313|EMBL:SFF03872.1};
GN ORFNames=SAMN05192532_11154 {ECO:0000313|EMBL:SFF03872.1};
OS Alteribacillus iranensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alteribacillus.
OX NCBI_TaxID=930128 {ECO:0000313|EMBL:SFF03872.1, ECO:0000313|Proteomes:UP000199516};
RN [1] {ECO:0000313|EMBL:SFF03872.1, ECO:0000313|Proteomes:UP000199516}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23995 {ECO:0000313|EMBL:SFF03872.1,
RC ECO:0000313|Proteomes:UP000199516};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FONT01000011; SFF03872.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2FEN0; -.
DR STRING; 930128.SAMN05192532_11154; -.
DR OrthoDB; 9805628at2; -.
DR Proteomes; UP000199516; 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 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:SF23; 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:SFF03872.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU004516};
KW Reference proteome {ECO:0000313|Proteomes:UP000199516}.
SQ SEQUENCE 294 AA; 34275 MW; DC0BDF8ECF7CFA94 CRC64;
MYVYINDEIK KASDARLSVF EHGFMYGLGL FETFRIYDGH PFLLDDHFER LERGLQEMNI
SWRYNREEVF QNLKKLLEAN QWKNAYVRYN IAAGKGELGL AVDPYQEPTE IIYMKPLDYA
SKTGKNQKQG RILEVRRNTP ETSERLKSHH FLNSMLGKWE LRGEEGVEGI FLTECGHIAE
GTVSNVFWVK NHTIYTPSLQ TGILPGITRS FIIQLAKKLS FHVRVGKFPL QHLMEADEAF
VTNSIQEIVS LTAINDKQFE KGKDSLTDVL LDKYRQYCHH LWKSEDIFNK MNEI
//