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Database: UniProt
Entry: A0A1H3ZUH3_ALKAM
LinkDB: A0A1H3ZUH3_ALKAM
Original site: A0A1H3ZUH3_ALKAM 
ID   A0A1H3ZUH3_ALKAM        Unreviewed;       255 AA.
AC   A0A1H3ZUH3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=aminodeoxychorismate lyase {ECO:0000256|ARBA:ARBA00035676};
DE            EC=4.1.3.38 {ECO:0000256|ARBA:ARBA00035676};
GN   ORFNames=SAMN04488051_102367 {ECO:0000313|EMBL:SEA27357.1};
OS   Alkalimonas amylolytica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alkalimonas.
OX   NCBI_TaxID=152573 {ECO:0000313|EMBL:SEA27357.1, ECO:0000313|Proteomes:UP000198773};
RN   [1] {ECO:0000313|EMBL:SEA27357.1, ECO:0000313|Proteomes:UP000198773}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.3430 {ECO:0000313|EMBL:SEA27357.1,
RC   ECO:0000313|Proteomes:UP000198773};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-amino-4-deoxychorismate = 4-aminobenzoate + H(+) + pyruvate;
CC         Xref=Rhea:RHEA:16201, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17836, ChEBI:CHEBI:58406; EC=4.1.3.38;
CC         Evidence={ECO:0000256|ARBA:ARBA00035576};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 4-
CC       aminobenzoate from chorismate: step 2/2.
CC       {ECO:0000256|ARBA:ARBA00035633}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00009320}.
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DR   EMBL; FNRM01000002; SEA27357.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H3ZUH3; -.
DR   STRING; 152573.SAMN04488051_102367; -.
DR   OrthoDB; 9805628at2; -.
DR   Proteomes; UP000198773; Unassembled WGS sequence.
DR   GO; GO:0008696; F:4-amino-4-deoxychorismate lyase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd01559; ADCL_like; 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; IPR017824; Aminodeoxychorismate_lyase_IV.
DR   InterPro; IPR001544; Aminotrans_IV.
DR   InterPro; IPR036038; Aminotransferase-like.
DR   InterPro; IPR043132; BCAT-like_C.
DR   InterPro; IPR043131; BCAT-like_N.
DR   NCBIfam; TIGR03461; pabC_Proteo; 1.
DR   PANTHER; PTHR42743; AMINO-ACID AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR42743:SF2; AMINODEOXYCHORISMATE LYASE; 1.
DR   Pfam; PF01063; Aminotran_4; 1.
DR   SUPFAM; SSF56752; D-aminoacid aminotransferase-like PLP-dependent enzymes; 1.
PE   3: Inferred from homology;
KW   Folate biosynthesis {ECO:0000256|ARBA:ARBA00022909};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:SEA27357.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198773}.
SQ   SEQUENCE   255 AA;  28403 MW;  D15329F47723C1A6 CRC64;
     MQPGIPIGDR SFQFGDGIFT TIRVRAGVAE YWPQHLARLQ QGVARLGFVE PDWQQLTNQV
     QQAISAPEQV LKVVISRGHA GRGYSPLGVN GPDTYISTAE LPDFRLQRQQ GIRLGVARLQ
     LGCQPLLAGL KHNNRLEQVL LKQELATTDW DDLLVLDQRG FVTEAIAANV FFYRAGRWLT
     PVLDQAGVAG VMRQVLLEHL QAEQVQWTLD ELQGIEALFC CNALCGILPV HTFLEKPLQL
     APVQQLQQEF ACFVA
//
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