ID   Q8KUH2_ACTPA            Unreviewed;       388 AA.
AC   Q8KUH2;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   24-JAN-2024, entry version 63.
DE   SubName: Full=3-amino-5-hydroxybenzoate synthase {ECO:0000313|EMBL:AAM54102.1};
GN   Name=asm24 {ECO:0000313|EMBL:AAM54102.1};
OS   Actinosynnema pretiosum subsp. auranticum.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Actinosynnema.
OX   NCBI_TaxID=42198 {ECO:0000313|EMBL:AAM54102.1};
RN   [1] {ECO:0000313|EMBL:AAM54102.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 31565 {ECO:0000313|EMBL:AAM54102.1};
RA   Yu T.-W., Bai L., Clade D., Hoffmann D., Toelzer S., Trinh K.Q., Xu J.,
RA   Moss S.J., Leistner E., Floss H.G.;
RL   Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AAM54102.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 31565 {ECO:0000313|EMBL:AAM54102.1};
RX   PubMed=12060743; DOI=10.1073/pnas.092697199;
RA   Yu T.W., Bai L., Clade D., Hoffmann D., Toelzer S., Trinh K.Q., Xu J.,
RA   Moss S.J., Leistner E., Floss H.G.;
RT   "The biosynthetic gene cluster of the maytansinoid antitumor agent
RT   ansamitocin from Actinosynnema pretiosum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:7968-7973(2002).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC       {ECO:0000256|RuleBase:RU004508}.
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DR   EMBL; AF453501; AAM54102.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8KUH2; -.
DR   CDD; cd00616; AHBA_syn; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR000653; DegT/StrS_aminotransferase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR30244:SF34; DTDP-4-AMINO-4,6-DIDEOXYGALACTOSE TRANSAMINASE; 1.
DR   PANTHER; PTHR30244; TRANSAMINASE; 1.
DR   Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR   PIRSF; PIRSF000390; PLP_StrS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW   ECO:0000256|RuleBase:RU004508}.
FT   ACT_SITE        190
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         190
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   388 AA;  42202 MW;  E9BEA4F42D14E626 CRC64;
     MHLKAPQKLE FPAWPQFDST EREALLRTLD SGRWWRITGD EVVSFEREFA QAHGARHALA
     VTTGTHALEL VLEVMGAGPG TEVIVPAFTF ISSSQAAQRL GAVVVPVDVD PDTYCVDPAA
     VRAAITERTR AIMPVHMAGQ LADMDALRAL SAETGVPLLQ DAAHAHGARW RGEPLGALGS
     IAAFSFQNGK LMTAGEGGAV LLPDGDQHEE AFLRHACGRP LADRAYHHRT AGSNFRMNEF
     SAALLRAQLG RLQQQTDVRE RHWPVLSRLL AEVPGVVPQG TDPRCDRNPH YMAMFQVPGI
     GEERRARLVD ALVERGVPAF AGFRAIYRTA AFWERAAPDT TVDALARACP VTEALSSDCV
     WLHHRVLLGA EEQMPLVAEA VACALEEA
//