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Database: UniProt
Entry: A0A0J7YW14_STRVR
LinkDB: A0A0J7YW14_STRVR
Original site: A0A0J7YW14_STRVR 
ID   A0A0J7YW14_STRVR        Unreviewed;       388 AA.
AC   A0A0J7YW14;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=3-amino-5-hydroxybenzoic acid synthase {ECO:0000313|EMBL:KMS67846.1};
GN   ORFNames=ACM01_41235 {ECO:0000313|EMBL:KMS67846.1};
OS   Streptomyces viridochromogenes.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1938 {ECO:0000313|EMBL:KMS67846.1, ECO:0000313|Proteomes:UP000037432};
RN   [1] {ECO:0000313|EMBL:KMS67846.1, ECO:0000313|Proteomes:UP000037432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 3414 {ECO:0000313|EMBL:KMS67846.1,
RC   ECO:0000313|Proteomes:UP000037432};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KMS67846.1}.
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DR   EMBL; LFNT01000090; KMS67846.1; -; Genomic_DNA.
DR   RefSeq; WP_048586620.1; NZ_LFNT01000090.1.
DR   AlphaFoldDB; A0A0J7YW14; -.
DR   PATRIC; fig|1938.3.peg.9665; -.
DR   OrthoDB; 9804264at2; -.
DR   Proteomes; UP000037432; Unassembled WGS sequence.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
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   Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
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;  42565 MW;  A44381CFB5F4EE1F CRC64;
     MTDTVQRNLN FPEWPQYDDA EKTGLMRALE QGQWWRIGGQ EVELFEEEFA AYHGAPHALA
     VTSGTHALEL ALQVMGVGPG TEVIVPAFTF ISSSQAAQRL GAVAVPVDVD PATYCIDVRT
     TEAAITDRTR AIMPVHMAGV VADMDALEKL SADSGVGLLQ DAAHAHGAEW RGRRVGDLGS
     VAAFSFQNGK LMTAGEGGAV TFPEAEQYEL AFLRHSCGRP RTDRSYLHRT SGSNFRMNEF
     SASVLRAQLA RLDSQIETRE QRWPLLAELL SGIPGVEPQG GDARCTRNPH YMAMFRIPGI
     TEERRNAVVD ALIERGLPAF AAFRAVYRTA AFWEMAAPQE GVEDIARRCP HSEALTRDCV
     WLHHRTLLGT EEQMHAIADV VADVLGRS
//
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