ID   A0A2M9IZ91_9ACTN        Unreviewed;       434 AA.
AC   A0A2M9IZ91;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Lipopolysaccharide biosynthesis protein RfbH {ECO:0000313|EMBL:PJM99950.1};
GN   ORFNames=CG740_27095 {ECO:0000313|EMBL:PJM99950.1};
OS   Streptomyces sp. CB01201.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2020324 {ECO:0000313|EMBL:PJM99950.1, ECO:0000313|Proteomes:UP000231916};
RN   [1] {ECO:0000313|Proteomes:UP000231916}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB01201 {ECO:0000313|Proteomes:UP000231916};
RA   Pan G., Xu Z., Guo Z., Ma M., Yang D., Zhou H., Gansemans Y., Zhu X.,
RA   Zhao L.-X., Jiang Y., Cheng J., van Nieuwerburgh F., Suh J.W., Duan Y.,
RA   Shen B.;
RT   "Discovery of the Leinamycin Family of Natural Products by Mining
RT   Actinobacterial Genomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 114:0-0(2017).
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:PJM99950.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; NNBJ01000014; PJM99950.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2M9IZ91; -.
DR   OrthoDB; 5342089at2; -.
DR   Proteomes; UP000231916; 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|RuleBase:RU004508}.
SQ   SEQUENCE   434 AA;  48194 MW;  770747BDC3C3761D CRC64;
     MTSDAKALVL EQVREYHRQQ QPEHFVPGVT PILSSGAVLD EEDRIALVEA ALELRIAAGA
     YARRFESRFA RHIGVRKAHL VNSGSSANLL ALSALTSPRL GEQRLRPGDE VITVAGGFPT
     TVNPIIQNGL TPVFVDLELG TYNTTAERVR AAISDRTRAI MIAHTLGNPY EAAEIQQLAT
     DHELFLVEDN CDAVGSTYQG RMTGTFGDLA TVSFYPAHHI TTGEGGCVLT KNLELARIVE
     SFRDWGRDCW CEPGEDNTCL KRFDYQLGDL PKGYDHKYIF SHIGYNLKAT DLQGALALSQ
     LKKLPAFGEA RRRNWQRLRD GLADVPGLLL PSATPGSDPS WFGFVITVLP DATYTRRDLI
     AFLEDRRIGT RRLFGGNLTR HPAYLDTPHR VSGDLRNCDI ITEQSFWIGV YPGITEEMTD
     YMRESIVEFV AKNG
//