ID   SNAA_STRPR              Reviewed;         422 AA.
AC   P54991;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Pristinamycin IIA synthase subunit A;
DE            Short=PIIA synthase subunit A;
GN   Name=snaA;
OS   Streptomyces pristinaespiralis.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=38300;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SP92;
RX   PubMed=7665509; DOI=10.1128/jb.177.18.5206-5214.1995;
RA   Blanc V., Lagneaux D., Didier P., Gil P., Lacroix P., Crouzet J.;
RT   "Cloning and analysis of structural genes from Streptomyces
RT   pristinaespiralis encoding enzymes involved in the conversion of
RT   pristinamycin IIB to pristinamycin IIA (PIIA): PIIA synthase and
RT   NADH:riboflavin 5'-phosphate oxidoreductase.";
RL   J. Bacteriol. 177:5206-5214(1995).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-19 AND 365-384.
RX   PubMed=7665508; DOI=10.1128/jb.177.18.5199-5205.1995;
RA   Thibaut D., Ratet N., Bisch D., Faucher D., Debussche L., Blanche F.;
RT   "Purification of the two-enzyme system catalyzing the oxidation of the D-
RT   proline residue of pristinamycin IIB during the last step of pristinamycin
RT   IIA biosynthesis.";
RL   J. Bacteriol. 177:5199-5205(1995).
CC   -!- FUNCTION: Catalyzes the oxidation of the proline residue of
CC       pristinamycin IIB (PIIB) to pristinamycin IIA (PIIA).
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC   -!- SUBUNIT: Heterodimer of two subunits, SnaA and SnaB.
CC   -!- SIMILARITY: Belongs to the NtaA/SnaA/DszA monooxygenase family.
CC       {ECO:0000305}.
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; U21215; AAA83563.1; -; Genomic_DNA.
DR   RefSeq; WP_005321872.1; NZ_CP011340.1.
DR   AlphaFoldDB; P54991; -.
DR   SMR; P54991; -.
DR   STRING; 38300.SPRI_0185; -.
DR   PRIDE; P54991; -.
DR   OMA; DMFTVGH; -.
DR   OrthoDB; 1591714at2; -.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   CDD; cd01095; Nitrilotriacetate_monoxgenase; 1.
DR   Gene3D; 3.20.20.30; -; 1.
DR   InterPro; IPR011251; Luciferase-like_dom.
DR   InterPro; IPR036661; Luciferase-like_sf.
DR   InterPro; IPR016215; NTA_MOA.
DR   Pfam; PF00296; Bac_luciferase; 1.
DR   PIRSF; PIRSF000337; NTA_MOA; 1.
DR   SUPFAM; SSF51679; SSF51679; 1.
DR   TIGRFAMs; TIGR03860; FMN_nitrolo; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Flavoprotein; FMN; Monooxygenase;
KW   Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:7665508"
FT   CHAIN           2..422
FT                   /note="Pristinamycin IIA synthase subunit A"
FT                   /id="PRO_0000072000"
FT   BINDING         59
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:O34974"
FT   BINDING         101
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:O34974"
FT   BINDING         151..155
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:O34974"
FT   BINDING         204..207
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:O34974"
SQ   SEQUENCE   422 AA;  46504 MW;  B66CA9305DCC453E CRC64;
     MTAPRRRITL AGIIDGPGGH VAAWRHPATK ADAQLDFEFH RDNARTLERG LFDAVFIADI
     VAVWGTRLDS LCRTSRTEHF EPLTLLAAYA AVTEHIGLCA TATTTYNEPA HIAARFASLD
     HLSGGRAGWN VVTSAAPWES ANFGFPEHLE HGKRYERAEE FIDVVKKLWD SDGRPVDHRG
     THFEAPGPLG IARPPQGRPV IIQAGSSPVG REFAARHAEV IFTRHNRLSD AQDFYGDLKA
     RVARHGRDPE KVLVWPTLAP IVAATDTEAK QRLQELQDLT HDHVALRTLQ DHLGDVDLSA
     YPIDGPVPDI PYTNQSQSTT ERLIGLARRE NLSIRELALR LMGDIVVGTP EQLADHMESW
     FTGRGADGFN IDFPYLPGSA DDFVDHVVPE LQRRGLYRSG YEGTTLRANL GIDAPRKAGA
     AA