ID   HSPA_PSEPU              Reviewed;         312 AA.
AC   B1N1A2;
DT   29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=6-hydroxy-3-succinoylpyridine 3-monooxygenase HspA;
DE            EC=1.14.13.163;
DE   AltName: Full=6-hydroxy-3-succinoylpyridine hydroxylase;
DE            Short=HSP hydroxylase;
GN   Name=nicB; Synonyms=hspA;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=S16;
RX   PubMed=18203859; DOI=10.1128/aem.02529-07;
RA   Tang H., Wang S., Ma L., Meng X., Deng Z., Zhang D., Ma C., Xu P.;
RT   "A novel gene, encoding 6-hydroxy-3-succinoylpyridine hydroxylase, involved
RT   in nicotine degradation by Pseudomonas putida strain S16.";
RL   Appl. Environ. Microbiol. 74:1567-1574(2008).
RN   [2]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=S16;
RX   PubMed=21949128; DOI=10.1074/jbc.m111.283929;
RA   Tang H., Yao Y., Zhang D., Meng X., Wang L., Yu H., Ma L., Xu P.;
RT   "A novel NADH-dependent and FAD-containing hydroxylase is crucial for
RT   nicotine degradation by Pseudomonas putida.";
RL   J. Biol. Chem. 286:39179-39187(2011).
CC   -!- FUNCTION: Involved in the nicotine degradation. Catalyzes the cleavage
CC       of 6-hydroxy-3-succinoylpyridine (HSP) by incorporation of oxygen at
CC       the 3-position to produce to 2,5-dihydroxypyridine (DHP) and succinic
CC       semialdehyde. {ECO:0000269|PubMed:18203859}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 H(+) + 2 NADH +
CC         O2 = 2,5-dihydroxypyridine + H2O + 2 NAD(+) + succinate semialdehyde;
CC         Xref=Rhea:RHEA:33927, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16364, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57706, ChEBI:CHEBI:57945, ChEBI:CHEBI:66893;
CC         EC=1.14.13.163; Evidence={ECO:0000269|PubMed:18203859};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250};
CC   -!- PATHWAY: Alkaloid degradation; nicotine degradation.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene are still able to grow in
CC       nicotine medium. {ECO:0000269|PubMed:21949128}.
CC   -!- MISCELLANEOUS: The catalytic efficiency of HspA is lower than that of
CC       HspB. {ECO:0000305|PubMed:21949128}.
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DR   EMBL; DQ988162; ABM05923.1; -; Genomic_DNA.
DR   RefSeq; WP_004375200.1; NZ_LDPF01000134.1.
DR   AlphaFoldDB; B1N1A2; -.
DR   SMR; B1N1A2; -.
DR   OrthoDB; 1891199at2; -.
DR   BRENDA; 1.14.13.163; 5092.
DR   UniPathway; UPA00106; -.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004540; F:ribonuclease activity; IEA:InterPro.
DR   GO; GO:0009820; P:alkaloid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0019608; P:nicotine catabolic process; IDA:UniProtKB.
DR   InterPro; IPR021139; NYN_MARF1.
DR   InterPro; IPR024467; Xre/MbcA/ParS-like_toxin-bd.
DR   Pfam; PF09722; DUF2384; 1.
DR   Pfam; PF01936; NYN; 1.
PE   1: Evidence at protein level;
KW   Alkaloid metabolism; FAD; Flavoprotein; Monooxygenase; NAD; Oxidoreductase.
FT   CHAIN           1..312
FT                   /note="6-hydroxy-3-succinoylpyridine 3-monooxygenase HspA"
FT                   /id="PRO_0000422324"
FT   DOMAIN          14..211
FT                   /note="NYN"
FT   BINDING         218..228
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   312 AA;  35610 MW;  3978364DDC187622 CRC64;
     MQRKLDSEPL RTRIYIDGYN FYYGCLRGTP YKWLDLLPLF EKHILPSILV TDNHGQIRAW
     RLLESPSIKY FTAKIIESVA RAGDSVSSQA RYHTALRKLH DGRIELIEGY YAVNKMKVKI
     VDPENPDKAP RECREIQAWK VEEKQSDVNL ALQAYHDSIT GQVDHAVIVT NDTDIAPALQ
     MIRAHTDVRI GVVVPTSGQN RSANTDLIKF AHWKREHINS GELAACQLPR VIPGRKPTIK
     PESWYGQPEL LQEILDLAIP VRGSRAAAFK WMEQPNQFLS GERPIELVET AEGATRVLQY
     IHSWIAQQEE LP