HSPB_PSEP6
ID HSPB_PSEP6 Reviewed; 393 AA.
AC F8G0M4;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=6-hydroxy-3-succinoylpyridine 3-monooxygenase HspB;
DE EC=1.14.13.163;
DE AltName: Full=6-hydroxy-3-succinoylpyridine hydroxylase;
DE Short=HSP hydroxylase;
GN Name=hspB; ORFNames=PPS_4061;
OS Pseudomonas putida (strain S16).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1042876;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S16;
RX PubMed=21914868; DOI=10.1128/jb.05663-11;
RA Yu H., Tang H., Wang L., Yao Y., Wu G., Xu P.;
RT "Complete genome sequence of the nicotine-degrading Pseudomonas putida
RT strain S16.";
RL J. Bacteriol. 193:5541-5542(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11, FUNCTION,
RP CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL PROPERTIES,
RP COFACTOR, ACTIVITY REGULATION, AND SUBUNIT.
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:21949128}.
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:21949128};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000305|PubMed:21949128};
CC Note=Binds 1 FAD per subunit. {ECO:0000305|PubMed:21949128};
CC -!- ACTIVITY REGULATION: Inhibited by Cu(2+) and Zn(2+).
CC {ECO:0000269|PubMed:21949128}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.175 mM for HSP {ECO:0000269|PubMed:21949128};
CC KM=0.2 mM for NADH {ECO:0000269|PubMed:21949128};
CC Note=kcat is 2 sec(-1).;
CC pH dependence:
CC Optimum pH is 8. At pH below 7.0 or above 9.0, there is substantial
CC loss of activity. {ECO:0000269|PubMed:21949128};
CC Temperature dependence:
CC Optimum temperature is 25 degrees Celsius. The enzyme activity
CC measured at 5 degrees Celsius is maintained up to 25 degrees Celsius
CC but is lost quickly at higher temperatures.
CC {ECO:0000269|PubMed:21949128};
CC -!- PATHWAY: Alkaloid degradation; nicotine degradation.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21949128}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are not able to grow in
CC nicotine medium. {ECO:0000269|PubMed:21949128}.
CC -!- MISCELLANEOUS: The catalytic efficiency of HspB is higher than that of
CC HspA. {ECO:0000305|PubMed:21949128}.
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DR EMBL; CP002870; AEJ14602.1; -; Genomic_DNA.
DR EMBL; GQ857548; ADN26547.1; -; Genomic_DNA.
DR RefSeq; WP_013973865.1; NC_015733.1.
DR PDB; 7DA9; X-ray; 2.11 A; A/B=1-393.
DR PDBsum; 7DA9; -.
DR AlphaFoldDB; F8G0M4; -.
DR SMR; F8G0M4; -.
DR STRING; 1042876.PPS_4061; -.
DR EnsemblBacteria; AEJ14602; AEJ14602; PPS_4061.
DR KEGG; ppt:PPS_4061; -.
DR eggNOG; COG0654; Bacteria.
DR HOGENOM; CLU_009665_2_2_6; -.
DR BioCyc; MetaCyc:MON-17159; -.
DR BioCyc; PPUT1042876:PPS_RS21025-MON; -.
DR BRENDA; 1.14.13.163; 5092.
DR UniPathway; UPA00106; -.
DR Proteomes; UP000000502; Chromosome.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0009820; P:alkaloid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0019608; P:nicotine catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01494; FAD_binding_3; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alkaloid metabolism; Direct protein sequencing; FAD;
KW Flavoprotein; Monooxygenase; NAD; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:21949128"
FT CHAIN 2..393
FT /note="6-hydroxy-3-succinoylpyridine 3-monooxygenase HspB"
FT /id="PRO_0000422325"
FT BINDING 6..35
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 277..287
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT STRAND 7..10
FT /evidence="ECO:0007829|PDB:7DA9"
FT HELIX 14..25
FT /evidence="ECO:0007829|PDB:7DA9"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:7DA9"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:7DA9"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:7DA9"
FT HELIX 53..58
FT /evidence="ECO:0007829|PDB:7DA9"
FT HELIX 62..68
FT /evidence="ECO:0007829|PDB:7DA9"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:7DA9"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:7DA9"
FT TURN 80..83
FT /evidence="ECO:0007829|PDB:7DA9"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:7DA9"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:7DA9"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:7DA9"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:7DA9"
FT HELIX 107..119
FT /evidence="ECO:0007829|PDB:7DA9"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:7DA9"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:7DA9"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:7DA9"
FT STRAND 154..162
FT /evidence="ECO:0007829|PDB:7DA9"
FT HELIX 169..172
FT /evidence="ECO:0007829|PDB:7DA9"
FT STRAND 179..194
FT /evidence="ECO:0007829|PDB:7DA9"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:7DA9"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:7DA9"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:7DA9"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:7DA9"
FT STRAND 221..232
FT /evidence="ECO:0007829|PDB:7DA9"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:7DA9"
FT HELIX 241..252
FT /evidence="ECO:0007829|PDB:7DA9"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:7DA9"
FT STRAND 260..275
FT /evidence="ECO:0007829|PDB:7DA9"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:7DA9"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:7DA9"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:7DA9"
FT HELIX 298..319
FT /evidence="ECO:0007829|PDB:7DA9"
FT HELIX 325..340
FT /evidence="ECO:0007829|PDB:7DA9"
FT HELIX 342..354
FT /evidence="ECO:0007829|PDB:7DA9"
FT HELIX 360..373
FT /evidence="ECO:0007829|PDB:7DA9"
FT HELIX 376..383
FT /evidence="ECO:0007829|PDB:7DA9"
FT HELIX 385..389
FT /evidence="ECO:0007829|PDB:7DA9"
SQ SEQUENCE 393 AA; 43971 MW; B650BF5A199C8089 CRC64;
MSMKQRVIIV GGGPVGLLTA LGLAKAGTNV VVLEAESQPS DSPRALVYHF PVLPHLKRLG
VLDDCVAAGL MRQNFAWRVH STSEMIFWDL SCLEGDVELP YALHLGQDKL SRILIEHLKA
LPNVEVRYSS PVVDCEVGPR SVRVVLGGES PGVIVEGDWL IGADGANSFV RREVLNQNFF
GITWPQRYVA TNTRFDFDKL GFGKTTMQVD DVYGSVICNI DADSLWRVTF MEDPNLPMEG
IRGRIDQVFK ELLPTNDPYE VVAFSPYRMH QRVTDRMRNG RVILIGDAAH VTNPTGGLGL
TGGMFDAFAL TSVLNQVIHD GRSEDILDVF EADRRRKFIE LVSPRASDNL RNLYHQKPGE
GKNDWVNNTR SISKDIDRMR DALRFPETME TFL
