LUH_PSESP
ID LUH_PSESP Reviewed; 695 AA.
AC Q934G0;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Lupanine 17-hydroxylase [cytochrome c];
DE EC=1.17.2.2;
DE AltName: Full=Quinohemoprotein lupanine hydroxylase;
DE Flags: Precursor;
GN Name=luh;
OS Pseudomonas sp.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=306;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Hopper D.J., Kaderbhai M.A., Little A.R., Marriott S.A., Young M.,
RA Rogozinski J.;
RT "Cloning, sequencing and analysis of the gene for lupanine hydroxylase, a
RT quinocytochrome c from a Pseudomonas sp.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PARTIAL PROTEIN SEQUENCE, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, AND COFACTOR.
RC STRAIN=DH2001;
RX PubMed=12686118; DOI=10.1016/s1570-9639(03)00070-0;
RA Hopper D.J., Kaderbhai M.A.;
RT "The quinohaemoprotein lupanine hydroxylase from Pseudomonas putida.";
RL Biochim. Biophys. Acta 1647:110-115(2003).
RN [3]
RP FUNCTION AS A LUPANINE 17-HYDROXYLASE, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, AND COFACTOR.
RC STRAIN=DH2001;
RX PubMed=1656935; DOI=10.1042/bj2790105;
RA Hopper D.J., Rogozinski J., Toczko M.;
RT "Lupanine hydroxylase, a quinocytochrome c from an alkaloid-degrading
RT Pseudomonas sp.";
RL Biochem. J. 279:105-109(1991).
CC -!- FUNCTION: Catalyzes the first reaction in the catabolism of the
CC alkaloid lupanine. It dehydrogenates lupanine, which can then be
CC hydrated to produce 17-hydroxylupanine. {ECO:0000269|PubMed:1656935}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(III)-[cytochrome c] + H2O + lupanine = 17-hydroxylupanine
CC + 2 Fe(II)-[cytochrome c] + 2 H(+); Xref=Rhea:RHEA:32643, Rhea:RHEA-
CC COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:64261, ChEBI:CHEBI:64262; EC=1.17.2.2;
CC -!- COFACTOR:
CC Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442;
CC Note=Binds 1 PQQ group per subunit.;
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Note=Binds 1 heme c group covalently per subunit.;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.87 uM for sparteine (at 25 degrees Celsius and at pH 8.5)
CC {ECO:0000269|PubMed:12686118, ECO:0000269|PubMed:1656935};
CC KM=3.6 uM for lupanine (at 25 degrees Celsius and at pH 8.5)
CC {ECO:0000269|PubMed:12686118, ECO:0000269|PubMed:1656935};
CC KM=21.3 uM for cytochrome C (at 25 degrees Celsius and at pH 8.5)
CC {ECO:0000269|PubMed:12686118, ECO:0000269|PubMed:1656935};
CC Note=kcat is 217 sec(-1) with lupanine as substrate and 11.8 sec(-1)
CC with sparteine as substrate.;
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12686118,
CC ECO:0000269|PubMed:1656935}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:12686118}.
CC -!- SIMILARITY: Belongs to the bacterial PQQ dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AJ318095; CAC67410.1; -; Genomic_DNA.
DR AlphaFoldDB; Q934G0; -.
DR SMR; Q934G0; -.
DR PRIDE; Q934G0; -.
DR KEGG; ag:CAC67410; -.
DR BRENDA; 1.17.2.2; 5085.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0052934; F:alcohol dehydrogenase (cytochrome c) activity; IDA:UniProtKB.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.760.10; -; 1.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR InterPro; IPR002372; PQQ_repeat.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR Pfam; PF13442; Cytochrome_CBB3; 1.
DR Pfam; PF01011; PQQ; 1.
DR Pfam; PF13360; PQQ_2; 1.
DR SMART; SM00564; PQQ; 6.
DR SUPFAM; SSF46626; SSF46626; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Heme; Iron; Metal-binding; Oxidoreductase;
KW Periplasm; PQQ; Signal.
FT SIGNAL 1..26
FT CHAIN 27..695
FT /note="Lupanine 17-hydroxylase [cytochrome c]"
FT /id="PRO_5000067658"
FT DOMAIN 598..677
FT /note="Cytochrome c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 612
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 615
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 616
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
SQ SEQUENCE 695 AA; 74956 MW; 9096C6387E457FE0 CRC64;
MSANKNIWII RLGVAFVCVA IGAAQANEKD GSAVTSGNWS LLGGGNEQHY FSALKDVNKS
NVKNLGLSWF TDMEAGDGLV GNPLVADGVI YQGGPPGKIY ANDLKTGKNL WTYTPEVQYD
KDTSWTGFWG THVNRGLAVD DDNVYIGSYC KLLAVSRTTH KLTWSSQSCD PKKMQAITGA
PRVGGGKVFI GNASGDFGGD RGHLDAFDAK TGKHLWRFYT MPGDPSKPFE NDLLAKASKT
WGTDYWKYTK GGVSPWDAIT YDEASDTLYF GTDGPSPWSP AQRAPDAGDE LFSHSIIAVD
ASTGAYKWHF QTVQNDGSNM SATMHIMLAD LPVEGVSKRV VMTAPKNGYF YVLDASTGKF
ISADHYVPVN WTKGLDPKTG RPIPSNEANY WERPGEMTIP LPGDVGGHNW EAMAYNPELR
TVYIPSTLVP VTVVASKDTG ELDLDYYYGM RPDATIKTQG DLVAWDPLLQ KEKWRAKRSL
PVNGGVLATA GGLVFQGTGD GHFEAFDANT GEKLWSFHVG GSILAAPTTV EVDGDQYLIV
ASGNGGASGM RGIPRLMNNL QSQGPARLLA FRLGGKTELP ITSTPDFPKP QYPKPTSAMA
ESGRHIFNAN ACGACHGFNA EGSTPGLPDL RRSDKLDLAV MKSIVIDGAF KPLGMPGHPH
ISDADLQALQ AFILQKAWTA YDTQQTLKTS DTGAQ
