KDHB_PAENI
ID KDHB_PAENI Reviewed; 160 AA.
AC O87682;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=6-hydroxypseudooxynicotine dehydrogenase complex subunit beta;
DE EC=1.5.99.14;
DE AltName: Full=Ketone dehydrogenase small FeS subunit;
GN Name=kdhB; Synonyms=kdhS;
OS Paenarthrobacter nicotinovorans (Arthrobacter nicotinovorans).
OG Plasmid pAO1.
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Paenarthrobacter.
OX NCBI_TaxID=29320;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-15, FUNCTION,
RP COFACTOR, AND SUBUNIT.
RX PubMed=9878353; DOI=10.1006/jmbi.1998.2227;
RA Schenk S., Hoelz A., Kraus B., Decker K.;
RT "Gene structures and properties of enzymes of the plasmid-encoded nicotine
RT catabolism of Arthrobacter nicotinovorans.";
RL J. Mol. Biol. 284:1323-1339(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11514508; DOI=10.1128/jb.183.18.5262-5267.2001;
RA Baitsch D., Sandu C., Brandsch R., Igloi G.L.;
RT "Gene cluster on pAO1 of Arthrobacter nicotinovorans involved in
RT degradation of the plant alkaloid nicotine: cloning, purification, and
RT characterization of 2,6-dihydroxypyridine 3-hydroxylase.";
RL J. Bacteriol. 183:5262-5267(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12618462; DOI=10.1128/jb.185.6.1976-1986.2003;
RA Igloi G.L., Brandsch R.;
RT "Sequence of the 165-kilobase catabolic plasmid pAO1 from Arthrobacter
RT nicotinovorans and identification of a pAO1-dependent nicotine uptake
RT system.";
RL J. Bacteriol. 185:1976-1986(2003).
CC -!- FUNCTION: Molybdo-flavoprotein enzyme complex involved in nicotine
CC degradation. The subunit gamma (large subunit) contains the substrate-
CC binding sites, the subunit alpha (medium subunit) binds FAD and the
CC subunit beta (small subunit) has a 2Fe-2S ferredoxin-type domain which
CC binds 2 2Fe-2S clusters. {ECO:0000269|PubMed:9878353}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-hydroxypseudooxynicotine + A + H2O = 2,6-
CC dihydroxypseudooxynicotine + AH2; Xref=Rhea:RHEA:34223,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:58682, ChEBI:CHEBI:66944; EC=1.5.99.14;
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:9878353};
CC Note=Binds 2 [2Fe-2S] clusters. {ECO:0000269|PubMed:9878353};
CC -!- PATHWAY: Alkaloid degradation; nicotine degradation.
CC -!- SUBUNIT: Heterohexamer of 2 alpha (kdhA), 2 beta (kdhB) and 2 gamma
CC (kdhC) subunit. Dimer of heterotrimers (Probable).
CC {ECO:0000305|PubMed:9878353}.
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DR EMBL; AF373840; AAK64247.1; -; Genomic_DNA.
DR EMBL; AJ001137; CAA04551.1; -; Genomic_DNA.
DR EMBL; AJ507836; CAD47946.1; -; Genomic_DNA.
DR RefSeq; WP_016359457.1; NC_021229.1.
DR RefSeq; YP_007988772.1; NC_021229.1.
DR PDB; 7DQX; X-ray; 3.44 A; C/F=1-160.
DR PDBsum; 7DQX; -.
DR AlphaFoldDB; O87682; -.
DR SMR; O87682; -.
DR KEGG; ag:CAA04551; -.
DR BioCyc; MetaCyc:MON-982; -.
DR UniPathway; UPA00106; -.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0034909; F:6-hydroxypseudooxynicotine dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019608; P:nicotine catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR InterPro; IPR002888; 2Fe-2S-bd.
DR InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF01799; Fer2_2; 1.
DR SUPFAM; SSF47741; SSF47741; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Direct protein sequencing; Iron; Iron-sulfur;
KW Metal-binding; Oxidoreductase; Plasmid.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9878353"
FT CHAIN 2..160
FT /note="6-hydroxypseudooxynicotine dehydrogenase complex
FT subunit beta"
FT /id="PRO_0000424216"
FT DOMAIN 4..80
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 42
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 47
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 50
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 62
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 101
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 104
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 137
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 139
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:7DQX"
FT HELIX 25..30
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:7DQX"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:7DQX"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:7DQX"
FT HELIX 88..95
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:7DQX"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:7DQX"
FT HELIX 106..117
FT /evidence="ECO:0007829|PDB:7DQX"
FT HELIX 125..132
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:7DQX"
FT HELIX 143..154
FT /evidence="ECO:0007829|PDB:7DQX"
FT TURN 155..158
FT /evidence="ECO:0007829|PDB:7DQX"
SQ SEQUENCE 160 AA; 17639 MW; 20E81C24F2287C6A CRC64;
MNAFRLTVEV NGVTHATDVE PRRLLADFLR DDLHLRGTRV GCEHGVCGSC TVLLDGQPVR
SCTVLAVQAN NSRIETVESL QKDGQLHPLQ RSFSKCHALQ CGFCTSGFLM TLKPLYDDED
VTLDATSARE AISGNICRCT GYQQIVEATV DAFHCRDHND
