KDHC_PAENI
ID KDHC_PAENI Reviewed; 794 AA.
AC Q933N0;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=6-hydroxypseudooxynicotine dehydrogenase complex subunit gamma;
DE EC=1.5.99.14;
DE AltName: Full=Ketone dehydrogenase large molybdopterin subunit;
GN Name=kdhC; Synonyms=kdhL;
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 7-15, FUNCTION, AND
RP 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).
RN [4]
RP FUNCTION, AND COFACTOR.
RX PubMed=16820521; DOI=10.1128/aem.00437-06;
RA Sachelaru P., Schiltz E., Brandsch R.;
RT "A functional mobA gene for molybdopterin cytosine dinucleotide cofactor
RT biosynthesis is required for activity and holoenzyme assembly of the
RT heterotrimeric nicotine dehydrogenases of Arthrobacter nicotinovorans.";
RL Appl. Environ. Microbiol. 72:5126-5131(2006).
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:16820521,
CC 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=Mo-molybdopterin cytosine dinucleotide; Xref=ChEBI:CHEBI:71308;
CC Evidence={ECO:0000269|PubMed:16820521};
CC Note=Binds 1 Mo-molybdopterin cytosine dinucleotide (Mo-MCD) per
CC subunit. {ECO:0000269|PubMed:16820521};
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; AAK64253.1; -; Genomic_DNA.
DR EMBL; AJ306904; CAC37487.1; -; Genomic_DNA.
DR EMBL; AJ507836; CAD47940.1; -; Genomic_DNA.
DR RefSeq; WP_016359451.1; NC_021229.1.
DR RefSeq; YP_007988766.1; NC_021229.1.
DR PDB; 7DQX; X-ray; 3.44 A; A/D=1-794.
DR PDBsum; 7DQX; -.
DR AlphaFoldDB; Q933N0; -.
DR SMR; Q933N0; -.
DR KEGG; ag:CAC37487; -.
DR BioCyc; MetaCyc:MON-983; -.
DR UniPathway; UPA00106; -.
DR GO; GO:0034909; F:6-hydroxypseudooxynicotine dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0019608; P:nicotine catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
DR InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
DR InterPro; IPR016208; Ald_Oxase/xanthine_DH.
DR InterPro; IPR008274; AldOxase/xan_DH_Mopterin-bd.
DR InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
DR PANTHER; PTHR11908; PTHR11908; 1.
DR Pfam; PF01315; Ald_Xan_dh_C; 1.
DR Pfam; PF02738; Ald_Xan_dh_C2; 1.
DR SMART; SM01008; Ald_Xan_dh_C; 1.
DR SUPFAM; SSF54665; SSF54665; 1.
DR SUPFAM; SSF56003; SSF56003; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Metal-binding; Molybdenum;
KW Oxidoreductase; Plasmid.
FT CHAIN 1..794
FT /note="6-hydroxypseudooxynicotine dehydrogenase complex
FT subunit gamma"
FT /id="PRO_0000424217"
FT HELIX 35..40
FT /evidence="ECO:0007829|PDB:7DQX"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:7DQX"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:7DQX"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 131..139
FT /evidence="ECO:0007829|PDB:7DQX"
FT HELIX 140..148
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:7DQX"
FT HELIX 163..167
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:7DQX"
FT HELIX 191..196
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 199..207
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:7DQX"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:7DQX"
FT HELIX 244..251
FT /evidence="ECO:0007829|PDB:7DQX"
FT TURN 269..271
FT /evidence="ECO:0007829|PDB:7DQX"
FT HELIX 277..287
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 293..296
FT /evidence="ECO:0007829|PDB:7DQX"
FT HELIX 299..305
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 312..320
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 333..336
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 343..346
FT /evidence="ECO:0007829|PDB:7DQX"
FT HELIX 347..352
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 368..372
FT /evidence="ECO:0007829|PDB:7DQX"
FT HELIX 387..404
FT /evidence="ECO:0007829|PDB:7DQX"
FT HELIX 409..416
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 420..422
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 428..430
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 434..438
FT /evidence="ECO:0007829|PDB:7DQX"
FT HELIX 448..453
FT /evidence="ECO:0007829|PDB:7DQX"
FT HELIX 458..461
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 466..469
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 474..477
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 492..497
FT /evidence="ECO:0007829|PDB:7DQX"
FT TURN 498..500
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 501..508
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 511..513
FT /evidence="ECO:0007829|PDB:7DQX"
FT HELIX 515..527
FT /evidence="ECO:0007829|PDB:7DQX"
FT HELIX 531..533
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 534..539
FT /evidence="ECO:0007829|PDB:7DQX"
FT TURN 541..543
FT /evidence="ECO:0007829|PDB:7DQX"
FT HELIX 555..577
FT /evidence="ECO:0007829|PDB:7DQX"
FT TURN 578..581
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 593..595
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 599..602
FT /evidence="ECO:0007829|PDB:7DQX"
FT HELIX 607..613
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 614..619
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 645..652
FT /evidence="ECO:0007829|PDB:7DQX"
FT TURN 654..656
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 659..666
FT /evidence="ECO:0007829|PDB:7DQX"
FT HELIX 676..695
FT /evidence="ECO:0007829|PDB:7DQX"
FT TURN 712..714
FT /evidence="ECO:0007829|PDB:7DQX"
FT TURN 720..722
FT /evidence="ECO:0007829|PDB:7DQX"
FT TURN 740..742
FT /evidence="ECO:0007829|PDB:7DQX"
FT TURN 747..753
FT /evidence="ECO:0007829|PDB:7DQX"
FT HELIX 754..764
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 774..776
FT /evidence="ECO:0007829|PDB:7DQX"
FT TURN 779..784
FT /evidence="ECO:0007829|PDB:7DQX"
FT TURN 787..789
FT /evidence="ECO:0007829|PDB:7DQX"
SQ SEQUENCE 794 AA; 86371 MW; 64297D11BFFC5F2C CRC64;
MMAKAKALIP DNGRAGADEG NRQAWIGQEV LRREDRRLLT GTATFAGDLG VPGQLHMRIV
RSTQAHARIV SIDATEAEKT PGVRMVITSE HTRHLGSVLL EELGYHEIYE NIEDFSHPVL
AVDKVLYVGQ PVVAVLAVDP YLAEDAAELV SIEYEPLPVL LDPEEALTGK VELFPGRGNE
GARIKKAYGD IDRAFAEAEH VIRHKYVTNR HSGVPMEPRA VVVQPDPARD TLFIWGTVHV
HDNRRIIAKM LNLPEVNVRM KHVEIGGSFG VKGGVFPENV VAAWAARTLG VPIKWTEDRV
EHMTSTSHAR EMVHKLELAL DAEGRILGMK DEIFHNHGAY FRQAEPLVSD ITAGIVFGPY
RVPAYDATLH AVFTNKTPVG AYRAPGRYES TFARERIFDL ACAEIGLSKT EFRRRNLLTA
EDLPWTPGLD IVHEPYHFDS GDVVKHFNEA LEAANFSEWL EESKRLRADG RKVGVGLGVL
MDKAGLGLFE TGGVEVSRAG RVTVKTGGSS VGQGIETVLA QIVAEELQIA PENIDIVHSD
TELIPDGVGS WSSRSTVLAG GAARKAALAV VEKARRLASE MLEADPDDLE LTAGSFKVKG
TDQQISLYEI AAARDPFTAR ADNDEPGLAA DAVYMNNAMN YPYGVTLVQI ELDPDTGGHR
ILRFSTSTEA GRVINPLTTR GQIIGAAVQG IGGALYEEFL YEEDGQPITT SFMDYLLPSA
QEMPNVDCFV TEDAKSPDNP FGAKGLGEIG IIAAGAAIAS AIDDAIADGV HTDRLPVTPE
QIFSRCQGLN KAER
