DADHH_EGGLE
ID DADHH_EGGLE Reviewed; 1017 AA.
AC C8WLC6;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Uncharacterized oxidoreductase Elen_0471 {ECO:0000305};
DE EC=1.-.-.- {ECO:0000305};
DE AltName: Full=Dopamine dehydroxylase homolog {ECO:0000305};
DE AltName: Full=Inactive dopamine dehydroxylase {ECO:0000305|PubMed:31196984};
DE Flags: Precursor;
GN OrderedLocusNames=Elen_0471 {ECO:0000312|EMBL:ACV54456.1};
OS Eggerthella lenta (strain ATCC 25559 / DSM 2243 / CCUG 17323 / JCM 9979 /
OS KCTC 3265 / NCTC 11813 / VPI 0255 / 1899 B) (Eubacterium lentum).
OC Bacteria; Actinobacteria; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC Eggerthella.
OX NCBI_TaxID=479437;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25559 / DSM 2243 / CCUG 17323 / JCM 9979 / KCTC 3265 / NCTC
RC 11813 / VPI 0255 / 1899 B;
RX PubMed=21304654; DOI=10.4056/sigs.33592;
RA Saunders E., Pukall R., Abt B., Lapidus A., Glavina Del Rio T.,
RA Copeland A., Tice H., Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D.,
RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Chain P., Meincke L., Sims D., Brettin T., Detter J.C.,
RA Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Han C.;
RT "Complete genome sequence of Eggerthella lenta type strain (IPP VPI
RT 0255).";
RL Stand. Genomic Sci. 1:174-182(2009).
RN [2]
RP LACK OF DOPAMINE DEHYDROXYLATION ACTIVITY, AND INDUCTION.
RC STRAIN=ATCC 25559 / DSM 2243 / CCUG 17323 / JCM 9979 / KCTC 3265 / NCTC
RC 11813 / VPI 0255 / 1899 B;
RX PubMed=31196984; DOI=10.1126/science.aau6323;
RA Maini Rekdal V., Bess E.N., Bisanz J.E., Turnbaugh P.J., Balskus E.P.;
RT "Discovery and inhibition of an interspecies gut bacterial pathway for
RT Levodopa metabolism.";
RL Science 364:0-0(2019).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P07658};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:P07658};
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000250|UniProtKB:A0A369NIV7};
CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC bis-MGD) cofactor per subunit. {ECO:0000250|UniProtKB:P07658};
CC -!- INDUCTION: Up-regulated in response to dopamine.
CC {ECO:0000269|PubMed:31196984}.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has not been experimentally proven.
CC {ECO:0000255|PROSITE-ProRule:PRU00648}.
CC -!- MISCELLANEOUS: E.lenta strain ATCC 25559 / DSM 2243 is not able to
CC dehydroxylate dopamine, likely due to the presence of a serine residue
CC in position 506 in this protein, instead of an arginine residue in
CC dopamine metabolizing strains. {ECO:0000269|PubMed:31196984}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; CP001726; ACV54456.1; -; Genomic_DNA.
DR RefSeq; WP_015759999.1; NC_013204.1.
DR AlphaFoldDB; C8WLC6; -.
DR SMR; C8WLC6; -.
DR STRING; 479437.Elen_0471; -.
DR EnsemblBacteria; ACV54456; ACV54456; Elen_0471.
DR KEGG; ele:Elen_0471; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_11; -.
DR OMA; VHCDLFE; -.
DR OrthoDB; 88184at2; -.
DR BioCyc; ELEN479437:G1GFY-473-MON; -.
DR Proteomes; UP000001377; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0018818; F:acetylene hydratase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd02781; MopB_CT_Acetylene-hydratase; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR037949; MopB_CT_Acetylene-hydratase.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006311; TAT_signal.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS51318; TAT; 1.
PE 2: Evidence at transcript level;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Molybdenum; Oxidoreductase;
KW Reference proteome; Signal.
FT SIGNAL 1..34
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 35..1017
FT /note="Uncharacterized oxidoreductase Elen_0471"
FT /id="PRO_5002993564"
FT DOMAIN 45..103
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT ACT_SITE 91
FT /note="Electron donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P07658"
FT BINDING 53
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P07658"
FT BINDING 56
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P07658"
FT BINDING 61
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P07658"
FT BINDING 89
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P07658"
SQ SEQUENCE 1017 AA; 114957 MW; 2D95F41B1C898ECD CRC64;
MGNLTMSRRT FVKTAAITGA AAAAFGASTH TALAEETYSS VSGNDTVAVK TCCRGCGKME
CGVKVIVQNG RAIRVEGDEG AFQSMGNCCT KSQSSIQAAY HPDRLHYPMK RTNPKGEEPG
WQRISWDEAM QSIVDNFMDI KAKHGGEAIA CQVGTSRIWC MHSESILKNM LETPNNVEAW
QICKGPRHFA TTMVSQFAMS WMETITRPKV YVQWGGASEL SNYDDSCRTT VDVASRADVH
ISVDPRMANM GKEADYWQHL RPGTDGALAL AWTNVIIEKK LYDELYVKKW TNAPFLVCED
MEPSGFPTVR TDGSYWDVKT ALLKESDIKE GGSPYKFLVY DNNWEKLKAE GVEHEYGAFT
WFNADQEGVI DETGGFWEGE NYDSEKARQG REAAQDNLLP GQTQGWLPDP MPFDPAIDPA
LEGEFEITLK DGKTVKVKPV WEHYKARAAE YKPEVAAEIT GIPASEIEAA ATAYGTRIDP
STGYGNGGIQ YMLAVEHFCS AIQNCSAFDN LVGITGNMDT PGGNRGPTIV PIDGDLQGFS
AWAPGATTPP EEVNRKQIGI DKFPLLGWWQ YWCDSHSLWD AVITGDPYPV RALWNESGNF
MSQTNTTRAW EALCSLDFYV DLNLWHTPQN DTADIILPVA HWIELNSPRA SQGSAGAMGA
TVKCVQPPAE AKYDPEIVMD LARRMNWKWT DEPGNEWPDI NWQLDDSIKL LTDDELTYTT
WHVENGKPTF ERHGVPMAEV TPKYKTWDEY VKAFQEHGWW QAKDIEPRNW GTYRRYQTGA
MRARDRVWGR LDYTAGKGIG DWKPGWFTPT MKQEIWSTVM ESHHPDHPEW RLPTYTEPPH
GPKDGDRIKE YPLTATTGRR IPVYFHSEHR QLPWCRELWP VPRVEINPKT AAEYGIEQGD
WVWIETEWGK IREVADLYYG VKEDVINLEH TWWYPEVKDA GHGWQFSQVN QLIDHYAQDP
HSGTSNLRAY QVKIYKATPE NSPFNNPVPC DSTGTPIIHT SDDPRLKEWL PTYEGRE
