DDHC_RHOSU
ID DDHC_RHOSU Reviewed; 265 AA.
AC Q8GPG1;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Dimethylsulfide dehydrogenase subunit gamma;
DE Short=DMS DH subunit gamma;
DE AltName: Full=DMS DH heme subunit;
DE AltName: Full=Dimethyl sulfide:cytochrome c2 reductase subunit beta;
DE AltName: Full=Dimethylsulfide heme subunit;
DE Flags: Precursor;
GN Name=ddhC;
OS Rhodovulum sulfidophilum (Rhodobacter sulfidophilus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodovulum.
OX NCBI_TaxID=35806;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 26-35.
RC STRAIN=SH1;
RX PubMed=12067345; DOI=10.1046/j.1365-2958.2002.02978.x;
RA McDevitt C.A., Hugenholtz P., Hanson G.R., McEwan A.G.;
RT "Molecular analysis of dimethyl sulphide dehydrogenase from Rhodovulum
RT sulfidophilum: its place in the dimethyl sulphoxide reductase family of
RT microbial molybdopterin-containing enzymes.";
RL Mol. Microbiol. 44:1575-1587(2002).
RN [2]
RP FUNCTION, SUBUNIT, AND COFACTOR.
RX PubMed=8706745; DOI=10.1111/j.1432-1033.1996.0391u.x;
RA Hanlon S.P., Toh T.H., Solomon P.S., Holt R.A., McEwan A.G.;
RT "Dimethylsulfide:acceptor oxidoreductase from Rhodobacter sulfidophilus.
RT The purified enzyme contains b-type haem and a pterin molybdenum
RT cofactor.";
RL Eur. J. Biochem. 239:391-396(1996).
CC -!- FUNCTION: May transfer electrons to the iron-sulfur centers of DdhB.
CC {ECO:0000269|PubMed:8706745}.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000305};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000305};
CC -!- SUBUNIT: Heterotrimer of alpha, beta and gamma subunits.
CC {ECO:0000269|PubMed:8706745}.
CC -!- SUBCELLULAR LOCATION: Periplasm.
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DR EMBL; AF453479; AAN46635.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8GPG1; -.
DR SMR; Q8GPG1; -.
DR STRING; 1188256.BASI01000002_gene2974; -.
DR KEGG; ag:AAN46635; -.
DR eggNOG; COG2010; Bacteria.
DR BioCyc; MetaCyc:MON-14244; -.
DR BRENDA; 1.8.2.4; 5384.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd09623; DOMON_EBDH; 1.
DR InterPro; IPR017838; DMSO_Rdtase_II_haem_b-bd_su.
DR TIGRFAMs; TIGR03477; DMSO_red_II_gam; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Electron transport; Heme; Iron; Metal-binding;
KW Periplasm; Signal; Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:12067345"
FT CHAIN 26..265
FT /note="Dimethylsulfide dehydrogenase subunit gamma"
FT /id="PRO_0000021095"
FT BINDING 81
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255"
FT BINDING 147
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255"
SQ SEQUENCE 265 AA; 29499 MW; 6835763DDE0B1C33 CRC64;
MPGFRFLLAA TAAFLATSPA LPLSADSLNA GNIRLVDPEE TVPVIKIPDG IYLRTPNDPD
DIIWARVPEF RVEMVMAPPV HPSVGLRYRD EYPEQDLVVQ LARTSERFYV RLRWVDPTRD
MSTLRDRFRD GAAIEFSESD DSVSYMMGTD AESPVNIWYW HPDGDRVESL AAGSPGSLTR
LDRQPVTGAS EYRTGHGPDD SQWIVVMSRP LASEGDHQVS FERDTIPVAF ALWQGADAQR
DGLKLVSLNW IFARMTPDAA PAPGN
