ID D2ZQ78_METSM Unreviewed; 341 AA.
AC D2ZQ78;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=CoB--CoM heterodisulfide reductase, subunit C {ECO:0000313|EMBL:EFC93425.1};
DE EC=1.8.98.1 {ECO:0000313|EMBL:EFC93425.1};
GN Name=hdrC {ECO:0000313|EMBL:EFC93425.1};
GN ORFNames=METSMIF1_03005 {ECO:0000313|EMBL:EFC93425.1};
OS Methanobrevibacter smithii DSM 2374.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=521002 {ECO:0000313|EMBL:EFC93425.1, ECO:0000313|Proteomes:UP000004028};
RN [1] {ECO:0000313|EMBL:EFC93425.1, ECO:0000313|Proteomes:UP000004028}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2374 {ECO:0000313|EMBL:EFC93425.1,
RC ECO:0000313|Proteomes:UP000004028};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cofactor metabolism; coenzyme M-coenzyme B heterodisulfide
CC reduction; coenzyme B and coenzyme M from coenzyme M-coenzyme B
CC heterodisulfide: step 1/1. {ECO:0000256|ARBA:ARBA00004808}.
CC -!- SIMILARITY: Belongs to the HdrC family.
CC {ECO:0000256|ARBA:ARBA00007097}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFC93425.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ABYV02000006; EFC93425.1; -; Genomic_DNA.
DR RefSeq; WP_004033132.1; NZ_GG704759.1.
DR AlphaFoldDB; D2ZQ78; -.
DR PATRIC; fig|521002.11.peg.980; -.
DR HOGENOM; CLU_068200_0_0_2; -.
DR UniPathway; UPA00647; UER00700.
DR Proteomes; UP000004028; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0051912; F:CoB--CoM heterodisulfide reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR017680; CoB/CoM_hetero-S_Rdtase_csu.
DR InterPro; IPR009051; Helical_ferredxn.
DR NCBIfam; TIGR03290; CoB_CoM_SS_C; 1.
DR PANTHER; PTHR43255:SF1; FERREDOXIN_F(420)H(2)-DEPENDENT COB-COM HETERODISULFIDE REDUCTASE SUBUNIT C; 1.
DR PANTHER; PTHR43255; IRON-SULFUR-BINDING OXIDOREDUCTASE FADF-RELATED-RELATED; 1.
DR Pfam; PF13183; Fer4_8; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
PE 3: Inferred from homology;
KW Methanogenesis {ECO:0000256|ARBA:ARBA00022994};
KW Oxidoreductase {ECO:0000313|EMBL:EFC93425.1}.
FT DOMAIN 187..248
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|Pfam:PF13183"
FT REGION 1..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..139
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 341 AA; 38117 MW; 209A07B5E7415BA6 CRC64;
MSIIDNLKSL FKRDKDNEEK GMDDLKSEDT KVTSSNNLDK SVVSGTKTTE PMVKIKISSD
DTEDMTFKKD VKTSETSDVE ENEEIAPEID DAEEKTEVLD ELDILTDDSN EDDEVSEDEN
NTTETEDESI DESEEVVNDE KVENEVSKDN DKKRDNMTLL TDKELLTDAN RDKEFTAEFI
DAGIETVKHC FQCGTCGGSC PSGRRTPYKV RQIVRKCLLG LKEEVISDDA LWMCTTCYTC
QERCPRSVKI VEIIKKARNV AAHAGYMALA HKKTGLFVIK TGHGVPINDA TKALRSKIGL
SELPATTHSF PEALEEVQKI CEITAFDELI GYDKATGDLK E
//
