ID A0A2I0PSM9_9EURY Unreviewed; 193 AA.
AC A0A2I0PSM9;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=CoB--CoM heterodisulfide reductase subunit C {ECO:0000313|EMBL:PKL69254.1};
GN Name=hdrC {ECO:0000313|EMBL:PKL69254.1};
GN ORFNames=CVV30_06675 {ECO:0000313|EMBL:PKL69254.1};
OS Methanomicrobiales archaeon HGW-Methanomicrobiales-1.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales.
OX NCBI_TaxID=2013817 {ECO:0000313|EMBL:PKL69254.1};
RN [1] {ECO:0000313|EMBL:PKL69254.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HGW-Methanomicrobiales-1 {ECO:0000313|EMBL:PKL69254.1};
RX PubMed=28350393; DOI=10.1038/ismej.2017.39;
RA Hernsdorf A.W., Amano Y., Miyakawa K., Ise K., Suzuki Y., Anantharaman K.,
RA Probst A., Burstein D., Thomas B.C., Banfield J.F.;
RT "Potential for microbial H2 and metal transformations associated with novel
RT bacteria and archaea in deep terrestrial subsurface sediments.";
RL ISME J. 11:1915-1929(2017).
RN [2] {ECO:0000313|EMBL:PKL69254.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HGW-Methanomicrobiales-1 {ECO:0000313|EMBL:PKL69254.1};
RA Han C.G.;
RL Submitted (NOV-2017) 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:PKL69254.1}.
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DR EMBL; PGYM01000002; PKL69254.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0PSM9; -.
DR UniPathway; UPA00647; UER00700.
DR Proteomes; UP000233367; 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:InterPro.
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.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 3: Inferred from homology;
KW Methanogenesis {ECO:0000256|ARBA:ARBA00022994}.
FT DOMAIN 34..63
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 77..108
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 193 AA; 21876 MW; 8CC28A7CBDD3F253 CRC64;
MERTKGYPAA LDKKLQDTRL YLNDSNPEFT KNVKAISRTN AHMCYQCGTC TGSCPSAPRS
SYRIRLFMRR AVLGLENEAL TDPDLWLCTT CYSCADRCPR DIIPTDVIMS MRNLAFKRDI
VPVNFLKTVT AIYASGHGVP NNDVNRAARE KIGLSRDPPT THSYPEYMPG IRKILDHYKL
KANADRIIKE REG
//