GenomeNet

Database: UniProt
Entry: Q8Q0T0
LinkDB: Q8Q0T0
Original site: Q8Q0T0 
ID   HDRA_METMA              Reviewed;         793 AA.
AC   Q8Q0T0;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   10-APR-2019, entry version 118.
DE   RecName: Full=Ferredoxin:CoB-CoM heterodisulfide reductase subunit A {ECO:0000250|UniProtKB:Q8TLB0};
DE            EC=1.8.7.3 {ECO:0000250|UniProtKB:Q8TLB0};
GN   Name=hdrA; OrderedLocusNames=MM_0056;
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 /
OS   JCM 11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene
RT   transfer between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
CC   -!- FUNCTION: Part of a complex that catalyzes the reversible
CC       reduction of CoM-S-S-CoB to the thiol-coenzymes H-S-CoM (coenzyme
CC       M) and H-S-CoB (coenzyme B). {ECO:0000250|UniProtKB:Q8TLB0}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=coenzyme B + coenzyme M + 2 oxidized [2Fe-2S]-
CC         [ferredoxin] = coenzyme M-coenzyme B heterodisulfide + 2 H(+) +
CC         2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:55160,
CC         Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:58319,
CC         ChEBI:CHEBI:58411, ChEBI:CHEBI:58596; EC=1.8.7.3;
CC         Evidence={ECO:0000250|UniProtKB:Q8TLB0};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00711};
CC       Note=Binds 4 [4Fe-4S] cluster. {ECO:0000255|PROSITE-
CC       ProRule:PRU00711};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:Q8TM02};
CC   -!- PATHWAY: Cofactor metabolism; coenzyme M-coenzyme B
CC       heterodisulfide reduction; coenzyme B and coenzyme M from coenzyme
CC       M-coenzyme B heterodisulfide: step 1/1.
CC       {ECO:0000250|UniProtKB:Q8TLB0}.
CC   -!- SUBUNIT: The ferredoxin:CoB-CoM heterodisulfide reductase is
CC       composed of three subunits; HdrA, HdrB and HdrC.
CC       {ECO:0000250|UniProtKB:Q8TLB0}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8TLB0}.
CC   -!- SIMILARITY: Belongs to the HdrA family. {ECO:0000305}.
DR   EMBL; AE008384; AAM29752.1; -; Genomic_DNA.
DR   RefSeq; WP_011032010.1; NC_003901.1.
DR   ProteinModelPortal; Q8Q0T0; -.
DR   SMR; Q8Q0T0; -.
DR   STRING; 192952.MM_0056; -.
DR   PRIDE; Q8Q0T0; -.
DR   EnsemblBacteria; AAM29752; AAM29752; MM_0056.
DR   GeneID; 24877469; -.
DR   KEGG; mma:MM_0056; -.
DR   PATRIC; fig|192952.21.peg.69; -.
DR   eggNOG; arCOG02235; Archaea.
DR   eggNOG; arCOG02476; Archaea.
DR   eggNOG; COG1148; LUCA.
DR   eggNOG; COG1908; LUCA.
DR   HOGENOM; HOG000230698; -.
DR   KO; K03388; -.
DR   OMA; TAKHAML; -.
DR   OrthoDB; 1148at2157; -.
DR   BioCyc; MMAZ192952:G1FZI-61-MONOMER; -.
DR   UniPathway; UPA00647; UER00700.
DR   Proteomes; UP000000595; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR039650; HdrA-like.
DR   InterPro; IPR003813; MvhD/FlpD.
DR   PANTHER; PTHR43498; PTHR43498; 1.
DR   Pfam; PF00037; Fer4; 1.
DR   Pfam; PF13187; Fer4_9; 1.
DR   Pfam; PF02662; FlpD; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 4.
PE   3: Inferred from homology;
KW   4Fe-4S; Complete proteome; Cytoplasm; FAD; Flavoprotein; Iron;
KW   Iron-sulfur; Metal-binding; Methanogenesis; Oxidoreductase; Repeat.
FT   CHAIN         1    793       Ferredoxin:CoB-CoM heterodisulfide
FT                                reductase subunit A.
FT                                /FTId=PRO_0000150060.
FT   DOMAIN      233    264       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN      282    311       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN      571    600       4Fe-4S ferredoxin-type 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN      601    629       4Fe-4S ferredoxin-type 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   NP_BIND     147    170       FAD. {ECO:0000255}.
FT   METAL       243    243       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       246    246       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       250    250       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       254    254       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       291    291       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       294    294       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       297    297       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       301    301       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       580    580       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       583    583       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       586    586       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       590    590       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       609    609       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       612    612       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       615    615       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       619    619       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
SQ   SEQUENCE   793 AA;  86803 MW;  F34517E61FD4B362 CRC64;
     MRIGVYVCHC GLNIAGVIDV SALEEMAGEL EDVVLAREVQ FLCSDSGQEG IIKDIKDNKI
     DRVVIAACSP RLHEKTFRHV MEKADLNPYL MEMVNIREQC SWVHADDPQM ATQKAFDLIR
     MGVAKARFLR ELSATSSKAS RNVLIIGGGV AGIEAALNLA EAGFPVTMVE RESTIGGKMA
     LMNEVFPTND CSICVLAPKM TEVQNHPNIT LYTYSEVTDI SGSVGKFHVR VTRKPRFVLE
     DKCKGCVDLC SEVCPVEIEN PMNYGIGKSR AIYMPIPQSV PQVVLIDPDH CVGCGLCQLA
     CPAEAVDYEQ KPEEIEFEAG AVIVSTGYQL FDASRKKEYG FGKYPDVITN MQLERMLNSA
     GPTGGRVLVP STGQPPESVA FIQCVGSRDK TVGNEHCSRV CCMAALKNSQ MVKERYPGTD
     ITIHYIDIRA AGEMYEEYYA RTQGMGVDFI RGKVAEVYAG EDGRPVVRYE NTLESRVEEE
     AHDLVVLSTG YEPSKAAEGI GRMLNLARRP DRFFASAHPK MRPVDAPVSG VFLAGCASGP
     KEIQVSIAQG SACASKVMQL LGTGELEADP MGAHVDPDKC IGCRTCVEVC KFGKISIVDK
     KAVVDEVSCY GCGDCSAACP VGAIQMRNFE NEQILAQVRA ATAHKSQCPF VVAFLCNWCS
     YACADLTGMS RIHYPTNIRV IRTMCSARIN PEFVLEALKG GADGVLVAGC RMDECHYIHG
     NFDAKKRMDV LKEIIKEIGL DPKRLRTLWI SAAEGERFSN TITEFVKELE EIGPIGSELK
     REYTATGLEE VAK
//
DBGET integrated database retrieval system