ID   HRB_MOOTA               Reviewed;         229 AA.
AC   Q9FDN6; Q2RIY7;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=High molecular weight rubredoxin;
DE   AltName: Full=Nitric oxide reductase NADH:FprA oxidoreductase;
GN   Name=hrb; OrderedLocusNames=Moth_1288;
OS   Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Moorella group; Moorella.
OX   NCBI_TaxID=264732;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11160086; DOI=10.1128/jb.183.5.1560-1567.2001;
RA   Das A., Coulter E.D., Kurtz D.M. Jr., Ljungdahl L.G.;
RT   "Five-gene cluster in Clostridium thermoaceticum consisting of two
RT   divergent operons encoding rubredoxin oxidoreductase-rubredoxin and
RT   rubrerythrin-type A flavoprotein- high-molecular-weight rubredoxin.";
RL   J. Bacteriol. 183:1560-1567(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39073 / JCM 9320;
RX   PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x;
RA   Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C.,
RA   Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.;
RT   "The complete genome sequence of Moorella thermoacetica (f. Clostridium
RT   thermoaceticum).";
RL   Environ. Microbiol. 10:2550-2573(2008).
RN   [3]
RP   CHARACTERIZATION, AND COFACTOR.
RX   PubMed=12627946; DOI=10.1021/bi027253k;
RA   Silaghi-Dumitrescu R., Coulter E.D., Das A., Ljungdahl L.G.,
RA   Jameson G.N.L., Huynh B.H., Kurtz D.M. Jr.;
RT   "A flavodiiron protein and high molecular weight rubredoxin from Moorella
RT   thermoacetica with nitric oxide reductase activity.";
RL   Biochemistry 42:2806-2815(2003).
CC   -!- FUNCTION: Has nitric oxide reductase activity in combination with FprA;
CC       probably involved in nitrosative stress protection. Acts as an
CC       NADH:FprA oxidoreductase.
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000269|PubMed:12627946};
CC       Note=Binds 2 iron ions per homodimer. {ECO:0000269|PubMed:12627946};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000269|PubMed:12627946};
CC       Note=Binds 2 FMN per homodimer. The occupancy is 1.3-1.9.
CC       {ECO:0000269|PubMed:12627946};
CC   -!- SUBUNIT: Homodimer.
CC   -!- INDUCTION: Constitutively expressed.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the flavodoxin
CC       reductase family. {ECO:0000305}.
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DR   EMBL; AF202316; AAG00803.1; -; Genomic_DNA.
DR   EMBL; CP000232; ABC19602.1; -; Genomic_DNA.
DR   RefSeq; WP_011392802.1; NC_007644.1.
DR   RefSeq; YP_430145.1; NC_007644.1.
DR   AlphaFoldDB; Q9FDN6; -.
DR   SMR; Q9FDN6; -.
DR   STRING; 264732.Moth_1288; -.
DR   EnsemblBacteria; ABC19602; ABC19602; Moth_1288.
DR   GeneID; 61290012; -.
DR   KEGG; mta:Moth_1288; -.
DR   PATRIC; fig|264732.11.peg.1382; -.
DR   eggNOG; COG1773; Bacteria.
DR   eggNOG; COG1853; Bacteria.
DR   HOGENOM; CLU_059021_4_1_9; -.
DR   OMA; CANTCFQ; -.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016646; F:oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor; IEA:UniProt.
DR   CDD; cd00730; rubredoxin; 1.
DR   Gene3D; 2.30.110.10; -; 1.
DR   InterPro; IPR002563; Flavin_Rdtase-like_dom.
DR   InterPro; IPR024934; Rubredoxin-like_dom.
DR   InterPro; IPR024935; Rubredoxin_dom.
DR   InterPro; IPR018527; Rubredoxin_Fe_BS.
DR   InterPro; IPR012349; Split_barrel_FMN-bd.
DR   Pfam; PF01613; Flavin_Reduct; 1.
DR   Pfam; PF00301; Rubredoxin; 1.
DR   PRINTS; PR00163; RUBREDOXIN.
DR   SMART; SM00903; Flavin_Reduct; 1.
DR   PROSITE; PS00202; RUBREDOXIN; 1.
DR   PROSITE; PS50903; RUBREDOXIN_LIKE; 1.
PE   1: Evidence at protein level;
KW   Electron transport; Flavoprotein; FMN; Iron; Metal-binding; Oxidoreductase;
KW   Transport.
FT   CHAIN           1..229
FT                   /note="High molecular weight rubredoxin"
FT                   /id="PRO_0000135073"
FT   DOMAIN          178..229
FT                   /note="Rubredoxin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00241"
FT   REGION          1..158
FT                   /note="Flavodoxin-reductase-like"
FT   BINDING         183
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000305"
FT   BINDING         186
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000305"
FT   BINDING         216
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000305"
FT   BINDING         219
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   229 AA;  24887 MW;  DA57FFEF16E92F7F CRC64;
     MDTKALHTLT YGLYIITAKK GDRFNGQVAN TVFQITSDPP TIAVSINKQN LTHEFIQAGQ
     GFVISVLARE VPLSLIGQFG FKSGREMDKF AGINYKLSEG GLPYLADHTL AYLEASLNQT
     VDAGTHSIFI GTVTDAAVLL QGEPMTYAYY HQVKRGTTPK TAPTFTVGRE KDKTALASPK
     YQCTICNYVY DPVQGDPEHG IAPGTPFADL PEDWTCPICG AGKDAFEQI