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Database: UniProt
Entry: Q0QLF7
LinkDB: Q0QLF7
Original site: Q0QLF7 
ID   HNR_EUBBA               Reviewed;         499 AA.
AC   Q0QLF7;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   05-DEC-2018, entry version 48.
DE   RecName: Full=6-hydroxynicotinate reductase {ECO:0000312|EMBL:ABC88393.1};
DE            EC=1.3.7.1;
GN   Name=Hnr {ECO:0000312|EMBL:ABC88393.1};
OS   Eubacterium barkeri (Clostridium barkeri).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae;
OC   Eubacterium.
OX   NCBI_TaxID=1528;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:ABC88393.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-26, COFACTOR,
RP   PATHWAY, AND SUBUNIT.
RC   STRAIN=ATCC 25849 / DSM 1223 / JCM 1389 / NCIB 10623
RC   {ECO:0000312|EMBL:ABC88393.1};
RX   PubMed=16894175; DOI=10.1073/pnas.0601635103;
RA   Alhapel A., Darley D.J., Wagener N., Eckel E., Elsner N., Pierik A.J.;
RT   "Molecular and functional analysis of nicotinate catabolism in
RT   Eubacterium barkeri.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:12341-12346(2006).
RN   [2] {ECO:0000305}
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=5767303;
RA   Holcenberg J.S., Tsai L.;
RT   "Nicotinic acid metabolism. IV. Ferredoxin-dependent reduction of 6-
RT   hydroxynicotinic acid to 6-oxo-1,4,5,6-tetrahydronicotinic acid.";
RL   J. Biol. Chem. 244:1204-1211(1969).
CC   -!- FUNCTION: Catalyzes the reversible reduction of 6-
CC       hydroxynicotinate to 6-oxo-1,4,5,6-tetrahydronicotinate.
CC       {ECO:0000269|PubMed:5767303}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,4,5,6-tetrahydro-6-oxonicotinate + oxidized 2[4Fe-4S]-
CC         [ferredoxin] = 6-hydroxynicotinate + 2 H(+) + reduced 2[4Fe-4S]-
CC         [ferredoxin]; Xref=Rhea:RHEA:17225, Rhea:RHEA-COMP:10002,
CC         Rhea:RHEA-COMP:10004, ChEBI:CHEBI:15378, ChEBI:CHEBI:33722,
CC         ChEBI:CHEBI:33723, ChEBI:CHEBI:57664, ChEBI:CHEBI:57777;
CC         EC=1.3.7.1; Evidence={ECO:0000269|PubMed:5767303};
CC   -!- COFACTOR:
CC       Name=an oxidized flavin; Xref=ChEBI:CHEBI:60531;
CC         Evidence={ECO:0000269|PubMed:16894175};
CC       Note=Binds 1 flavin covalently per subunit.
CC       {ECO:0000269|PubMed:16894175};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601;
CC         Evidence={ECO:0000269|PubMed:16894175};
CC       Note=Binds 1 [2Fe-2S] cluster per subunit.
CC       {ECO:0000269|PubMed:16894175};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000269|PubMed:16894175};
CC       Note=Binds 2 [4Fe-4S] clusters per subunit.
CC       {ECO:0000269|PubMed:16894175};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=16 uM for reduced ferrodoxin {ECO:0000269|PubMed:5767303};
CC       pH dependence:
CC         Optimum pH for the reduction of 6-hydroxynicotinate is 6.5.
CC         Activity declines rapidly below pH 5.6.
CC         {ECO:0000269|PubMed:5767303};
CC   -!- PATHWAY: Cofactor degradation; nicotinate degradation; propanoate
CC       and pyruvate from 6-hydroxynicotinate: step 1/8.
CC       {ECO:0000269|PubMed:16894175}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16894175}.
DR   EMBL; DQ310789; ABC88393.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q0QLF7; -.
DR   SMR; Q0QLF7; -.
DR   KEGG; ag:ABC88393; -.
DR   KO; K20449; -.
DR   BioCyc; MetaCyc:MONOMER-13675; -.
DR   UniPathway; UPA01010; UER01012.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0047595; F:6-hydroxynicotinate reductase activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051187; P:cofactor catabolic process; IDA:UniProtKB.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   Pfam; PF13237; Fer4_10; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   1: Evidence at protein level;
KW   2Fe-2S; 4Fe-4S; Direct protein sequencing; Iron; Iron-sulfur;
KW   Metal-binding; Oxidoreductase; Repeat.
FT   CHAIN         1    499       6-hydroxynicotinate reductase.
FT                                /FTId=PRO_0000403975.
FT   DOMAIN        1     29       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN       31     61       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL         9      9       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P00195}.
FT   METAL        12     12       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P00195}.
FT   METAL        15     15       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P00195}.
FT   METAL        19     19       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P00195}.
FT   METAL        41     41       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P00195}.
FT   METAL        44     44       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P00195}.
FT   METAL        47     47       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P00195}.
FT   METAL        51     51       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P00195}.
SQ   SEQUENCE   499 AA;  53097 MW;  211F9BB464FEF5F8 CRC64;
     MFKIDEEKCK KCRMCVKECP VHAVYYEKKD KGAIVEITEK CVECGICKRV CKFGAIENDA
     PLESVITCSS CPIQCKVPLG ETGACTRYRN VGGKLVRDRE LVVEALEQKE AADNIKKPII
     TAVGAGTNYP CSKPAPHIVS ECRDGVDVVT VVTEAPLSYS GLVIKLDTNT YIGEEGDPVY
     RDGKVVGMVN TEEYGSKMIA IGGANRLTGD NGFATARTIV ELANGEEVEL KVNKKIVLKL
     KAGVAPVIDG VEESIMRIGC GSATVGLFAK RMKDAVDECI VIDHHVIGLC SEHLAGEAVG
     MTWSGIIPNA TKSSRGRYFG GHGSGIGGTS LETPRDAIKG ADMSIAKAGM QVMVVNTTGE
     IYALFELKAD GSFDEIPMTE AALGVALAIQ DNCQRSMTSI LYTGGTGGSA RGGVCTHPVK
     ITEAVHEQKA VLTIGGAPAF VYPGGGINFM VDTQKVVNKA FTWVPTPATV APVEYTMTVA
     DYEAMGGHMD QIKDVSEYK
//
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