NDSFS_EUBBA
ID NDSFS_EUBBA Reviewed; 157 AA.
AC Q0QLF3;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Nicotinate dehydrogenase small FeS subunit {ECO:0000312|EMBL:ABC88397.1};
DE Short=NDH {ECO:0000303|PubMed:19549881};
DE EC=1.17.1.5;
DE AltName: Full=Nicotinic acid hydroxylase small FeS subunit {ECO:0000303|PubMed:8555176};
DE Short=NAH {ECO:0000303|PubMed:8555176};
GN Name=ndhS;
OS Eubacterium barkeri (Clostridium barkeri).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=1528;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABC88397.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
RC STRAIN=ATCC 25849 / DSM 1223 / JCM 1389 / NCIMB 10623 / VKM B-1775 / VPI
RC 5359 {ECO:0000312|EMBL:ABC88397.1};
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 Eubacterium
RT barkeri.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:12341-12346(2006).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 1-10, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND SUBUNIT.
RC STRAIN=ATCC 25849 / DSM 1223 / JCM 1389 / NCIMB 10623 / VKM B-1775 / VPI
RC 5359 {ECO:0000269|PubMed:8555176};
RX PubMed=8555176; DOI=10.1021/bi951793i;
RA Gladyshev V.N., Khangulov S.V., Stadtman T.C.;
RT "Properties of the selenium- and molybdenum-containing nicotinic acid
RT hydroxylase from Clostridium barkeri.";
RL Biochemistry 35:212-223(1996).
RN [3] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH FAD; IRON-SULFUR
RP CLUSTERS; NDHM; NDHL AND NDHF, COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 25849 / DSM 1223 / JCM 1389 / NCIMB 10623 / VKM B-1775 / VPI
RC 5359 {ECO:0000269|PubMed:19549881};
RX PubMed=19549881; DOI=10.1073/pnas.0902210106;
RA Wagener N., Pierik A.J., Ibdah A., Hille R., Dobbek H.;
RT "The Mo-Se active site of nicotinate dehydrogenase.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:11055-11060(2009).
CC -!- FUNCTION: Catalyzes the hydroxylation of nicotinate to 6-
CC hydroxynicotinate. Also active against 2-pyrazinecarboxylic acid, but
CC inactive against other nicotinate analogs.
CC {ECO:0000269|PubMed:8555176}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NADP(+) + nicotinate = 6-hydroxynicotinate + H(+) +
CC NADPH; Xref=Rhea:RHEA:12236, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32544, ChEBI:CHEBI:57664, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.17.1.5;
CC Evidence={ECO:0000269|PubMed:8555176};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:19549881, ECO:0000269|PubMed:8555176};
CC Note=Binds 2 [2Fe-2S] clusters per subunit.
CC {ECO:0000269|PubMed:19549881, ECO:0000269|PubMed:8555176};
CC -!- ACTIVITY REGULATION: Reversibly inactivated by selenide and sulfide.
CC Not inhibited by cyanide. {ECO:0000269|PubMed:8555176}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Most stable at pH 8.0. Unstable at acidic pH values.
CC {ECO:0000269|PubMed:8555176};
CC -!- PATHWAY: Cofactor degradation; nicotinate degradation; 6-
CC hydroxynicotinate from nicotinate: step 1/1.
CC {ECO:0000269|PubMed:16894175}.
CC -!- SUBUNIT: Heterooctamer of NDHM, NDHL, NDHS and NDHF. Dimer of
CC heterotetramers. {ECO:0000269|PubMed:19549881,
CC ECO:0000269|PubMed:8555176}.
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DR EMBL; DQ310789; ABC88397.1; -; Genomic_DNA.
DR PDB; 3HRD; X-ray; 2.20 A; D/H=1-157.
DR PDBsum; 3HRD; -.
DR AlphaFoldDB; Q0QLF3; -.
DR SMR; Q0QLF3; -.
DR DIP; DIP-48912N; -.
DR IntAct; Q0QLF3; 1.
DR STRING; 1528.SAMN04488579_11215; -.
DR KEGG; ag:ABC88397; -.
DR BioCyc; MetaCyc:MON-11708; -.
DR UniPathway; UPA01010; UER01011.
DR EvolutionaryTrace; Q0QLF3; -.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050138; F:nicotinate dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:1901848; P:nicotinate catabolic process; IDA:UniProtKB.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR InterPro; IPR002888; 2Fe-2S-bd.
DR InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF01799; Fer2_2; 1.
DR SUPFAM; SSF47741; SSF47741; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Direct protein sequencing; Iron; Iron-sulfur;
KW Metal-binding; NADP; Nucleotide-binding; Oxidoreductase.
FT CHAIN 1..157
FT /note="Nicotinate dehydrogenase small FeS subunit"
FT /id="PRO_0000404246"
FT DOMAIN 4..80
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 42
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465,
FT ECO:0000269|PubMed:19549881"
FT BINDING 47
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465,
FT ECO:0000269|PubMed:19549881"
FT BINDING 50
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465,
FT ECO:0000269|PubMed:19549881"
FT BINDING 62
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465,
FT ECO:0000269|PubMed:19549881"
FT BINDING 101
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465,
FT ECO:0000269|PubMed:19549881"
FT BINDING 104
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465,
FT ECO:0000269|PubMed:19549881"
FT BINDING 136
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465,
FT ECO:0000269|PubMed:19549881"
FT BINDING 138
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465,
FT ECO:0000269|PubMed:19549881"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:3HRD"
FT HELIX 25..30
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:3HRD"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:3HRD"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:3HRD"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:3HRD"
FT HELIX 88..96
FT /evidence="ECO:0007829|PDB:3HRD"
FT HELIX 105..116
FT /evidence="ECO:0007829|PDB:3HRD"
FT HELIX 124..131
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:3HRD"
FT HELIX 142..157
FT /evidence="ECO:0007829|PDB:3HRD"
SQ SEQUENCE 157 AA; 16766 MW; 4750940AB90ED093 CRC64;
MNKITINLNL NGEARSIVTE PNKRLLDLLR EDFGLTSVKE GCSEGECGAC TVIFNGDPVT
TCCMLAGQAD ESTIITLEGV AEDGKPSLLQ QCFLEAGAVQ CGYCTPGMIL TAKALLDKNP
DPTDEEITVA MSGNLCRCTG YIKIHAAVRY AVERCAN
