NDFS_EUBBA
ID NDFS_EUBBA Reviewed; 296 AA.
AC Q0QLF4;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Nicotinate dehydrogenase FAD-subunit {ECO:0000312|EMBL:ABC88396.1};
DE Short=NDH {ECO:0000303|PubMed:19549881};
DE EC=1.17.1.5;
DE AltName: Full=Nicotinic acid hydroxylase FAD-subunit {ECO:0000303|PubMed:8555176};
DE Short=NAH {ECO:0000303|PubMed:8555176};
GN Name=ndhF;
OS Eubacterium barkeri (Clostridium barkeri).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=1528;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABC88396.1}
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:ABC88396.1};
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 1-25, 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; NDHM; NDHS AND
RP NDHL, 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=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:19549881, ECO:0000269|PubMed:8555176};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:19549881,
CC 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; ABC88396.1; -; Genomic_DNA.
DR PDB; 3HRD; X-ray; 2.20 A; C/G=1-296.
DR PDBsum; 3HRD; -.
DR AlphaFoldDB; Q0QLF4; -.
DR SMR; Q0QLF4; -.
DR DIP; DIP-48911N; -.
DR IntAct; Q0QLF4; 3.
DR STRING; 1528.SAMN04488579_11216; -.
DR KEGG; ag:ABC88396; -.
DR BioCyc; MetaCyc:MON-11707; -.
DR UniPathway; UPA01010; UER01011.
DR EvolutionaryTrace; Q0QLF4; -.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0050138; F:nicotinate dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:1901848; P:nicotinate catabolic process; IDA:UniProtKB.
DR Gene3D; 3.30.43.10; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR005107; CO_DH_flav_C.
DR InterPro; IPR036683; CO_DH_flav_C_dom_sf.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR Pfam; PF03450; CO_deh_flav_C; 1.
DR Pfam; PF00941; FAD_binding_5; 1.
DR SMART; SM01092; CO_deh_flav_C; 1.
DR SUPFAM; SSF55447; SSF55447; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; FAD; Flavoprotein; NADP;
KW Oxidoreductase.
FT CHAIN 1..296
FT /note="Nicotinate dehydrogenase FAD-subunit"
FT /id="PRO_0000404245"
FT DOMAIN 1..179
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT BINDING 29..36
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:19549881"
FT BINDING 101
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:19549881"
FT BINDING 110..114
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:19549881"
FT BINDING 123
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:19549881"
FT BINDING 160
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:19549881"
FT BINDING 169
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:19549881"
FT BINDING 187
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:19549881"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:3HRD"
FT HELIX 12..21
FT /evidence="ECO:0007829|PDB:3HRD"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:3HRD"
FT HELIX 36..41
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:3HRD"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:3HRD"
FT HELIX 77..82
FT /evidence="ECO:0007829|PDB:3HRD"
FT HELIX 84..89
FT /evidence="ECO:0007829|PDB:3HRD"
FT HELIX 91..98
FT /evidence="ECO:0007829|PDB:3HRD"
FT HELIX 103..108
FT /evidence="ECO:0007829|PDB:3HRD"
FT HELIX 111..117
FT /evidence="ECO:0007829|PDB:3HRD"
FT HELIX 123..130
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:3HRD"
FT HELIX 148..153
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 168..175
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 181..188
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 198..208
FT /evidence="ECO:0007829|PDB:3HRD"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 212..221
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:3HRD"
FT HELIX 231..237
FT /evidence="ECO:0007829|PDB:3HRD"
FT HELIX 244..248
FT /evidence="ECO:0007829|PDB:3HRD"
FT HELIX 251..261
FT /evidence="ECO:0007829|PDB:3HRD"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:3HRD"
FT HELIX 268..290
FT /evidence="ECO:0007829|PDB:3HRD"
SQ SEQUENCE 296 AA; 32622 MW; B14B447981D8E7FD CRC64;
MKDFEFFAPK TLEEAKGLLH QYKDVPPAII AGGTDLVIEI NDRWEKPDVV IDIKKLKELE
YIRVEENTIH IGALSTFTQI ENHPFIRSHV RALYKAASQV GSPQIRNLGT IGGNLSTSSV
AGDGVSAMTT LDATVVLESV RGTRQMKLTD FFDGEGFKRR NALEADEIMT EVIIDRPDAH
SASAFYKLAK RKSLAISVIG GGMAVKVDDA GVCTWASMRG GCIGRYPLHF KQAEEMLVGA
PLTMETMEAT LPILHDTVYD MARARPSVLY KKESVQGVFK KLFVDILDQL EGGCNE
