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Nicotinate dehydrogenase large molybdopterin subunit (NDH) (EC 1.17.1.5) (Nicotinic acid hydroxylase large molybdopterin subunit) (NAH)

 NDLMS_EUBBA             Reviewed;         425 AA.
Q0QLF2;
08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
05-SEP-2006, sequence version 1.
12-APR-2017, entry version 47.
RecName: Full=Nicotinate dehydrogenase large molybdopterin subunit {ECO:0000312|EMBL:ABC88398.1};
Short=NDH {ECO:0000303|PubMed:19549881};
EC=1.17.1.5;
AltName: Full=Nicotinic acid hydroxylase large molybdopterin subunit {ECO:0000303|PubMed:8555176};
Short=NAH {ECO:0000303|PubMed:8555176};
Name=ndhL;
Eubacterium barkeri (Clostridium barkeri).
Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae;
Eubacterium.
NCBI_TaxID=1528;
[1] {ECO:0000305, ECO:0000312|EMBL:ABC88398.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
STRAIN=ATCC 25849 / DSM 1223 / JCM 1389 / NCIB 10623
{ECO:0000312|EMBL:ABC88398.1};
PubMed=16894175; DOI=10.1073/pnas.0601635103;
Alhapel A., Darley D.J., Wagener N., Eckel E., Elsner N., Pierik A.J.;
"Molecular and functional analysis of nicotinate catabolism in
Eubacterium barkeri.";
Proc. Natl. Acad. Sci. U.S.A. 103:12341-12346(2006).
[2] {ECO:0000305}
PROTEIN SEQUENCE OF 2-26, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, AND SUBUNIT.
STRAIN=ATCC 25849 / DSM 1223 / JCM 1389 / NCIB 10623
{ECO:0000269|PubMed:8555176};
PubMed=8555176; DOI=10.1021/bi951793i;
Gladyshev V.N., Khangulov S.V., Stadtman T.C.;
"Properties of the selenium- and molybdenum-containing nicotinic acid
hydroxylase from Clostridium barkeri.";
Biochemistry 35:212-223(1996).
[3] {ECO:0000305}
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH COFACTOR; NDHM;
NDHS AND NDHF, AND SUBUNIT.
STRAIN=ATCC 25849 / DSM 1223 / JCM 1389 / NCIB 10623
{ECO:0000269|PubMed:19549881};
PubMed=19549881; DOI=10.1073/pnas.0902210106;
Wagener N., Pierik A.J., Ibdah A., Hille R., Dobbek H.;
"The Mo-Se active site of nicotinate dehydrogenase.";
Proc. Natl. Acad. Sci. U.S.A. 106:11055-11060(2009).
-!- FUNCTION: Catalyzes the hydroxylation of nicotinate to 6-
hydroxynicotinate. Also active against 2-pyrazinecarboxylic acid,
but inactive against other nicotinate analogs.
{ECO:0000269|PubMed:8555176}.
-!- CATALYTIC ACTIVITY: Nicotinate + H(2)O + NADP(+) = 6-
hydroxynicotinate + NADPH. {ECO:0000269|PubMed:8555176}.
-!- COFACTOR:
Name=Se-Mo-molybdopterin cytosine dinucleotide;
Xref=ChEBI:CHEBI:73094; Evidence={ECO:0000269|PubMed:8555176};
Note=Binds 1 Se-Mo-molybdopterin cytosine dinucleotide (Se-Mo-MCD)
cofactor per heterotetramer. The cofactor is bound between the
NdhL and NdhM subunits. {ECO:0000269|PubMed:8555176};
-!- ENZYME REGULATION: Reversibly inactivated by selenide and sulfide.
Not inhibited by cyanide. {ECO:0000269|PubMed:8555176}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Most stable at pH 8.0. Unstable at acidic pH values.
{ECO:0000269|PubMed:8555176};
-!- PATHWAY: Cofactor degradation; nicotinate degradation; 6-
hydroxynicotinate from nicotinate: step 1/1.
{ECO:0000269|PubMed:16894175}.
-!- SUBUNIT: Heterooctamer of NDHM, NDHL, NDHS and NDHF. Dimer of
heterotetramers. {ECO:0000269|PubMed:19549881,
ECO:0000269|PubMed:8555176}.
-!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
{ECO:0000255}.
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EMBL; DQ310789; ABC88398.1; -; Genomic_DNA.
PDB; 3HRD; X-ray; 2.20 A; A/E=1-425.
PDBsum; 3HRD; -.
ProteinModelPortal; Q0QLF2; -.
SMR; Q0QLF2; -.
DIP; DIP-48913N; -.
KEGG; ag:ABC88398; -.
KO; K20447; -.
BioCyc; MetaCyc:MONOMER-11705; -.
BRENDA; 1.17.1.5; 1459.
UniPathway; UPA01010; UER01011.
EvolutionaryTrace; Q0QLF2; -.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0050138; F:nicotinate dehydrogenase activity; IDA:UniProtKB.
GO; GO:0051187; P:cofactor catabolic process; IDA:UniProtKB.
Gene3D; 3.30.365.10; -; 2.
Gene3D; 3.90.1170.50; -; 1.
InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
InterPro; IPR008274; AldOxase/xan_DH_Mopterin-bd.
Pfam; PF01315; Ald_Xan_dh_C; 1.
Pfam; PF02738; Ald_Xan_dh_C2; 1.
SMART; SM01008; Ald_Xan_dh_C; 1.
SUPFAM; SSF54665; SSF54665; 1.
SUPFAM; SSF56003; SSF56003; 1.
1: Evidence at protein level;
3D-structure; Direct protein sequencing; Metal-binding; Molybdenum;
NADP; Oxidoreductase; Selenium.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:8555176}.
CHAIN 2 425 Nicotinate dehydrogenase large
molybdopterin subunit.
{ECO:0000269|PubMed:8555176}.
/FTId=PRO_0000404243.
REGION 238 240 Se-Mo-molybdopterin cytosine dinucleotide
binding. {ECO:0000269|PubMed:19549881}.
BINDING 208 208 Se-Mo-molybdopterin cytosine
dinucleotide.
{ECO:0000269|PubMed:19549881}.
HELIX 17 21 {ECO:0000244|PDB:3HRD}.
HELIX 28 30 {ECO:0000244|PDB:3HRD}.
STRAND 37 43 {ECO:0000244|PDB:3HRD}.
STRAND 45 55 {ECO:0000244|PDB:3HRD}.
HELIX 57 60 {ECO:0000244|PDB:3HRD}.
STRAND 65 69 {ECO:0000244|PDB:3HRD}.
HELIX 71 73 {ECO:0000244|PDB:3HRD}.
STRAND 82 84 {ECO:0000244|PDB:3HRD}.
STRAND 101 109 {ECO:0000244|PDB:3HRD}.
HELIX 110 119 {ECO:0000244|PDB:3HRD}.
STRAND 121 126 {ECO:0000244|PDB:3HRD}.
HELIX 133 137 {ECO:0000244|PDB:3HRD}.
STRAND 149 159 {ECO:0000244|PDB:3HRD}.
HELIX 161 166 {ECO:0000244|PDB:3HRD}.
STRAND 169 178 {ECO:0000244|PDB:3HRD}.
STRAND 190 195 {ECO:0000244|PDB:3HRD}.
STRAND 201 205 {ECO:0000244|PDB:3HRD}.
HELIX 210 220 {ECO:0000244|PDB:3HRD}.
HELIX 225 227 {ECO:0000244|PDB:3HRD}.
STRAND 228 232 {ECO:0000244|PDB:3HRD}.
TURN 239 242 {ECO:0000244|PDB:3HRD}.
HELIX 248 258 {ECO:0000244|PDB:3HRD}.
STRAND 262 265 {ECO:0000244|PDB:3HRD}.
HELIX 268 274 {ECO:0000244|PDB:3HRD}.
STRAND 281 289 {ECO:0000244|PDB:3HRD}.
STRAND 295 309 {ECO:0000244|PDB:3HRD}.
HELIX 313 323 {ECO:0000244|PDB:3HRD}.
STRAND 333 341 {ECO:0000244|PDB:3HRD}.
STRAND 343 345 {ECO:0000244|PDB:3HRD}.
TURN 351 354 {ECO:0000244|PDB:3HRD}.
HELIX 355 372 {ECO:0000244|PDB:3HRD}.
HELIX 377 384 {ECO:0000244|PDB:3HRD}.
HELIX 404 419 {ECO:0000244|PDB:3HRD}.
SEQUENCE 425 AA; 46488 MW; F8270B4ABECD71A5 CRC64;
MGKDYQVLGK NKVKVDSLEK VMGTAKFAAD YSFPDMLYAG VFRSTVPHAR IVSLDLSKAR
AIDGVEAVLD YHAIPGKNRF GIIIKDEPCL VDDKVRRYGD AIAVVAAQTP DLVQEALDAI
TIEYEELEGI FTMERALEED SPAIHGDTNI HQVKHLEYGD VDAAFKQCDI VVEDTYSTHR
LTHMFIEPDA GVSYYDNEGM LTVVVSTQNP HYDRGEVAGM LALPNSKVRI IQATTGGGFG
GKLDLSVQCH CALLTYHTKK PVKMVRSREE STTVSSKRHP MTMHCKTGAT KDGRLQAVQV
EMFGDTGAYA SYGPAVITRA TVHCMGPYVV PNVRVDAKFV YTNNPMSGAF RGFGVPQASV
CHEGQMNALA KALGMDPIDI RILNAHQVGA KLATGQVLEN SVGLIETLEK AREKAVEVMG
YEKTR


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