NDLMS_EUBBA
ID NDLMS_EUBBA Reviewed; 425 AA.
AC Q0QLF2;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Nicotinate dehydrogenase large molybdopterin subunit {ECO:0000312|EMBL:ABC88398.1};
DE Short=NDH {ECO:0000303|PubMed:19549881};
DE EC=1.17.1.5;
DE AltName: Full=Nicotinic acid hydroxylase large molybdopterin subunit {ECO:0000303|PubMed:8555176};
DE Short=NAH {ECO:0000303|PubMed:8555176};
GN Name=ndhL;
OS Eubacterium barkeri (Clostridium barkeri).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=1528;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABC88398.1}
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:ABC88398.1};
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 2-26, 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 COFACTOR; NDHM; NDHS
RP AND NDHF, 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=Se-Mo-molybdopterin cytosine dinucleotide; Xref=ChEBI:CHEBI:73094;
CC Evidence={ECO:0000269|PubMed:8555176};
CC Note=Binds 1 Se-Mo-molybdopterin cytosine dinucleotide (Se-Mo-MCD)
CC cofactor per heterotetramer. The cofactor is bound between the NdhL and
CC NdhM subunits. {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}.
CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC {ECO:0000255}.
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DR EMBL; DQ310789; ABC88398.1; -; Genomic_DNA.
DR PDB; 3HRD; X-ray; 2.20 A; A/E=1-425.
DR PDBsum; 3HRD; -.
DR AlphaFoldDB; Q0QLF2; -.
DR SMR; Q0QLF2; -.
DR DIP; DIP-48913N; -.
DR IntAct; Q0QLF2; 1.
DR STRING; 1528.SAMN04488579_11214; -.
DR KEGG; ag:ABC88398; -.
DR BioCyc; MetaCyc:MON-11705; -.
DR BRENDA; 1.17.1.5; 1459.
DR UniPathway; UPA01010; UER01011.
DR EvolutionaryTrace; Q0QLF2; -.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0050138; F:nicotinate dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:1901848; P:nicotinate catabolic process; IDA:UniProtKB.
DR InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
DR InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
DR InterPro; IPR016208; Ald_Oxase/xanthine_DH.
DR InterPro; IPR008274; AldOxase/xan_DH_Mopterin-bd.
DR InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
DR PANTHER; PTHR11908; PTHR11908; 1.
DR Pfam; PF01315; Ald_Xan_dh_C; 1.
DR Pfam; PF02738; Ald_Xan_dh_C2; 1.
DR SMART; SM01008; Ald_Xan_dh_C; 1.
DR SUPFAM; SSF54665; SSF54665; 1.
DR SUPFAM; SSF56003; SSF56003; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Metal-binding; Molybdenum; NADP;
KW Oxidoreductase; Selenium.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8555176"
FT CHAIN 2..425
FT /note="Nicotinate dehydrogenase large molybdopterin
FT subunit"
FT /evidence="ECO:0000269|PubMed:8555176"
FT /id="PRO_0000404243"
FT BINDING 208
FT /ligand="Se-Mo-molybdopterin cytosine dinucleotide"
FT /ligand_id="ChEBI:CHEBI:73094"
FT /evidence="ECO:0000269|PubMed:19549881"
FT BINDING 238..240
FT /ligand="Se-Mo-molybdopterin cytosine dinucleotide"
FT /ligand_id="ChEBI:CHEBI:73094"
FT /evidence="ECO:0000269|PubMed:19549881"
FT HELIX 17..21
FT /evidence="ECO:0007829|PDB:3HRD"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 45..55
FT /evidence="ECO:0007829|PDB:3HRD"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:3HRD"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 101..109
FT /evidence="ECO:0007829|PDB:3HRD"
FT HELIX 110..119
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:3HRD"
FT HELIX 133..137
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 149..159
FT /evidence="ECO:0007829|PDB:3HRD"
FT HELIX 161..166
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 169..178
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:3HRD"
FT HELIX 210..220
FT /evidence="ECO:0007829|PDB:3HRD"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:3HRD"
FT TURN 239..242
FT /evidence="ECO:0007829|PDB:3HRD"
FT HELIX 248..258
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:3HRD"
FT HELIX 268..274
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 281..289
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 295..309
FT /evidence="ECO:0007829|PDB:3HRD"
FT HELIX 313..323
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 333..341
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:3HRD"
FT TURN 351..354
FT /evidence="ECO:0007829|PDB:3HRD"
FT HELIX 355..372
FT /evidence="ECO:0007829|PDB:3HRD"
FT HELIX 377..384
FT /evidence="ECO:0007829|PDB:3HRD"
FT HELIX 404..419
FT /evidence="ECO:0007829|PDB:3HRD"
SQ 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
