NDMMS_EUBBA
ID NDMMS_EUBBA Reviewed; 330 AA.
AC Q0QLF1;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Nicotinate dehydrogenase medium molybdopterin subunit {ECO:0000312|EMBL:ABC88399.1};
DE Short=NDH {ECO:0000303|PubMed:19549881};
DE EC=1.17.1.5;
DE AltName: Full=Nicotinic acid hydroxylase medium molybdopterin subunit {ECO:0000303|PubMed:8555176};
DE Short=NAH {ECO:0000303|PubMed:8555176};
GN Name=ndhM;
OS Eubacterium barkeri (Clostridium barkeri).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=1528;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABC88399.1}
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:ABC88399.1};
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 COFACTOR; NDHL; 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; ABC88399.1; -; Genomic_DNA.
DR PDB; 3HRD; X-ray; 2.20 A; B/F=1-330.
DR PDBsum; 3HRD; -.
DR AlphaFoldDB; Q0QLF1; -.
DR SMR; Q0QLF1; -.
DR DIP; DIP-48914N; -.
DR IntAct; Q0QLF1; 1.
DR STRING; 1528.SAMN04488579_11213; -.
DR KEGG; ag:ABC88399; -.
DR BioCyc; MetaCyc:MON-11706; -.
DR UniPathway; UPA01010; UER01011.
DR EvolutionaryTrace; Q0QLF1; -.
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; 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; PF02738; Ald_Xan_dh_C2; 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 CHAIN 1..330
FT /note="Nicotinate dehydrogenase medium molybdopterin
FT subunit"
FT /id="PRO_0000404244"
FT ACT_SITE 289
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80457"
FT BINDING 45..49
FT /ligand="Se-Mo-molybdopterin cytosine dinucleotide"
FT /ligand_id="ChEBI:CHEBI:73094"
FT /evidence="ECO:0000269|PubMed:19549881"
FT BINDING 85..90
FT /ligand="Se-Mo-molybdopterin cytosine dinucleotide"
FT /ligand_id="ChEBI:CHEBI:73094"
FT /evidence="ECO:0000269|PubMed:19549881"
FT BINDING 211..223
FT /ligand="Se-Mo-molybdopterin cytosine dinucleotide"
FT /ligand_id="ChEBI:CHEBI:73094"
FT /evidence="ECO:0000269|PubMed:19549881"
FT BINDING 284..289
FT /ligand="Se-Mo-molybdopterin cytosine dinucleotide"
FT /ligand_id="ChEBI:CHEBI:73094"
FT /evidence="ECO:0000269|PubMed:19549881"
FT CONFLICT 10
FT /note="S -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 2..14
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 24..30
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:3HRD"
FT HELIX 49..61
FT /evidence="ECO:0007829|PDB:3HRD"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:3HRD"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:3HRD"
FT HELIX 89..113
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:3HRD"
FT HELIX 142..151
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:3HRD"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 182..194
FT /evidence="ECO:0007829|PDB:3HRD"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 200..213
FT /evidence="ECO:0007829|PDB:3HRD"
FT HELIX 217..236
FT /evidence="ECO:0007829|PDB:3HRD"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:3HRD"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:3HRD"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:3HRD"
FT STRAND 267..274
FT /evidence="ECO:0007829|PDB:3HRD"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:3HRD"
FT TURN 288..294
FT /evidence="ECO:0007829|PDB:3HRD"
FT HELIX 295..307
FT /evidence="ECO:0007829|PDB:3HRD"
FT HELIX 318..328
FT /evidence="ECO:0007829|PDB:3HRD"
SQ SEQUENCE 330 AA; 34476 MW; 1190FDAC03FB5C08 CRC64;
MKKRGKGVGS MWYGIGNTGL PNPAAAFVEI HGDGSANVMF GAADIGQGSG TAMAQIAAEE
LGLDYEKIHV TWGDTMVTPD GGATSASRQT LITGNAVILA CRQAKETLAK TAAEKLDCAP
EELSFRDNTV FITADPERSM TYGELMAAMK AAGRMAVGAG SYNPNTTGLA PENMSGIPFE
VYSYATTIAE VEVDTETGEV DVLKVVSAHD VGTPINRSMV EGQIEGGVTM GQGFVLMEEI
EVNTKNGAIK NPSMSKYIIP SNRDVPEIHS ILVESEGGPG PFGAKGVGEP ALIPMIPAVV
AAIEDALGTR FTHTPIMPKD IVAAVKAQEK
