NADA_METB6
ID NADA_METB6 Reviewed; 302 AA.
AC A7IA72;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Quinolinate synthase {ECO:0000255|HAMAP-Rule:MF_00568};
DE EC=2.5.1.72 {ECO:0000255|HAMAP-Rule:MF_00568};
GN Name=nadA {ECO:0000255|HAMAP-Rule:MF_00568}; OrderedLocusNames=Mboo_2119;
OS Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanoregulaceae; Methanoregula.
OX NCBI_TaxID=456442;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21154 / JCM 14090 / 6A8;
RX PubMed=25998264; DOI=10.1099/mic.0.000117;
RA Braeuer S., Cadillo-Quiroz H., Kyrpides N., Woyke T., Goodwin L.,
RA Detter C., Podell S., Yavitt J.B., Zinder S.H.;
RT "Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic
RT peatland environments.";
RL Microbiology 161:1572-1581(2015).
CC -!- FUNCTION: Catalyzes the condensation of iminoaspartate with
CC dihydroxyacetone phosphate to form quinolinate. {ECO:0000255|HAMAP-
CC Rule:MF_00568}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dihydroxyacetone phosphate + iminosuccinate = H(+) + 2 H2O +
CC phosphate + quinolinate; Xref=Rhea:RHEA:25888, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29959, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57642, ChEBI:CHEBI:77875; EC=2.5.1.72;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00568};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25889;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00568};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00568};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00568};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC iminoaspartate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00568}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00568}.
CC -!- SIMILARITY: Belongs to the quinolinate synthase family. Type 2
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00568}.
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DR EMBL; CP000780; ABS56633.1; -; Genomic_DNA.
DR RefSeq; WP_012107691.1; NC_009712.1.
DR AlphaFoldDB; A7IA72; -.
DR SMR; A7IA72; -.
DR STRING; 456442.Mboo_2119; -.
DR PRIDE; A7IA72; -.
DR EnsemblBacteria; ABS56633; ABS56633; Mboo_2119.
DR GeneID; 5411217; -.
DR KEGG; mbn:Mboo_2119; -.
DR eggNOG; arCOG04459; Archaea.
DR HOGENOM; CLU_047382_0_0_2; -.
DR OMA; CFCSTMN; -.
DR OrthoDB; 18897at2157; -.
DR UniPathway; UPA00253; UER00327.
DR Proteomes; UP000002408; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008987; F:quinolinate synthetase A activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.10800; -; 3.
DR HAMAP; MF_00568; NadA_type2; 1.
DR InterPro; IPR003473; NadA.
DR InterPro; IPR036094; NadA_sf.
DR InterPro; IPR023066; Quinolinate_synth_type2.
DR PANTHER; PTHR30573; PTHR30573; 1.
DR Pfam; PF02445; NadA; 1.
DR SUPFAM; SSF142754; SSF142754; 1.
DR TIGRFAMs; TIGR00550; nadA; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Metal-binding;
KW Pyridine nucleotide biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..302
FT /note="Quinolinate synthase"
FT /id="PRO_1000146814"
FT BINDING 25
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
FT BINDING 42
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
FT BINDING 87
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
FT BINDING 113..115
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
FT BINDING 130
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
FT BINDING 172
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
FT BINDING 198..200
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
FT BINDING 215
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
FT BINDING 260
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
SQ SEQUENCE 302 AA; 32791 MW; 63FA9D763B4F574F CRC64;
MDDTALLQEE ILRLKEKKNA ILLAHNYQRP EVQDIADLTG DSLELARAAA AMQGDTIVFC
GVDFMAETAA ILAPDKTVLL PAADACCPMA EMVTAEELRF ARARHPGAAV VCYVNTTAGV
KAESDICCTS ANAISVVNSL TEDRVIFVPD KNLGRYAARF TEKKVLPWEG FCLVHDRYTP
DDVARAKDAH PGAAVVVHPE CRPEVIDLAD HVASTSGIIR YVQTSPGSEF IIGTEIGILH
RLSKECPGKR CFPLSDKAVC VNMKKTTLVH VRDALVTGQP RITVPDEIAS RARRAIGRML
AL
