(data stored in ACNUC10043 zone)

SWISSPROT: A0B530_METTP

ID   A0B530_METTP            Unreviewed;       306 AA.
AC   A0B530;
DT   28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2006, sequence version 1.
DT   11-DEC-2019, entry version 73.
DE   RecName: Full=Quinolinate synthase A {ECO:0000256|HAMAP-Rule:MF_00568};
DE            EC=2.5.1.72 {ECO:0000256|HAMAP-Rule:MF_00568};
GN   Name=nadA {ECO:0000256|HAMAP-Rule:MF_00568};
GN   OrderedLocusNames=Mthe_0001 {ECO:0000313|EMBL:ABK13804.1};
OS   Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 /
OS   PT) (Methanosaeta thermophila).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanotrichaceae; Methanothrix.
OX   NCBI_TaxID=349307 {ECO:0000313|EMBL:ABK13804.1, ECO:0000313|Proteomes:UP000000674};
RN   [1] {ECO:0000313|EMBL:ABK13804.1, ECO:0000313|Proteomes:UP000000674}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6194 / JCM 14653 / NBRC 101360 / PT
RC   {ECO:0000313|Proteomes:UP000000674};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Smith K.S., Ingram-Smith C., Richardson P.;
RT   "Complete sequence of Methanosaeta thermophila PT.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the condensation of iminoaspartate with
CC       dihydroxyacetone phosphate to form quinolinate. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00568};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00568};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00568};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC       iminoaspartate: step 1/1. {ECO:0000256|HAMAP-Rule:MF_00568}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00568}.
CC   -!- SIMILARITY: Belongs to the quinolinate synthase A family. Type 2
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00568}.
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DR   EMBL; CP000477; ABK13804.1; -; Genomic_DNA.
DR   EnsemblBacteria; ABK13804; ABK13804; Mthe_0001.
DR   KEGG; mtp:Mthe_0001; -.
DR   eggNOG; arCOG04459; Archaea.
DR   eggNOG; COG0379; LUCA.
DR   HOGENOM; HOG000222770; -.
DR   KO; K03517; -.
DR   OMA; LWAPDRH; -.
DR   UniPathway; UPA00253; UER00327.
DR   Proteomes; UP000000674; 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;
DR   PRODOM; A0B530.
DR   SWISS-2DPAGE; A0B530.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00568};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00568};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00568};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00568};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00568};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00568};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000674};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00568}.
FT   BINDING         29
FT                   /note="Iminoaspartate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00568"
FT   BINDING         46
FT                   /note="Iminoaspartate; via amide nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00568"
FT   BINDING         117
FT                   /note="Iminoaspartate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00568"
FT   BINDING         134
FT                   /note="Iminoaspartate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00568"
FT   BINDING         202
FT                   /note="Iminoaspartate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00568"
FT   BINDING         219
FT                   /note="Iminoaspartate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00568"
SQ   SEQUENCE   306 AA;  33881 MW;  ADBC610B1D5153E4 CRC64;
     MTYHQIRTIM FEKEILRLKS ERNAIILAHN YQPGDVQDIA DLTGDSLELS RAAATIDCKV
     LVFCGVDFMA ETAAILSPEK IVIHPDTSAC CPMAQMISPH DVRSLREKHP DAAVVCYVNS
     SADVKAESDI CCTSANGVQV VNALDADEIL FIPDRNLAAY VARHTDKRII PWDGYCYVHD
     RYTASDVSEA RKKHPDAELL VHPECRPEVI DMADGVYSTS GMLKHARASG ANEFIIGTEV
     GILHRLCAEN PEKMFYPLSS GAVCEDMKKI SLKKVLRALE TLSPRVEVPQ TTAVRARRAI
     ERMLAV
//

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