(data stored in ACNUC10043 zone)

HOGENOM: METTP_1_PE1

ID   METTP_1_PE1                          STANDARD;      PRT;   306 AA.
AC   METTP_1_PE1; A0B530;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Quinolinate synthase A; EC=2.5.1 72; (METTP_1.PE1).
GN   Name=nadA; OrderedLocusNames=Mthe_0001;
OS   METHANOSAETA THERMOPHILA PT.
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosaetaceae; Methanosaeta.
OX   NCBI_TaxID=349307;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS METTP_1.PE1.
CC       Methanosaeta thermophila PT chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:A0B530_METTP
CC   -!- FUNCTION: Catalyzes the condensation of iminoaspartate with
CC       dihydroxyacetone phosphate to form quinolinate (By similarity).
CC   -!- CATALYTIC ACTIVITY: Glycerone phosphate + iminosuccinate =
CC       pyridine-2,3-dicarboxylate + 2 H(2)O + phosphate.
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit (By similarity).
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate
CC       from iminoaspartate: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the quinolinate synthase A family. Type 2
CC       subfamily.
CC   -!- GENE_FAMILY: HOG000222770 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A0B530; -.
DR   EMBL; CP000477; ABK13804.1; -; Genomic_DNA.
DR   RefSeq; YP_842444.1; NC_008553.1.
DR   ProteinModelPortal; A0B530; -.
DR   STRING; A0B530; -.
DR   GeneID; 4462856; -.
DR   GenomeReviews; CP000477_GR; Mthe_0001.
DR   KEGG; mtp:Mthe_0001; -.
DR   NMPDR; fig|349307.7.peg.1; -.
DR   eggNOG; arNOG04746; -.
DR   OMA; SMARMID; -.
DR   PhylomeDB; A0B530; -.
DR   ProtClustDB; CLSK960644; -.
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:HAMAP.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00568; NadA_type2; 1; -.
DR   InterPro; IPR003473; NadA.
DR   InterPro; IPR023066; Quinolinate_synth_type2.
DR   Pfam; PF02445; NadA; 1.
DR   TIGRFAMs; TIGR00550; NadA; 1.
DR   HOGENOMDNA; METTP_1.PE1; -.
KW   quinolinate synthetase complex, A subunit;
KW   4Fe-4S; Complete proteome; Cytoplasm; Iron; Iron-sulfur;
KW   Metal-binding; Pyridine nucleotide biosynthesis; Transferase.
SQ   SEQUENCE   306 AA;  UNKNOWN MW;  UNKNOWN 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
//

If you have problems or comments...

PBIL Back to PBIL home page