(data stored in SCRATCH zone)

SWISSPROT: B8IUG9_METNO

ID   B8IUG9_METNO            Unreviewed;       333 AA.
AC   B8IUG9;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   07-JUN-2017, entry version 67.
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=Mnod_0168 {ECO:0000313|EMBL:ACL55214.1};
OS   Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=460265 {ECO:0000313|EMBL:ACL55214.1, ECO:0000313|Proteomes:UP000008207};
RN   [1] {ECO:0000313|EMBL:ACL55214.1, ECO:0000313|Proteomes:UP000008207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060
RC   {ECO:0000313|Proteomes:UP000008207};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium nodulans ORS
RT   2060.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the condensation of iminoaspartate with
CC       dihydroxyacetone phosphate to form quinolinate.
CC       {ECO:0000256|HAMAP-Rule:MF_00568, ECO:0000256|SAAS:SAAS00772104}.
CC   -!- CATALYTIC ACTIVITY: Glycerone phosphate + iminosuccinate =
CC       pyridine-2,3-dicarboxylate + 2 H(2)O + phosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_00568, ECO:0000256|SAAS:SAAS00772083}.
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
CC       from iminoaspartate: step 1/1. {ECO:0000256|HAMAP-Rule:MF_00568,
CC       ECO:0000256|SAAS:SAAS00772086}.
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; CP001349; ACL55214.1; -; Genomic_DNA.
DR   RefSeq; WP_015926927.1; NC_011894.1.
DR   ProteinModelPortal; B8IUG9; -.
DR   STRING; 460265.Mnod_0168; -.
DR   EnsemblBacteria; ACL55214; ACL55214; Mnod_0168.
DR   KEGG; mno:Mnod_0168; -.
DR   eggNOG; ENOG4105D0I; Bacteria.
DR   eggNOG; COG0379; LUCA.
DR   HOGENOM; HOG000222770; -.
DR   KO; K03517; -.
DR   OMA; DKCLGEN; -.
DR   OrthoDB; POG091H03D2; -.
DR   UniPathway; UPA00253; UER00327.
DR   Proteomes; UP000008207; 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:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008987; F:quinolinate synthetase A activity; IEA:UniProtKB-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:UniProtKB-HAMAP.
DR   HAMAP; MF_00568; NadA_type2; 1.
DR   InterPro; IPR003473; NadA.
DR   InterPro; IPR023066; Quinolinate_synth_type2.
DR   PANTHER; PTHR30573:SF4; PTHR30573:SF4; 1.
DR   Pfam; PF02445; NadA; 1.
DR   SUPFAM; SSF142754; SSF142754; 1.
DR   TIGRFAMs; TIGR00550; nadA; 1.
PE   3: Inferred from homology;
DR   PRODOM; B8IUG9.
DR   SWISS-2DPAGE; B8IUG9.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00568,
KW   ECO:0000256|SAAS:SAAS00772053};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008207};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00568};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00568, ECO:0000256|SAAS:SAAS00772070};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00568,
KW   ECO:0000256|SAAS:SAAS00772098};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00568,
KW   ECO:0000256|SAAS:SAAS00772100};
KW   Methyltransferase {ECO:0000313|EMBL:ACL55214.1};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00568,
KW   ECO:0000256|SAAS:SAAS00772063};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008207};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00568,
KW   ECO:0000256|SAAS:SAAS00772051, ECO:0000313|EMBL:ACL55214.1}.
FT   BINDING      54     54       Iminoaspartate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00568}.
FT   BINDING      72     72       Iminoaspartate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00568}.
FT   BINDING     143    143       Iminoaspartate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00568}.
FT   BINDING     160    160       Iminoaspartate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00568}.
FT   BINDING     229    229       Iminoaspartate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00568}.
FT   BINDING     246    246       Iminoaspartate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00568}.
SQ   SEQUENCE   333 AA;  36032 MW;  B4CBAA5F40D8E458 CRC64;
     MAAVTQAVQE ALPLPDLYAR VKGHVPAIEW PALAEDVAAI QMLKRQRNAV VLAHNYQAPE
     IFHTVADIVG DSLALAREAA RTDADVIVLA GVHFMAETAK LLNPEKTVLI PDQAAGCSLA
     DSITAADVRA LRRSHPGVPI VTYVNTSAAV KAESDLCCTS GNAKAVVESL GVPRVLMIPD
     EYLARNVQAE LPQVEILSWA GHCEVHERFS PADIREVREA YPGVTVLAHP ECPPEVVAEA
     DFAGSTAAMQ DFVETRRPAQ VVMITECSMA DNLAVRNPEV AFVKPCNLCP HMKRISLSKI
     RRALETMTHE VTVPSDLIAP ARRAVERMLA VRP
//

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