(data stored in SCRATCH zone)

SWISSPROT: D7A403_STAND

ID   D7A403_STAND            Unreviewed;       356 AA.
AC   D7A403;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   16-JAN-2019, entry version 55.
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=Snov_0490 {ECO:0000313|EMBL:ADH87823.1};
OS   Starkeya novella (strain ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 /
OS   NBRC 12443 / NCIB 9113).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Xanthobacteraceae; Starkeya.
OX   NCBI_TaxID=639283 {ECO:0000313|EMBL:ADH87823.1, ECO:0000313|Proteomes:UP000006633};
RN   [1] {ECO:0000313|Proteomes:UP000006633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB
RC   9113 {ECO:0000313|Proteomes:UP000006633};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Brettin T., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Beatson S., Kappler U.,
RA   Woyke T.;
RT   "Complete sequence of Starkeya novella DSM 506.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADH87823.1, ECO:0000313|Proteomes:UP000006633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB
RC   9113 {ECO:0000313|Proteomes:UP000006633};
RX   PubMed=23450099; DOI=10.4056/sigs.3006378;
RA   Kappler U., Davenport K., Beatson S., Lucas S., Lapidus A.,
RA   Copeland A., Berry K.W., Glavina Del Rio T., Hammon N., Dalin E.,
RA   Tice H., Pitluck S., Richardson P., Bruce D., Goodwin L.A., Han C.,
RA   Tapia R., Detter J.C., Chang Y.J., Jeffries C.D., Land M., Hauser L.,
RA   Kyrpides N.C., Goker M., Ivanova N., Klenk H.P., Woyke T.;
RT   "Complete genome sequence of the facultatively chemolithoautotrophic
RT   and methylotrophic alpha Proteobacterium Starkeya novella type strain
RT   (ATCC 8093(T)).";
RL   Stand. Genomic Sci. 7:44-58(2012).
CC   -!- FUNCTION: Catalyzes the condensation of iminoaspartate with
CC       dihydroxyacetone phosphate to form quinolinate.
CC       {ECO:0000256|HAMAP-Rule:MF_00568, ECO:0000256|SAAS:SAAS00883591}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dihydroxyacetone phosphate + iminosuccinate = H(+) + 2
CC         H2O + phosphate + quinolinate; Xref=Rhea:RHEA:25888,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29959,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57642, ChEBI:CHEBI:77875;
CC         EC=2.5.1.72; Evidence={ECO:0000256|HAMAP-Rule:MF_00568,
CC         ECO:0000256|SAAS:SAAS01116083};
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:SAAS00883494}.
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; CP002026; ADH87823.1; -; Genomic_DNA.
DR   STRING; 639283.Snov_0490; -.
DR   EnsemblBacteria; ADH87823; ADH87823; Snov_0490.
DR   KEGG; sno:Snov_0490; -.
DR   eggNOG; ENOG4105D0I; Bacteria.
DR   eggNOG; COG0379; LUCA.
DR   HOGENOM; HOG000222770; -.
DR   KO; K03517; -.
DR   OMA; LWAPDRH; -.
DR   BioCyc; SNOV639283:G1GLM-495-MONOMER; -.
DR   UniPathway; UPA00253; UER00327.
DR   Proteomes; UP000006633; 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   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; D7A403.
DR   SWISS-2DPAGE; D7A403.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00568,
KW   ECO:0000256|SAAS:SAAS00883558};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006633};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00568};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00568, ECO:0000256|SAAS:SAAS00883499};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00568,
KW   ECO:0000256|SAAS:SAAS00883597};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00568,
KW   ECO:0000256|SAAS:SAAS00883634};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00568,
KW   ECO:0000256|SAAS:SAAS00883480};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006633};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00568,
KW   ECO:0000256|SAAS:SAAS00883490}.
FT   BINDING      74     74       Iminoaspartate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00568}.
FT   BINDING      92     92       Iminoaspartate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00568}.
FT   BINDING     163    163       Iminoaspartate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00568}.
FT   BINDING     180    180       Iminoaspartate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00568}.
FT   BINDING     253    253       Iminoaspartate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00568}.
FT   BINDING     270    270       Iminoaspartate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00568}.
SQ   SEQUENCE   356 AA;  39195 MW;  EF676BFA59F1130C CRC64;
     MLDLDVAARM GTTEDFAPDL APANAPSSPS ALPLAHLYER VSKHVTPAEW PLIVRDVEAI
     ERLKKQRNAV VLGHNYQAPE IFNTVADIVG DSLALAREAV TVDADVIVMA GVHFMAETAK
     LLNPSKIVLM PDMEAGCSLA ESITAEDIRL LRQRYPGVPV VTYVNTSAEV KAESDYCCTS
     GNAVKVVRAV AKEWGVNRIL MLPDEYLARN VQKEVPEIEL IAWKGHCEVH ERFTPQDIRD
     LRENHPGVVV LAHPECPPEV VAAADYAGST AGMADYVRDE KPARVVLITE CSMADNVAVN
     HPDVEFVRPC NLCPHMRRIT LPNIRRALET MGHQVEIDPA VADRARLAVE RMLAIR
//

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