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Database: UniProt/TrEMBL
Entry: A0KTZ0_SHESA
LinkDB: A0KTZ0_SHESA
Original site: A0KTZ0_SHESA 
ID   A0KTZ0_SHESA            Unreviewed;       277 AA.
AC   A0KTZ0;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   30-NOV-2016, entry version 68.
DE   RecName: Full=Dihydropteroate synthase {ECO:0000256|RuleBase:RU361205};
DE            Short=DHPS {ECO:0000256|RuleBase:RU361205};
DE            EC=2.5.1.15 {ECO:0000256|RuleBase:RU361205};
DE   AltName: Full=Dihydropteroate pyrophosphorylase {ECO:0000256|RuleBase:RU361205};
GN   OrderedLocusNames=Shewana3_1024 {ECO:0000313|EMBL:ABK47259.1};
OS   Shewanella sp. (strain ANA-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=94122 {ECO:0000313|EMBL:ABK47259.1, ECO:0000313|Proteomes:UP000002589};
RN   [1] {ECO:0000313|Proteomes:UP000002589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANA-3 {ECO:0000313|Proteomes:UP000002589};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Newman D., Salticov C., Konstantinidis K., Klappenback J.,
RA   Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA)
CC       with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to
CC       form 7,8-dihydropteroate (H2Pte), the immediate precursor of
CC       folate derivatives. {ECO:0000256|RuleBase:RU361205}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU361205};
CC   -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis;
CC       7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-
CC       dihydropteridine diphosphate and 4-aminobenzoate: step 1/2.
CC       {ECO:0000256|RuleBase:RU361205}.
CC   -!- SIMILARITY: Belongs to the DHPS family.
CC       {ECO:0000256|RuleBase:RU361205}.
CC   -!- SIMILARITY: Contains 1 pterin-binding domain.
CC       {ECO:0000256|RuleBase:RU361205}.
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DR   EMBL; CP000469; ABK47259.1; -; Genomic_DNA.
DR   RefSeq; WP_011716138.1; NC_008577.1.
DR   ProteinModelPortal; A0KTZ0; -.
DR   STRING; 94122.Shewana3_1024; -.
DR   EnsemblBacteria; ABK47259; ABK47259; Shewana3_1024.
DR   KEGG; shn:Shewana3_1024; -.
DR   PATRIC; 23569682; VBISheSp134792_1288.
DR   eggNOG; ENOG4105EEI; Bacteria.
DR   eggNOG; COG0294; LUCA.
DR   HOGENOM; HOG000217510; -.
DR   KO; K00796; -.
DR   OMA; SIDTYHA; -.
DR   OrthoDB; POG091H00BJ; -.
DR   BioCyc; SSP94122:GJ9K-1050-MONOMER; -.
DR   UniPathway; UPA00077; UER00156.
DR   Proteomes; UP000002589; Chromosome.
DR   GO; GO:0004156; F:dihydropteroate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00739; DHPS; 1.
DR   Gene3D; 3.20.20.20; -; 1.
DR   InterPro; IPR006390; DHP_synth.
DR   InterPro; IPR011005; Dihydropteroate_synth-like.
DR   InterPro; IPR000489; Pterin-binding_dom.
DR   Pfam; PF00809; Pterin_bind; 1.
DR   SUPFAM; SSF51717; SSF51717; 1.
DR   TIGRFAMs; TIGR01496; DHPS; 1.
DR   PROSITE; PS00792; DHPS_1; 1.
DR   PROSITE; PS00793; DHPS_2; 1.
DR   PROSITE; PS50972; PTERIN_BINDING; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000002589};
KW   Folate biosynthesis {ECO:0000256|RuleBase:RU361205};
KW   Magnesium {ECO:0000256|RuleBase:RU361205};
KW   Metal-binding {ECO:0000256|RuleBase:RU361205};
KW   Transferase {ECO:0000256|RuleBase:RU361205,
KW   ECO:0000313|EMBL:ABK47259.1}.
FT   DOMAIN       16    268       Pterin-binding. {ECO:0000259|PROSITE:
FT                                PS50972}.
SQ   SEQUENCE   277 AA;  30012 MW;  082F2A95B7E07F00 CRC64;
     MFELIAGTKR LSLASPVVMG ILNVTPDSFS DGGKFSSFEL ACQHADEMVA QGALIIDIGG
     ESTRPGAADV SVQDELARVI PLVEYVAKHH DVWISVDTSK PEVMRQAVNA GAHLINDVRA
     LLEPGALETA AQLNVPICLM HMQGAPRSMQ TAPEYQDLVA DVSEFLYERI QACIDAGIPR
     ERLLIDPGFG FGKTLEHNYE LLAKLDSFEQ FELPILIGLS RKSMIGNLLA RPTSERLAGS
     LAGAMIAAQK GAHIIRVHDV PETVDMLKVL QATQAYL
//
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