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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   26-NOV-2014, entry version 52.
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: DHPS catalyzes the formation of the immediate precursor
CC       of folic acid. {ECO:0000256|RuleBase:RU361205}.
CC   -!- COFACTOR:
CC       Note=Binds 1 magnesium ion per subunit. Magnesium is required for
CC       activity, even if it interacts primarily with the substrate.
CC       {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   RefSeq; YP_868665.1; NC_008577.1.
DR   ProteinModelPortal; A0KTZ0; -.
DR   SMR; A0KTZ0; 3-273.
DR   STRING; 94122.Shewana3_1024; -.
DR   EnsemblBacteria; ABK47259; ABK47259; Shewana3_1024.
DR   GeneID; 4479367; -.
DR   KEGG; shn:Shewana3_1024; -.
DR   PATRIC; 23569682; VBISheSp134792_1288.
DR   eggNOG; COG0294; -.
DR   HOGENOM; HOG000217510; -.
DR   KO; K00796; -.
DR   OMA; DCWISVD; -.
DR   OrthoDB; EOG67T5P5; -.
DR   BioCyc; SSP94122:GJ9K-1057-MONOMER; -.
DR   UniPathway; UPA00077; UER00156.
DR   GO; GO:0004156; F:dihydropteroate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009396; P:folic acid-containing compound biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.20.20.20; -; 1.
DR   InterPro; IPR006390; DHP_synth.
DR   InterPro; IPR011005; Dihydropteroate_synth-like.
DR   InterPro; IPR000489; Pterin-binding.
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}.
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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