(data stored in ACNUC7421 zone)

SWISSPROT: A4AVV7_MARSH

ID   A4AVV7_MARSH            Unreviewed;       273 AA.
AC   A4AVV7;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAY-2019, 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=FB2170_01647 {ECO:0000313|EMBL:EAR00037.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAR00037.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAR00037.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the
RT   genus Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP002157; EAR00037.1; -; Genomic_DNA.
DR   RefSeq; WP_013305023.1; NC_014472.1.
DR   STRING; 313603.FB2170_01647; -.
DR   EnsemblBacteria; EAR00037; EAR00037; FB2170_01647.
DR   KEGG; fbc:FB2170_01647; -.
DR   eggNOG; ENOG4105EEI; Bacteria.
DR   eggNOG; COG0294; LUCA.
DR   HOGENOM; HOG000217510; -.
DR   KO; K00796; -.
DR   OMA; WAVRVHD; -.
DR   OrthoDB; 1275854at2; -.
DR   BioCyc; MSP313603:G1GNS-591-MONOMER; -.
DR   UniPathway; UPA00077; UER00156.
DR   Proteomes; UP000001602; 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; PS50972; PTERIN_BINDING; 1.
PE   3: Inferred from homology;
DR   PRODOM; A4AVV7.
DR   SWISS-2DPAGE; A4AVV7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001602};
KW   Folate biosynthesis {ECO:0000256|RuleBase:RU361205};
KW   Magnesium {ECO:0000256|RuleBase:RU361205};
KW   Metal-binding {ECO:0000256|RuleBase:RU361205};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001602};
KW   Transferase {ECO:0000256|RuleBase:RU361205}.
FT   DOMAIN       15    267       Pterin-binding. {ECO:0000259|PROSITE:
FT                                PS50972}.
SQ   SEQUENCE   273 AA;  30607 MW;  F3958413D6D20676 CRC64;
     MTLNCKGNLI DLTTPKVMGI LNITPDSFYD GGKYENDTSI LEQVEKMLSE GAIFIDVGAY
     SSRPGADHIT ENEEKDRIVP VIRSIIKRFP EAILSIDTFR STVASACLNE GASIINDISA
     GKQDDKMFEI VAQHQAPYIM MHMKGTPKNM QQNTNYKNLM TDILYYFSER LSEARAHKIN
     DIIIDPGFGF SKTLEQNYEL LRKMDLLNTL ELPILVGVSR KSMIYKTLDV TPQEAMNGTT
     ALNMIALQKG AKILRVHDVA EAIECITLNE HLN
//

If you have problems or comments...

PBIL Back to PBIL home page