ID Q79KG6_PASMD Unreviewed; 271 AA.
AC Q79KG6;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE RecName: Full=Dihydropteroate synthase {ECO:0000256|ARBA:ARBA00012458, ECO:0000256|RuleBase:RU361205};
DE Short=DHPS {ECO:0000256|RuleBase:RU361205};
DE EC=2.5.1.15 {ECO:0000256|ARBA:ARBA00012458, ECO:0000256|RuleBase:RU361205};
DE AltName: Full=Dihydropteroate pyrophosphorylase {ECO:0000256|RuleBase:RU361205};
GN Name=sulII {ECO:0000313|EMBL:AAP15292.1};
GN Synonyms=sul2 {ECO:0000313|EMBL:AFV53153.1};
GN ORFNames=C2800_11470 {ECO:0000313|EMBL:NNI80026.1}, pov2012_p1
GN {ECO:0000313|EMBL:AFV53153.1};
OS Pasteurella multocida.
OG Plasmid pB1003 {ECO:0000313|EMBL:ABZ82584.1},
OG Plasmid pCCK1900 {ECO:0000313|EMBL:CAQ77167.1},
OG Plasmid pJR1 {ECO:0000313|EMBL:AAP15292.1}, and
OG Plasmid pOV {ECO:0000313|EMBL:AFV53153.1}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=747 {ECO:0000313|EMBL:AAP15292.1};
RN [1] {ECO:0000313|EMBL:AAP15292.1}
RP NUCLEOTIDE SEQUENCE.
RC PLASMID=pJR1 {ECO:0000313|EMBL:AAP15292.1};
RA Wu J., Shieh H.K., Shien J., Gong S., Chang P.;
RT "Molecular characterization of plasmids with antimicrobial resistant genes
RT in avian isolates of Pasteurella multocida.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAQ77167.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1900 {ECO:0000313|EMBL:CAQ77167.1};
RC PLASMID=pCCK1900 {ECO:0000313|EMBL:CAQ77167.1};
RX PubMed=18786941; DOI=10.1093/jac/dkn359;
RA Kehrenberg C., Wallmann J., Schwarz S.;
RT "Molecular analysis of florfenicol-resistant Pasteurella multocida isolates
RT in Germany.";
RL J. Antimicrob. Chemother. 62:951-955(2008).
RN [3] {ECO:0000313|EMBL:CAQ77167.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=1900 {ECO:0000313|EMBL:CAQ77167.1};
RC PLASMID=pCCK1900 {ECO:0000313|EMBL:CAQ77167.1};
RA Schwarz S.P.;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:ABZ82584.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BB1046 {ECO:0000313|EMBL:ABZ82584.1};
RC PLASMID=pB1003 {ECO:0000313|EMBL:ABZ82584.1};
RX PubMed=19528282; DOI=10.1128/AAC.01522-08;
RA San Millan A., Escudero J.A., Gutierrez B., Hidalgo L., Garcia N.,
RA Llagostera M., Dominguez L., Gonzalez-Zorn B.;
RT "Multiresistance in Pasteurella multocida is mediated by coexistence of
RT small plasmids.";
RL Antimicrob. Agents Chemother. 53:3399-3404(2009).
RN [5] {ECO:0000313|EMBL:NNI80026.1, ECO:0000313|Proteomes:UP000540079}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HNA06 {ECO:0000313|EMBL:NNI80026.1,
RC ECO:0000313|Proteomes:UP000540079};
RX PubMed=29997608;
RA Peng Z., Liang W., Wang F., Xu Z., Xie Z., Lian Z., Hua L., Zhou R.,
RA Chen H., Wu B.;
RT "Genetic and Phylogenetic Characteristics of Pasteurella multocida Isolates
RT From Different Host Species.";
RL Front. Microbiol. 9:1408-1400(2018).
RN [6] {ECO:0000313|EMBL:AFV53153.1}
RP NUCLEOTIDE SEQUENCE.
RC PLASMID=pOV {ECO:0000313|EMBL:AFV53153.1};
RX PubMed=31022414;
RA Lopez-Ochoa A.J., Sanchez-Alonso P., Vazquez-Cruz C., Horta-Valerdi G.,
RA Negrete-Abascal E., Vaca-Pacheco S., Mejia R., Perez-Marquez M.;
RT "Molecular and genetic characterization of the pOV plasmid from Pasteurella
RT multocida and construction of an integration vector for Gallibacterium
RT anatis.";
RL Plasmid 103:45-52(2019).
CC -!- FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with
CC 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-
CC dihydropteroate (H2Pte), the immediate precursor of folate derivatives.
CC {ECO:0000256|RuleBase:RU361205}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate =
CC 7,8-dihydropteroate + diphosphate; Xref=Rhea:RHEA:19949,
CC ChEBI:CHEBI:17836, ChEBI:CHEBI:17839, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:72950; EC=2.5.1.15;
CC Evidence={ECO:0000256|ARBA:ARBA00000012};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|RuleBase:RU361205};
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-
CC dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-
CC dihydropteridine diphosphate and 4-aminobenzoate: step 1/2.
CC {ECO:0000256|ARBA:ARBA00004763, ECO:0000256|RuleBase:RU361205}.
CC -!- SIMILARITY: Belongs to the DHPS family.
CC {ECO:0000256|RuleBase:RU361205}.
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DR EMBL; AY232670; AAP15292.1; -; Genomic_DNA.
DR EMBL; EU360945; ABZ82584.1; -; Genomic_DNA.
DR EMBL; JX827416; AFV53153.1; -; Genomic_DNA.
DR EMBL; FM179941; CAQ77167.1; -; Genomic_DNA.
DR EMBL; PPVL01000018; NNI80026.1; -; Genomic_DNA.
DR RefSeq; NP_848165.1; NC_004771.1.
DR RefSeq; WP_001043260.1; NZ_SHNK01000011.1.
DR RefSeq; YP_002286764.1; NC_011378.1.
DR RefSeq; YP_006966078.1; NC_019381.1.
DR AlphaFoldDB; Q79KG6; -.
DR SMR; Q79KG6; -.
DR GeneID; 84568452; -.
DR OMA; YDQGATF; -.
DR UniPathway; UPA00077; UER00156.
DR Proteomes; UP000540079; Unassembled WGS sequence.
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; Dihydropteroate synthase-like; 1.
DR InterPro; IPR045031; DHP_synth-like.
DR InterPro; IPR006390; DHP_synth_dom.
DR InterPro; IPR011005; Dihydropteroate_synth-like_sf.
DR InterPro; IPR000489; Pterin-binding_dom.
DR NCBIfam; TIGR01496; DHPS; 1.
DR PANTHER; PTHR20941; FOLATE SYNTHESIS PROTEINS; 1.
DR PANTHER; PTHR20941:SF1; FOLIC ACID SYNTHESIS PROTEIN FOL1; 1.
DR Pfam; PF00809; Pterin_bind; 1.
DR SUPFAM; SSF51717; Dihydropteroate synthetase-like; 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 Folate biosynthesis {ECO:0000256|ARBA:ARBA00022909,
KW ECO:0000256|RuleBase:RU361205};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU361205};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361205}; Plasmid {ECO:0000313|EMBL:AAP15292.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361205}.
FT DOMAIN 5..259
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 271 AA; 28470 MW; 4B00E71A3F7970FB CRC64;
MNKSLIIFGI VNITSDSFSD GGRYLAPDAA IAQARKLMAE GADVIDLGPA SSNPDAAPVS
SDTEIARIAP VLDALKADGI PVSLDSYQPA TQAYALSRGV AYLNDIRGFP DAAFYPQLAK
SSAKLVVMHS VQDGQADRRE APAGDIMDHI AAFFDARIAA LTGAGIKRNR LVLDPGMGFF
LGAAPETSLS VLARFDELRL RFDLPVLLSV SRKSFLRALT GRGPGDVGAA TLAAELAAAA
GGADFIRTHE PRPLRDGLAV LAALKETARI R
//
