FOLCP_HALSA
ID FOLCP_HALSA Reviewed; 815 AA.
AC Q9HS44;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Probable bifunctional folylpolyglutamate synthase/dihydropteroate synthase;
DE Includes:
DE RecName: Full=Probable folylpolyglutamate synthase;
DE EC=6.3.2.17;
DE AltName: Full=Tetrahydrofolylpolyglutamate synthase;
DE Short=Tetrahydrofolate synthase;
DE Includes:
DE RecName: Full=Probable dihydropteroate synthase;
DE Short=DHPS;
DE EC=2.5.1.15;
DE AltName: Full=Dihydropteroate pyrophosphorylase;
GN Name=folP; OrderedLocusNames=VNG_0412G;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
RN [2]
RP FUNCTION.
RX PubMed=15554970; DOI=10.1111/j.1365-2958.2004.04339.x;
RA Levin I., Giladi M., Altman-Price N., Ortenberg R., Mevarech M.;
RT "An alternative pathway for reduced folate biosynthesis in bacteria and
RT halophilic archaea.";
RL Mol. Microbiol. 54:1307-1318(2004).
CC -!- FUNCTION: Can complement an H.volcanii mutant strain that is thymidine
CC auxotroph because it lacks the two dihydrofolate reductase genes
CC encoded by hdrA and hdrB. {ECO:0000269|PubMed:15554970}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + ATP + L-
CC glutamate = (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n+1) + ADP +
CC H(+) + phosphate; Xref=Rhea:RHEA:10580, Rhea:RHEA-COMP:14738,
CC Rhea:RHEA-COMP:14740, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:141005,
CC ChEBI:CHEBI:456216; EC=6.3.2.17;
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P0AC13};
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolylpolyglutamate
CC biosynthesis.
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 -!- SIMILARITY: In the N-terminal section; belongs to the
CC folylpolyglutamate synthase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the DHPS family.
CC {ECO:0000305}.
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DR EMBL; AE004437; AAG18964.1; -; Genomic_DNA.
DR PIR; H84199; H84199.
DR RefSeq; WP_010902259.1; NC_002607.1.
DR AlphaFoldDB; Q9HS44; -.
DR SMR; Q9HS44; -.
DR STRING; 64091.VNG_0412G; -.
DR PaxDb; Q9HS44; -.
DR EnsemblBacteria; AAG18964; AAG18964; VNG_0412G.
DR GeneID; 5953823; -.
DR KEGG; hal:VNG_0412G; -.
DR PATRIC; fig|64091.14.peg.308; -.
DR HOGENOM; CLU_017222_0_0_2; -.
DR InParanoid; Q9HS44; -.
DR OMA; EDPEMRF; -.
DR OrthoDB; 5870at2157; -.
DR PhylomeDB; Q9HS44; -.
DR UniPathway; UPA00077; UER00156.
DR UniPathway; UPA00850; -.
DR Proteomes; UP000000554; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004156; F:dihydropteroate synthase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IBA:GO_Central.
DR CDD; cd00739; DHPS; 1.
DR Gene3D; 3.20.20.20; -; 1.
DR Gene3D; 3.40.1190.10; -; 1.
DR Gene3D; 3.90.190.20; -; 1.
DR InterPro; IPR045031; DHP_synth.
DR InterPro; IPR006390; DHP_synth_dom.
DR InterPro; IPR011005; Dihydropteroate_synth-like.
DR InterPro; IPR001645; Folylpolyglutamate_synth.
DR InterPro; IPR018109; Folylpolyglutamate_synth_CS.
DR InterPro; IPR036565; Mur-like_cat_sf.
DR InterPro; IPR004101; Mur_ligase_C.
DR InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR InterPro; IPR013221; Mur_ligase_cen.
DR InterPro; IPR000489; Pterin-binding_dom.
DR PANTHER; PTHR20941; PTHR20941; 1.
DR Pfam; PF02875; Mur_ligase_C; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR Pfam; PF00809; Pterin_bind; 1.
DR SUPFAM; SSF51717; SSF51717; 1.
DR SUPFAM; SSF53244; SSF53244; 1.
DR SUPFAM; SSF53623; SSF53623; 1.
DR TIGRFAMs; TIGR01496; DHPS; 1.
DR TIGRFAMs; TIGR01499; folC; 1.
DR PROSITE; PS00792; DHPS_1; 1.
DR PROSITE; PS00793; DHPS_2; 1.
DR PROSITE; PS01012; FOLYLPOLYGLU_SYNT_2; 1.
DR PROSITE; PS50972; PTERIN_BINDING; 1.
PE 3: Inferred from homology;
KW ATP-binding; Folate biosynthesis; Ligase; Magnesium; Metal-binding;
KW Multifunctional enzyme; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..815
FT /note="Probable bifunctional folylpolyglutamate
FT synthase/dihydropteroate synthase"
FT /id="PRO_0000428788"
FT DOMAIN 553..803
FT /note="Pterin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00334"
FT REGION 1..416
FT /note="Folylpolyglutamate synthase"
FT REGION 555..815
FT /note="DHPS"
FT BINDING 47..53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 560
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P9WND1"
FT BINDING 600
FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:72950"
FT /evidence="ECO:0000250|UniProtKB:P0AC13"
FT BINDING 633
FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:72950"
FT /evidence="ECO:0000250|UniProtKB:P0AC13"
FT BINDING 652
FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:72950"
FT /evidence="ECO:0000250|UniProtKB:P0AC13"
FT BINDING 722
FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:72950"
FT /evidence="ECO:0000250|UniProtKB:P0AC13"
FT BINDING 758
FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:72950"
FT /evidence="ECO:0000250|UniProtKB:P0AC13"
FT BINDING 791..793
FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:72950"
FT /evidence="ECO:0000250|UniProtKB:P0AC13"
SQ SEQUENCE 815 AA; 85894 MW; D760E1022B40956F CRC64;
MRYDEAANFL LDLRRYGPKP GTESTADLLA SLGDPHQDGP DYVQIAGSNG KGSTARFTES
ILRAAGLDVG LYTSPHFDDV RERVTVNGRR MSKAALTTFI ETITPYVTER AADGAAPTYF
EVVTAMALWQ FSRADVDVAV LEVGIGGRLD ATSVVDPSAS AVTSVTLEHT DVLGETIPEI
ARDKAHVAPA GDTPLVTATT DDALAAVRDH AGAVRTVGDT AGRDVTATYE GRTNHTEAAV
SITGDDWSVA TEIPLLGDHQ AENAGVAAAL ARQTAGVDDD AIARGLRSAH WPGRFEVMGA
DPVVVLDGAH NPGACGAVAE TVAEFDYDRL LTVFGAMHDK DHGAMAAALP TPDHVWACEP
VPDRAEDADV LAAVFEDAGA GTVSVTRAVE SAVADAIAEA TADDLVLVAG SLFAVAEART
RWTRTFAETD VDSLDDARDA LERAHVTPPG VWRMRGKGVH RVVKTRVQTR QAQYLKEELL
SLGGECSVSG LNAQSGAMVD AVMMATMAQF KRLCEKLDGQ PYGLSEVGAD LRESLGIQAA
PATHGYPWEG ERTAVMGILN VTPDSFHDGG EYDALEDAVA RAESMAENGV DVIDIGGEST
RPGADAVSVA DELDRVLPVI ERISDLDVLL SVDTRKAEVA RQALEAGADI LNDVTGLDDP
EMRFVAAEYD APIVVMHSID APVDPDSDPD YDDVVDDVIA ELTERVLLAE KAGVPRERII
VDPGLGFGKS AAEGFELLDR ADEFHALGGP VLVGHSHKSM FGAVDRYPDE GGYATAAASA
LAADRGADIV RVHDVPENVA AVRVAEATRT GADAE
