FOLCP_HALVD
ID FOLCP_HALVD Reviewed; 838 AA.
AC D4GW05; Q6B7M6;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 65.
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=folCP; Synonyms=folC-P; OrderedLocusNames=HVO_1088;
GN ORFNames=C498_13314;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=DS2 / DSM 5716 / WFD11;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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; AY676165; AAT77678.1; -; Genomic_DNA.
DR EMBL; CP001956; ADE02963.1; -; Genomic_DNA.
DR EMBL; AOHU01000092; ELY27524.1; -; Genomic_DNA.
DR RefSeq; WP_004043850.1; NZ_AOHU01000092.1.
DR AlphaFoldDB; D4GW05; -.
DR SMR; D4GW05; -.
DR STRING; 309800.C498_13314; -.
DR EnsemblBacteria; ADE02963; ADE02963; HVO_1088.
DR EnsemblBacteria; ELY27524; ELY27524; C498_13314.
DR GeneID; 8924871; -.
DR KEGG; hvo:HVO_1088; -.
DR PATRIC; fig|309800.29.peg.2554; -.
DR eggNOG; arCOG02817; Archaea.
DR HOGENOM; CLU_017222_0_0_2; -.
DR OMA; EDPEMRF; -.
DR OrthoDB; 5870at2157; -.
DR UniPathway; UPA00077; UER00156.
DR UniPathway; UPA00850; -.
DR Proteomes; UP000008243; Chromosome.
DR Proteomes; UP000011532; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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: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; IEA:UniProtKB-UniPathway.
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; 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; 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..838
FT /note="Probable bifunctional folylpolyglutamate
FT synthase/dihydropteroate synthase"
FT /id="PRO_0000428787"
FT DOMAIN 569..819
FT /note="Pterin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00334"
FT REGION 1..418
FT /note="Folylpolyglutamate synthase"
FT REGION 541..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..838
FT /note="DHPS"
FT BINDING 46..52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 576
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P9WND1"
FT BINDING 616
FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:72950"
FT /evidence="ECO:0000250|UniProtKB:P0AC13"
FT BINDING 649
FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:72950"
FT /evidence="ECO:0000250|UniProtKB:P0AC13"
FT BINDING 668
FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:72950"
FT /evidence="ECO:0000250|UniProtKB:P0AC13"
FT BINDING 738
FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:72950"
FT /evidence="ECO:0000250|UniProtKB:P0AC13"
FT BINDING 774
FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:72950"
FT /evidence="ECO:0000250|UniProtKB:P0AC13"
FT BINDING 807..809
FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:72950"
FT /evidence="ECO:0000250|UniProtKB:P0AC13"
FT CONFLICT 411..418
FT /note="VGSLYVVA -> AGSLNVVT (in Ref. 1; AAT77678)"
FT /evidence="ECO:0000305"
FT CONFLICT 430..440
FT /note="PKTHRTLDDAR -> QKTPRTLEDAG (in Ref. 1; AAT77678)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 838 AA; 89156 MW; 87D57AABE274B076 CRC64;
MEYHEAVNFL FDLRRFQVKP GTESIRRLLS HLGDPHEGVS FVQVAGSNGK GSTARMVDAM
LRESGAHVGL YTSPHFDDVR ERVRVDGRKI PKSALSAFVA EAKPYLVERA ADGEPLTFFE
TVTALALWYF DRAGVDVAVL EVGMGGELDA TSAVDPVASA VTNVSLEHTA VLGDTVAEIA
KTKAAVAPAD APLVTGTTGE ALSVIREEAG DVLTVGDADA DSDADVRVSY GGRVNHQEAA
VTVETDAETL DVRIPLLGAY QARNAGIAVS LARQVRPDID AEAIHRGLRN AHWPGRFEVM
GTEPTVVLDG AHNPDACAQV ATVLDEFDYD DLHLVYGAMH DKDHGEMVGA LPEVASVVTC
KADISRGEDP EILSSVFERL NGPAVETGGA VAAALDRARA RADPDDCVLV VGSLYVVAEA
RTTWTRAVVP KTHRTLDDAR RTLDRANVAD AAERSERARR AVNRTVHTRV QRRQARVLRE
ELLSVGGDCA VSGHEFGGEL VDVVLTGTLD QFERLTAALE DPPYALAGVA AEIRETLDIE
AADAGEDDER GAGDASDAGH DDYPWNDGTA VMGILNVTPN SFHDGGEFYD IDDAVEQARA
MVDAGVDIID VGGESTRPGA DEVPVDEEIR RVAPVIEAIA DLDVLVSVDT RKAAVGAAAL
DAGADILNDV TGLEDPEMRF LAAERGAPVI VMHSIDAPVD PSREVDYDDV VEDVIDELTE
LVLLAEKAGI PRRNLIVDPG LGFGKSKAEN FELLGRTDEF AALGCPILVG HSHKSMFSLV
GEEPGDNLAA TVAGTAIAAD RGADIVRVHD VPENVAAVNV ALASRDPNRF EADAERED
