ID E8QUX5_HELPW Unreviewed; 391 AA.
AC E8QUX5;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=tetrahydrofolate synthase {ECO:0000256|ARBA:ARBA00013025};
DE EC=6.3.2.17 {ECO:0000256|ARBA:ARBA00013025};
DE AltName: Full=Tetrahydrofolylpolyglutamate synthase {ECO:0000256|ARBA:ARBA00030592};
GN OrderedLocusNames=HPSA_07930 {ECO:0000313|EMBL:ADU85527.1};
OS Helicobacter pylori (strain SouthAfrica7).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=907239 {ECO:0000313|EMBL:ADU85527.1, ECO:0000313|Proteomes:UP000007467};
RN [1] {ECO:0000313|Proteomes:UP000007467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SouthAfrica7 {ECO:0000313|Proteomes:UP000007467};
RA Kersulyte D., Segal I., Mistry R., Berg D.E.;
RT "Genome sequence of Helicobacter pylori strain SouthAfrica7.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADU85527.1, ECO:0000313|Proteomes:UP000007467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SouthAfrica7 {ECO:0000313|EMBL:ADU85527.1,
RC ECO:0000313|Proteomes:UP000007467};
RX PubMed=24072860;
RA Duncan S.S., Bertoli M.T., Kersulyte D., Valk P.L., Tamma S., Segal I.,
RA McClain M.S., Cover T.L., Berg D.E.;
RT "Genome Sequences of Three hpAfrica2 Strains of Helicobacter pylori.";
RL Genome Announc. 1:e00729-13(2013).
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 Evidence={ECO:0000256|ARBA:ARBA00029332};
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DR EMBL; CP002336; ADU85527.1; -; Genomic_DNA.
DR RefSeq; WP_000798435.1; NC_017361.1.
DR AlphaFoldDB; E8QUX5; -.
DR KEGG; hes:HPSA_07930; -.
DR PATRIC; fig|907239.3.peg.1614; -.
DR eggNOG; COG0285; Bacteria.
DR HOGENOM; CLU_015869_1_1_7; -.
DR OrthoDB; 9809356at2; -.
DR UniPathway; UPA00077; UER00157.
DR Proteomes; UP000007467; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0008841; F:dihydrofolate 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:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR InterPro; IPR001645; Folylpolyglutamate_synth.
DR InterPro; IPR036565; Mur-like_cat_sf.
DR InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR InterPro; IPR013221; Mur_ligase_cen.
DR NCBIfam; TIGR01499; folC; 1.
DR PANTHER; PTHR11136:SF0; DIHYDROFOLATE SYNTHETASE-RELATED; 1.
DR PANTHER; PTHR11136; FOLYLPOLYGLUTAMATE SYNTHASE-RELATED; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
PE 4: Predicted;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 50..211
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
SQ SEQUENCE 391 AA; 44707 MW; 2BC7D63E0A070BD5 CRC64;
MKNSPLKGLK AFLETKPKEY HKFDPSRFIQ IYKDFKNAFF EIQAKVIHIV GTNGKGSTGR
FLTLLLADQN FKVLHFTSPH VFEFRERFFL NGSIISENAL ENAHQQLQLH AFSNACSYFE
YATLLAVMLA KDCDYLILEA GLGGEFDSTN ALEKTLSVFT PIDYDHKEFL GDSLESIATT
KLRAMGPLNI IAPQQELVLN VAQKIAKEKQ AQLIVVQNEI SQEVKAYIER HHLAHFLAMN
LEVALKAFET LLPCDRQKVL QRLKPLDLIG RCELLSPNIL IDVGHNPHSA KALKEEIKRV
FNAKIILIYN CYQDKDAFGV LEILKPVVKK VLILELHNER IIQLETLQGI LETLGLEHAL
FEEVKENENY LVYGSFLVAN AFYERYQKKR D
//
