ID A0P6I9_9PROT Unreviewed; 423 AA.
AC A0P6I9;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 37.
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 ORFNames=MB2181_03710 {ECO:0000313|EMBL:EAV47149.1};
OS Methylophilales bacterium HTCC2181.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales; OM43 clade.
OX NCBI_TaxID=383631 {ECO:0000313|EMBL:EAV47149.1, ECO:0000313|Proteomes:UP000054262};
RN [1] {ECO:0000313|EMBL:EAV47149.1, ECO:0000313|Proteomes:UP000054262}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2181 {ECO:0000313|EMBL:EAV47149.1,
RC ECO:0000313|Proteomes:UP000054262};
RA Giovannoni S., Vergin K., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
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};
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolylpolyglutamate
CC biosynthesis. {ECO:0000256|ARBA:ARBA00005150}.
CC -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
CC {ECO:0000256|PIRNR:PIRNR001563}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAV47149.1}.
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; AAUX01000001; EAV47149.1; -; Genomic_DNA.
DR AlphaFoldDB; A0P6I9; -.
DR OrthoDB; 9809356at2; -.
DR UniPathway; UPA00077; UER00157.
DR Proteomes; UP000054262; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 PIRSF; PIRSF001563; Folylpolyglu_synth; 1.
DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRNR:PIRNR001563};
KW Ligase {ECO:0000256|PIRNR:PIRNR001563};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR001563};
KW Reference proteome {ECO:0000313|Proteomes:UP000054262}.
FT DOMAIN 51..263
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
SQ SEQUENCE 423 AA; 46782 MW; 513ED2EC41FE9FB3 CRC64;
MLNKLSKKDS LEAWLDYIEK LHPSEIELTL ERVREVKDLA NISPDFPIIL VGGTNGKGSV
CAFIESILHA SDLKIGCYTS PHLLRFNERI RINKHEVDDK AIVNALDHIE RSRRDIPLTY
FEITTLAAVK CMNDEAVDIA ILEVGLGGRL DAVNIFSPTI SLITTVSLDH QAYLGDSVDK
IGFEKSGIFR RNIPAIINHK NPIPSMISAA NKINANLSLL GNDYNLVIHD KSLSYTSNDL
SYSDLPLPQI KGNHQIINLA GALRCIELLN STIPISIKAI KKGISDASIR GRFEVLLNNP
LVVVDVAHNP ESANNLANNF MDAKLDGITT AIFSVFEDKD VLSIIQPFIN VIDKWYIAEL
SSERALSCEG IEEALKSVMP TVTVEKFPTV RHAYKEALKN AHDNDNILMF GSFLVISESI
GET
//
