ID K2HAD4_9RHOB Unreviewed; 411 AA.
AC K2HAD4;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Dihydrofolate synthase/folylpolyglutamate synthase {ECO:0000256|ARBA:ARBA00019357};
DE EC=6.3.2.12 {ECO:0000256|ARBA:ARBA00013023};
DE EC=6.3.2.17 {ECO:0000256|ARBA:ARBA00013025};
DE AltName: Full=Folylpoly-gamma-glutamate synthetase-dihydrofolate synthetase {ECO:0000256|ARBA:ARBA00032510};
DE AltName: Full=Folylpolyglutamate synthetase {ECO:0000256|ARBA:ARBA00030048};
DE AltName: Full=Tetrahydrofolylpolyglutamate synthase {ECO:0000256|ARBA:ARBA00030592};
GN ORFNames=OCGS_1326 {ECO:0000313|EMBL:EKE44488.1};
OS Oceaniovalibus guishaninsula JLT2003.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Oceaniovalibus.
OX NCBI_TaxID=1231392 {ECO:0000313|EMBL:EKE44488.1, ECO:0000313|Proteomes:UP000006765};
RN [1] {ECO:0000313|EMBL:EKE44488.1, ECO:0000313|Proteomes:UP000006765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JLT2003 {ECO:0000313|EMBL:EKE44488.1,
RC ECO:0000313|Proteomes:UP000006765};
RX PubMed=23144420; DOI=10.1128/JB.01874-12;
RA Tang K., Liu K., Jiao N.;
RT "Draft Genome Sequence of Oceaniovalibus guishaninsula JLT2003T.";
RL J. Bacteriol. 194:6683-6683(2012).
CC -!- FUNCTION: Functions in two distinct reactions of the de novo folate
CC biosynthetic pathway. Catalyzes the addition of a glutamate residue to
CC dihydropteroate (7,8-dihydropteroate or H2Pte) to form dihydrofolate
CC (7,8-dihydrofolate monoglutamate or H2Pte-Glu). Also catalyzes
CC successive additions of L-glutamate to tetrahydrofolate or 10-
CC formyltetrahydrofolate or 5,10-methylenetetrahydrofolate, leading to
CC folylpolyglutamate derivatives. {ECO:0000256|ARBA:ARBA00002714}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-5,10-methylenetetrahydrofolyl-(gamma-L-Glu)(n) + ATP + L-
CC glutamate = (6R)-5,10-methylenetetrahydrofolyl-(gamma-L-Glu)(n+1) +
CC ADP + H(+) + phosphate; Xref=Rhea:RHEA:51912, Rhea:RHEA-COMP:13257,
CC Rhea:RHEA-COMP:13258, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:136572,
CC ChEBI:CHEBI:456216; EC=6.3.2.17;
CC Evidence={ECO:0000256|ARBA:ARBA00000809};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=10-formyltetrahydrofolyl-(gamma-L-Glu)(n) + ATP + L-glutamate
CC = 10-formyltetrahydrofolyl-(gamma-L-Glu)(n+1) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:51904, Rhea:RHEA-COMP:13088, Rhea:RHEA-
CC COMP:14300, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:134413, ChEBI:CHEBI:456216;
CC EC=6.3.2.17; Evidence={ECO:0000256|ARBA:ARBA00000058};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7,8-dihydropteroate + ATP + L-glutamate = 7,8-dihydrofolate +
CC ADP + H(+) + phosphate; Xref=Rhea:RHEA:23584, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17839, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57451, ChEBI:CHEBI:456216;
CC EC=6.3.2.12; Evidence={ECO:0000256|ARBA:ARBA00000104};
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 2/2.
CC {ECO:0000256|ARBA:ARBA00004799}.
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:EKE44488.1}.
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DR EMBL; AMGO01000021; EKE44488.1; -; Genomic_DNA.
DR RefSeq; WP_007426478.1; NZ_AMGO01000021.1.
DR AlphaFoldDB; K2HAD4; -.
DR STRING; 1231392.OCGS_1326; -.
DR PATRIC; fig|1231392.3.peg.1330; -.
DR eggNOG; COG0285; Bacteria.
DR OrthoDB; 9809356at2; -.
DR UniPathway; UPA00077; UER00157.
DR Proteomes; UP000006765; 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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
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; IPR018109; Folylpolyglutamate_synth_CS.
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.
DR PROSITE; PS01012; FOLYLPOLYGLU_SYNT_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRNR:PIRNR001563};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Folate biosynthesis {ECO:0000256|ARBA:ARBA00022909};
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 Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Reference proteome {ECO:0000313|Proteomes:UP000006765}.
FT DOMAIN 35..251
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
SQ SEQUENCE 411 AA; 43132 MW; 8BEB9B1BBE6C2E1B CRC64;
MTLHPKVIDL TLDRMWRLLD ALGNPQDALP PVIHVAGTNG KGSTLAMIRA GIEGAGQTAH
VYTSPHLARF NERIRVAGDL IGDDALSALL DECEAANGGR PITFFEITTC AALLAFARTP
ADYCLLEVGL GGRLDATNVV ARPRLTAITP VSPDHQQYLG DTLPLIAGEK AGILKPGVPC
IVGRQQDAAL DVIEAAAARL AAPLLVRGQH WHTDIQHGRL VFQDETGLLD LPLPNLPGPH
QIDNAGAALA ALRCLRIAPA AFEAAVTRAE WPARMQRLRR GPLPDAAPRA ELWLDGGHNP
AAGDALAATL AGMPRRPTRL VCGMLNTKDV AGYLRPLAAH ADSLTAISIP DEANTLPAEA
TADAARGAGL RADIADSALD AVRAIAAADP EARILICGSL YLAGNVLRDN G
//
