GenomeNet

Database: UniProt
Entry: A0A1G8A9J0_9NOCA
LinkDB: A0A1G8A9J0_9NOCA
Original site: A0A1G8A9J0_9NOCA 
ID   A0A1G8A9J0_9NOCA        Unreviewed;       227 AA.
AC   A0A1G8A9J0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=5-formyltetrahydrofolate cyclo-ligase {ECO:0000256|RuleBase:RU361279};
DE            EC=6.3.3.2 {ECO:0000256|RuleBase:RU361279};
GN   ORFNames=SAMN05444695_101360 {ECO:0000313|EMBL:SDH17559.1};
OS   Rhodococcus triatomae.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=300028 {ECO:0000313|EMBL:SDH17559.1, ECO:0000313|Proteomes:UP000183263};
RN   [1] {ECO:0000313|EMBL:SDH17559.1, ECO:0000313|Proteomes:UP000183263}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44892 {ECO:0000313|EMBL:SDH17559.1,
RC   ECO:0000313|Proteomes:UP000183263};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5-formyl-5,6,7,8-tetrahydrofolate + ATP = (6R)-5,10-
CC         methenyltetrahydrofolate + ADP + phosphate; Xref=Rhea:RHEA:10488,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57455,
CC         ChEBI:CHEBI:57457, ChEBI:CHEBI:456216; EC=6.3.3.2;
CC         Evidence={ECO:0000256|RuleBase:RU361279};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU361279};
CC   -!- SIMILARITY: Belongs to the 5-formyltetrahydrofolate cyclo-ligase
CC       family. {ECO:0000256|ARBA:ARBA00010638, ECO:0000256|RuleBase:RU361279}.
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; FNDN01000001; SDH17559.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8A9J0; -.
DR   OrthoDB; 3242798at2; -.
DR   Proteomes; UP000183263; Unassembled WGS sequence.
DR   GO; GO:0030272; F:5-formyltetrahydrofolate cyclo-ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.10420; NagB/RpiA/CoA transferase-like; 1.
DR   InterPro; IPR002698; FTHF_cligase.
DR   InterPro; IPR024185; FTHF_cligase-like_sf.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   NCBIfam; TIGR02727; MTHFS_bact; 1.
DR   PANTHER; PTHR23407:SF1; 5-FORMYLTETRAHYDROFOLATE CYCLO-LIGASE; 1.
DR   PANTHER; PTHR23407; ATPASE INHIBITOR/5-FORMYLTETRAHYDROFOLATE CYCLO-LIGASE; 1.
DR   Pfam; PF01812; 5-FTHF_cyc-lig; 1.
DR   SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361279};
KW   Ligase {ECO:0000313|EMBL:SDH17559.1};
KW   Magnesium {ECO:0000256|RuleBase:RU361279};
KW   Metal-binding {ECO:0000256|RuleBase:RU361279};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU361279};
KW   Reference proteome {ECO:0000313|Proteomes:UP000183263}.
FT   REGION          208..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   227 AA;  23931 MW;  2CCC08D94FD2C7CF CRC64;
     MERPPDVSAK ADVSAKADVS AKADVSAKAR WRERALSSRR ALDARRRDAE NRALVDFVTG
     RWPGGGTVCA YVPLPSEPGS PALLAALRAG GSRVLVPVTG DPGPLSWAEY TGPDSLVAGQ
     YGIPRPTGPV LAPDEIRSAE VVLVPALGVD RRGVRLGRGA GFYDRTLPIA SAGTRLIAVV
     RDEELVEALP EEAHDVRMHE ALTPARGFVT LGGAGTGTRR GDAREQE
//
DBGET integrated database retrieval system