ID A0A140D693_9GAMM Unreviewed; 297 AA. AC A0A140D693; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 08-JUN-2016, entry version 2. DE RecName: Full=Bifunctional protein FolD {ECO:0000256|HAMAP-Rule:MF_01576}; GN Name=mthD {ECO:0000313|EMBL:AMK07367.1}; GN Synonyms=folD {ECO:0000256|HAMAP-Rule:MF_01576}; OS gamma proteobacterium 10BT. OC Bacteria; Proteobacteria; Gammaproteobacteria. OX NCBI_TaxID=1778877 {ECO:0000313|EMBL:AMK07367.1}; RN [1] {ECO:0000313|EMBL:AMK07367.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=10BTContig1 {ECO:0000313|EMBL:AMK07367.1}; RX PubMed=26822785; DOI=10.1186/s12864-016-2404-0; RA Maruthamuthu M., Jimenez D.J., Stevens P., van Elsas J.D.; RT "A multi-substrate approach for functional metagenomics-based RT screening for (hemi)cellulases in two wheat straw-degrading microbial RT consortia unveils novel thermoalkaliphilic enzymes."; RL BMC Genomics 17:86-86(2016). CC -!- FUNCTION: Catalyzes the oxidation of 5,10- CC methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and CC then the hydrolysis of 5,10-methenyltetrahydrofolate to 10- CC formyltetrahydrofolate. {ECO:0000256|HAMAP-Rule:MF_01576, CC ECO:0000256|SAAS:SAAS00315597}. CC -!- CATALYTIC ACTIVITY: 5,10-methenyltetrahydrofolate + H(2)O = 10- CC formyltetrahydrofolate. {ECO:0000256|HAMAP-Rule:MF_01576, CC ECO:0000256|SAAS:SAAS00315596}. CC -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + NADP(+) = CC 5,10-methenyltetrahydrofolate + NADPH. {ECO:0000256|HAMAP- CC Rule:MF_01576, ECO:0000256|SAAS:SAAS00315567}. CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC {ECO:0000256|HAMAP-Rule:MF_01576, ECO:0000256|SAAS:SAAS00315571}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01576, CC ECO:0000256|SAAS:SAAS00315581}. CC -!- SIMILARITY: Belongs to the tetrahydrofolate CC dehydrogenase/cyclohydrolase family. {ECO:0000256|HAMAP- CC Rule:MF_01576, ECO:0000256|SAAS:SAAS00542791}. 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; KU505133; AMK07367.1; -; Genomic_DNA. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_01576; THF_DHG_CYH; 1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR000672; THF_DH/CycHdrlase. DR InterPro; IPR020630; THF_DH/CycHdrlase_cat_dom. DR InterPro; IPR020867; THF_DH/CycHdrlase_CS. DR InterPro; IPR020631; THF_DH/CycHdrlase_NAD-bd_dom. DR Pfam; PF00763; THF_DHG_CYH; 1. DR Pfam; PF02882; THF_DHG_CYH_C; 1. DR PRINTS; PR00085; THFDHDRGNASE. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS00767; THF_DHG_CYH_2; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01576, KW ECO:0000256|SAAS:SAAS00426175}; KW Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01576, KW ECO:0000256|SAAS:SAAS00426222}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01576, KW ECO:0000256|SAAS:SAAS00426197}; KW Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01576, KW ECO:0000256|SAAS:SAAS00426216}; KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01576, KW ECO:0000256|SAAS:SAAS00426169}; KW NADP {ECO:0000256|HAMAP-Rule:MF_01576, ECO:0000256|SAAS:SAAS00426165}; KW One-carbon metabolism {ECO:0000256|HAMAP-Rule:MF_01576, KW ECO:0000256|SAAS:SAAS00426229}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01576, KW ECO:0000256|SAAS:SAAS00426231, ECO:0000313|EMBL:AMK07367.1}; KW Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01576, KW ECO:0000256|SAAS:SAAS00426184}. FT NP_BIND 169 171 NADP. {ECO:0000256|HAMAP-Rule:MF_01576}. FT BINDING 194 194 NADP. {ECO:0000256|HAMAP-Rule:MF_01576}. FT BINDING 235 235 NADP; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01576}. SQ SEQUENCE 297 AA; 31485 MW; B41D2755AF1337B4 CRC64; MSAVPGVKLI DGKATAARVL AEVREQVLEL RQGGVQPGLA VVLVGADAAS HVYVRNKVLR AEEVGIRSLE HRLHADTTQA HLLALIDRLN RDPEVNGILV QLPLPGHIDE HRVLQAISPF KDVDGFHSEN VGGLAQGRDV LTPCTPSACM RLLRDACGEL RGKHAVVVGR SNIVGKPMAA LLLQADCTVT VVHSHSRDLP ALCRQADILV AAVGQPRLIG ADWLKPGAVV IDVGINRVDD GGHSRLVGDV DFAAALPQVA GITPVPGGVG PMTIAYLMKN TLLALDLQQQ AAHQERT //