ID C3ZVK0_BRAFL Unreviewed; 909 AA.
AC C3ZVK0;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 92.
DE RecName: Full=10-formyltetrahydrofolate dehydrogenase {ECO:0000256|PIRNR:PIRNR036489};
DE EC=1.5.1.6 {ECO:0000256|PIRNR:PIRNR036489};
GN ORFNames=BRAFLDRAFT_129324 {ECO:0000313|EMBL:EEN43434.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN43434.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN43434.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN43434.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-10-formyltetrahydrofolate + H2O + NADP(+) = (6S)-5,6,7,8-
CC tetrahydrofolate + CO2 + H(+) + NADPH; Xref=Rhea:RHEA:10180,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:195366; EC=1.5.1.6;
CC Evidence={ECO:0000256|PIRNR:PIRNR036489};
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|RuleBase:RU003345}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the aldehyde
CC dehydrogenase family. ALDH1L subfamily.
CC {ECO:0000256|PIRNR:PIRNR036489}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the GART family.
CC {ECO:0000256|PIRNR:PIRNR036489}.
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DR EMBL; GG666690; EEN43434.1; -; Genomic_DNA.
DR RefSeq; XP_002587423.1; XM_002587377.1.
DR AlphaFoldDB; C3ZVK0; -.
DR STRING; 7739.C3ZVK0; -.
DR eggNOG; KOG2452; Eukaryota.
DR InParanoid; C3ZVK0; -.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IBA:GO_Central.
DR GO; GO:0016155; F:formyltetrahydrofolate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0009258; P:10-formyltetrahydrofolate catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR CDD; cd08703; FDH_Hydrolase_C; 1.
DR CDD; cd08647; FMT_core_FDH_N; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.10.25.10; Formyl transferase, C-terminal domain; 1.
DR Gene3D; 3.40.50.170; Formyl transferase, N-terminal domain; 1.
DR InterPro; IPR011407; 10_FTHF_DH.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR005793; Formyl_trans_C.
DR InterPro; IPR037022; Formyl_trans_C_sf.
DR InterPro; IPR002376; Formyl_transf_N.
DR InterPro; IPR036477; Formyl_transf_N_sf.
DR InterPro; IPR011034; Formyl_transferase-like_C_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR PANTHER; PTHR11699:SF190; 10-FORMYLTETRAHYDROFOLATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF00171; Aldedh; 2.
DR Pfam; PF02911; Formyl_trans_C; 1.
DR Pfam; PF00551; Formyl_trans_N; 1.
DR Pfam; PF00550; PP-binding; 1.
DR PIRSF; PIRSF036489; 10-FTHFDH; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR SUPFAM; SSF50486; FMT C-terminal domain-like; 1.
DR SUPFAM; SSF53328; Formyltransferase; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|PIRNR:PIRNR036489, ECO:0000256|PIRSR:PIRSR036489-3};
KW One-carbon metabolism {ECO:0000256|PIRNR:PIRNR036489};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR036489,
KW ECO:0000256|RuleBase:RU003345}.
FT DOMAIN 306..382
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT ACT_SITE 106
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-1"
FT ACT_SITE 678
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 678
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-1"
FT ACT_SITE 712
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-1"
FT BINDING 88..90
FT /ligand="(6R)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:195366"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-2"
FT BINDING 142
FT /ligand="(6R)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:195366"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-2"
FT BINDING 602..605
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-3"
FT BINDING 635..640
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-3"
FT BINDING 655..656
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-3"
FT BINDING 809..811
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-3"
FT SITE 142
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-4"
SQ SEQUENCE 909 AA; 99980 MW; 7CDC508BB58CE915 CRC64;
MKIAVIGQSQ FGTEVYNLLK KEGHEIVGVF TIPDLQGKPD PLAVAGEKDG VPTFKFPRWR
VKGQSIPEVV QQYQACGADL NVLPFCSQFI PMDVINTPKH GSIIYHPSIL PRHRGASAIN
WTLIHGDKKA GFTIFWADDG LDTGPILLQR ECYAGPNETL DGLYNKFLYP EGIKAMAEAV
QLIADGKAPR IPQSEDGATY EPMLKKKESV QINWDQTGEA LHNFIRGNDK LPGAWTTING
EGQRNYTPPS LQVTLYGSKM FKKEVPEGAE VEVPGASKPA IVHKGGMIFT GNDGKMLSQS
RSSCVVSISE QHKFVKDVWK GILSIAEIQG ETDFFKAGAG SMDVVRLVEE VLQRCSDVSL
QNEDVYMNTT FHDFMQMVVR KARGLDEPDE FEYDAIEMHV NNLKLEFPNQ LFINNEFVDA
SNGATFDTIN PTDESVICKV SKGTKDDVNT AVKAAKEAFE DGPWGKMNPR DRGKLMYRLA
DLMDEHKEEL ATLEAIDSGA VYTLALKTHV GMSIDTFRYY AGWCDKIMGT TIPINQARPN
HNLTYTKREP VGNRCWPDRA VELSADDVSV EDGRRAHAGD TIVLKPAQKA AALTPGNTIV
LKPAQVTPLT ALKFAELAVK AGFPPGVINI LPGAGSQVGQ AILDHPDVRK VGFTGSTPVG
KDIMRSCAVS NLKRVSLELG GKSPLVIFND CDLDRAVRQS LSGCFFNKGE NCIASGRLFV
EESIHDEFVT RVVEEIKKMK IGDPLDRSVD HGPQNHLAHF NSLLQYCKVG VEQGAKLVYG
GTRVDRPGLF LHPTVFTDVT DDMWIAEEES FGPVMIISKF KDGDIDGMLK SANNTEFGLA
SGVFTKDINK ALYVADHLQA GTVFVNTYNK TDVAAPFGGF KQSGFGKDLG QEALHEYTRT
KAVTVEYWL
//
