AL1L1_RAT
ID AL1L1_RAT Reviewed; 902 AA.
AC P28037; Q5HZB2;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 3.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Cytosolic 10-formyltetrahydrofolate dehydrogenase {ECO:0000305|PubMed:1848231};
DE Short=10-FTHFDH {ECO:0000303|PubMed:7822273};
DE Short=FDH {ECO:0000303|PubMed:10585460};
DE EC=1.5.1.6 {ECO:0000269|PubMed:10585460, ECO:0000269|PubMed:17302434, ECO:0000269|PubMed:17884809, ECO:0000269|PubMed:1848231, ECO:0000269|PubMed:7822273};
DE AltName: Full=Aldehyde dehydrogenase family 1 member L1 {ECO:0000312|RGD:621294};
DE AltName: Full=FBP-CI;
GN Name=Aldh1l1 {ECO:0000312|RGD:621294}; Synonyms=Fthfd;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC
RP ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=1848231; DOI=10.1016/s0021-9258(19)67743-4;
RA Cook R.J., Lloyd R.S., Wagner C.;
RT "Isolation and characterization of cDNA clones for rat liver 10-
RT formyltetrahydrofolate dehydrogenase.";
RL J. Biol. Chem. 266:4965-4973(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, CATALYTIC ACTIVITY, DOMAIN,
RP REGION, ACTIVE SITE, SITE, AND MUTAGENESIS OF ASP-142.
RX PubMed=10585460; DOI=10.1074/jbc.274.50.35777;
RA Krupenko S.A., Wagner C.;
RT "Aspartate 142 is involved in both hydrolase and dehydrogenase catalytic
RT centers of 10-formyltetrahydrofolate dehydrogenase.";
RL J. Biol. Chem. 274:35777-35784(1999).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=3392008; DOI=10.1016/s0021-9258(19)81498-9;
RA Case G.L., Kaisaki P.J., Steele R.D.;
RT "Resolution of rat liver 10-formyltetrahydrofolate dehydrogenase/hydrolase
RT activities.";
RL J. Biol. Chem. 263:10204-10207(1988).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, DOMAIN, AND MUTAGENESIS OF CYS-707.
RX PubMed=7822273; DOI=10.1074/jbc.270.2.519;
RA Krupenko S.A., Wagner C., Cook R.J.;
RT "Cysteine 707 is involved in the dehydrogenase activity site of rat 10-
RT formyltetrahydrofolate dehydrogenase.";
RL J. Biol. Chem. 270:519-522(1995).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16396499; DOI=10.1021/pr0503073;
RA Moser K., White F.M.;
RT "Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-
RT MS/MS.";
RL J. Proteome Res. 5:98-104(2006).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, PHOSPHOPANTETHEINYLATION AT SER-354, DOMAIN,
RP AND MUTAGENESIS OF SER-354.
RX PubMed=17884809; DOI=10.1074/jbc.m707627200;
RA Donato H., Krupenko N.I., Tsybovsky Y., Krupenko S.A.;
RT "10-formyltetrahydrofolate dehydrogenase requires a 4'-phosphopantetheine
RT prosthetic group for catalysis.";
RL J. Biol. Chem. 282:34159-34166(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [9] {ECO:0007744|PDB:1S3I}
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-309, AND ACTIVE SITE.
RX PubMed=14729668; DOI=10.1074/jbc.m313934200;
RA Chumanevich A.A., Krupenko S.A., Davies C.;
RT "The crystal structure of the hydrolase domain of 10-formyltetrahydrofolate
RT dehydrogenase: mechanism of hydrolysis and its interplay with the
RT dehydrogenase domain.";
RL J. Biol. Chem. 279:14355-14364(2004).
RN [10] {ECO:0007744|PDB:2O2P, ECO:0007744|PDB:2O2Q, ECO:0007744|PDB:2O2R}
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 397-902 IN COMPLEX WITH NADP,
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, DOMAIN, MUTAGENESIS OF GLU-673,
RP ACTIVE SITE, AND REACTION MECHANISM.
RX PubMed=17302434; DOI=10.1021/bi0619573;
RA Tsybovsky Y., Donato H., Krupenko N.I., Davies C., Krupenko S.A.;
RT "Crystal structures of the carboxyl terminal domain of rat 10-
RT formyltetrahydrofolate dehydrogenase: implications for the catalytic
RT mechanism of aldehyde dehydrogenases.";
RL Biochemistry 46:2917-2929(2007).
RN [11] {ECO:0007744|PDB:3RHJ, ECO:0007744|PDB:3RHL, ECO:0007744|PDB:3RHM, ECO:0007744|PDB:3RHO, ECO:0007744|PDB:3RHP, ECO:0007744|PDB:3RHQ, ECO:0007744|PDB:3RHR}
RP X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 397-902 IN COMPLEX WITH NADP,
RP ACTIVE SITE, AND SUBUNIT.
RX PubMed=21540484; DOI=10.1074/jbc.m111.221069;
RA Tsybovsky Y., Krupenko S.A.;
RT "Conserved catalytic residues of the ALDH1L1 aldehyde dehydrogenase domain
RT control binding and discharging of the coenzyme.";
RL J. Biol. Chem. 286:23357-23367(2011).
CC -!- FUNCTION: Cytosolic 10-formyltetrahydrofolate dehydrogenase that
CC catalyzes the NADP(+)-dependent conversion of 10-formyltetrahydrofolate
CC to tetrahydrofolate and carbon dioxide (PubMed:1848231,
CC PubMed:10585460, PubMed:7822273, PubMed:17884809, PubMed:17302434). May
CC also have an NADP(+)-dependent aldehyde dehydrogenase activity towards
CC formaldehyde, acetaldehyde, propionaldehyde, and benzaldehyde
CC (PubMed:1848231). {ECO:0000269|PubMed:10585460,
CC ECO:0000269|PubMed:17302434, ECO:0000269|PubMed:17884809,
CC ECO:0000269|PubMed:1848231, ECO:0000269|PubMed:7822273}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-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:57454, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.5.1.6; Evidence={ECO:0000269|PubMed:10585460,
CC ECO:0000269|PubMed:17302434, ECO:0000269|PubMed:17884809,
CC ECO:0000269|PubMed:1848231, ECO:0000269|PubMed:7822273};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10181;
CC Evidence={ECO:0000305|PubMed:1848231};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:17302434,
CC ECO:0000269|PubMed:21540484, ECO:0000269|PubMed:7822273}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:1848231,
CC ECO:0000269|PubMed:3392008}.
CC -!- TISSUE SPECIFICITY: Expressed in liver. {ECO:0000269|PubMed:1848231}.
CC -!- DOMAIN: The N-terminal hydrolase domain has an NADP-independent
CC formyltetrahydrofolate hydrolase activity, releasing formate and
CC tetrahydrofolate. {ECO:0000269|PubMed:10585460}.
CC -!- DOMAIN: The C-terminal aldehyde dehydrogenase domain has an NADP-
CC dependent dehydrogenase activity (PubMed:10585460, PubMed:7822273,
CC PubMed:17302434). It catalyzes the oxidation of formate, released by
CC the hydrolysis of formyltetrahydrofolate, into CO2 (Probable).
CC {ECO:0000269|PubMed:10585460, ECO:0000269|PubMed:17302434,
CC ECO:0000269|PubMed:7822273, ECO:0000305|PubMed:17884809}.
CC -!- DOMAIN: The carrier domain is phosphopantetheinylated and uses the 4'-
CC phosphopantetheine/4'-PP swinging arm to transfer the formyl group
CC released by the N-terminal formyltetrahydrofolate hydrolase activity to
CC the C-terminal aldehyde dehydrogenase domain that catalyzes its NADP-
CC dependent oxidation into CO2 (PubMed:17884809). The overall NADP-
CC dependent physiological reaction requires the 3 domains (N-terminal
CC hydrolase, C-terminal aldehyde dehydrogenase and carrier domains) to
CC convert formyltetrahydrofolate into tetrahydrofolate and CO2
CC (PubMed:10585460, PubMed:7822273, PubMed:17884809, PubMed:17302434).
CC {ECO:0000269|PubMed:10585460, ECO:0000269|PubMed:17302434,
CC ECO:0000269|PubMed:17884809, ECO:0000269|PubMed:7822273}.
CC -!- PTM: Phosphopantetheinylation at Ser-354 by AASDHPPT is required for
CC the formyltetrahydrofolate dehydrogenase activity.
CC {ECO:0000269|PubMed:17884809}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the GART family.
CC {ECO:0000305|PubMed:10585460}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the aldehyde
CC dehydrogenase family. ALDH1L subfamily. {ECO:0000305|PubMed:10585460}.
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DR EMBL; M59861; AAA70429.1; -; mRNA.
DR EMBL; BC089101; AAH89101.1; -; mRNA.
DR PIR; A23709; A60560.
DR RefSeq; NP_071992.1; NM_022547.1.
DR PDB; 1S3I; X-ray; 2.30 A; A=1-310.
DR PDB; 2O2P; X-ray; 1.70 A; A/B/C/D=397-902.
DR PDB; 2O2Q; X-ray; 2.00 A; A/B/C/D=397-902.
DR PDB; 2O2R; X-ray; 2.20 A; A/B/C/D=397-902.
DR PDB; 3RHJ; X-ray; 1.89 A; A/B/C/D=397-902.
DR PDB; 3RHL; X-ray; 2.00 A; A/B/C/D=397-902.
DR PDB; 3RHM; X-ray; 2.38 A; A/B/C/D=397-902.
DR PDB; 3RHO; X-ray; 2.26 A; A/B/C/D=397-902.
DR PDB; 3RHP; X-ray; 2.50 A; A/B/C/D=397-902.
DR PDB; 3RHQ; X-ray; 2.10 A; A/B/C/D=397-902.
DR PDB; 3RHR; X-ray; 2.30 A; A/B/C/D=397-902.
DR PDB; 4GNZ; X-ray; 2.30 A; A/B/C/D=397-902.
DR PDB; 4GO0; X-ray; 3.38 A; A/B/C/D=397-902.
DR PDB; 4GO2; X-ray; 2.28 A; A/B/C/D=397-902.
DR PDB; 7RLT; EM; 3.70 A; A/B/C/D=1-902.
DR PDB; 7RLU; EM; 2.90 A; A/B/C/D=1-902.
DR PDBsum; 1S3I; -.
DR PDBsum; 2O2P; -.
DR PDBsum; 2O2Q; -.
DR PDBsum; 2O2R; -.
DR PDBsum; 3RHJ; -.
DR PDBsum; 3RHL; -.
DR PDBsum; 3RHM; -.
DR PDBsum; 3RHO; -.
DR PDBsum; 3RHP; -.
DR PDBsum; 3RHQ; -.
DR PDBsum; 3RHR; -.
DR PDBsum; 4GNZ; -.
DR PDBsum; 4GO0; -.
DR PDBsum; 4GO2; -.
DR PDBsum; 7RLT; -.
DR PDBsum; 7RLU; -.
DR AlphaFoldDB; P28037; -.
DR SMR; P28037; -.
DR STRING; 10116.ENSRNOP00000065882; -.
DR ChEMBL; CHEMBL3414419; -.
DR iPTMnet; P28037; -.
DR PhosphoSitePlus; P28037; -.
DR PeptideAtlas; P28037; -.
DR PRIDE; P28037; -.
DR ABCD; P28037; 3 sequenced antibodies.
DR Ensembl; ENSRNOT00000096748; ENSRNOP00000089314; ENSRNOG00000047023.
DR GeneID; 64392; -.
DR KEGG; rno:64392; -.
DR CTD; 10840; -.
DR RGD; 621294; Aldh1l1.
DR eggNOG; KOG2452; Eukaryota.
DR GeneTree; ENSGT00940000160913; -.
DR InParanoid; P28037; -.
DR OrthoDB; 153834at2759; -.
DR BRENDA; 1.5.1.6; 5301.
DR Reactome; R-RNO-196757; Metabolism of folate and pterines.
DR SABIO-RK; P28037; -.
DR EvolutionaryTrace; P28037; -.
DR PRO; PR:P28037; -.
DR Proteomes; UP000002494; Chromosome 4.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IBA:GO_Central.
DR GO; GO:0033721; F:aldehyde dehydrogenase (NADP+) activity; IDA:UniProtKB.
DR GO; GO:0004030; F:aldehyde dehydrogenase [NAD(P)+] activity; IDA:RGD.
DR GO; GO:0016155; F:formyltetrahydrofolate dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0016742; F:hydroxymethyl-, formyl- and related transferase activity; IEA:InterPro.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0009258; P:10-formyltetrahydrofolate catabolic process; IDA:UniProtKB.
DR GO; GO:0038183; P:bile acid signaling pathway; IEP:RGD.
DR GO; GO:0046655; P:folic acid metabolic process; IDA:UniProtKB.
DR GO; GO:0006740; P:NADPH regeneration; IDA:UniProtKB.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; TAS:RGD.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.10.25.10; -; 1.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 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; IPR001555; GART_AS.
DR InterPro; IPR009081; PP-bd_ACP.
DR Pfam; PF00171; Aldedh; 1.
DR Pfam; PF02911; Formyl_trans_C; 1.
DR Pfam; PF00551; Formyl_trans_N; 1.
DR PIRSF; PIRSF036489; 10-FTHFDH; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF50486; SSF50486; 1.
DR SUPFAM; SSF53328; SSF53328; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00373; GART; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; NADP;
KW One-carbon metabolism; Oxidoreductase; Phosphopantetheine; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..902
FT /note="Cytosolic 10-formyltetrahydrofolate dehydrogenase"
FT /id="PRO_0000199422"
FT DOMAIN 318..395
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 1..310
FT /note="Hydrolase domain"
FT /evidence="ECO:0000305|PubMed:10585460"
FT REGION 417..902
FT /note="Aldehyde dehydrogenase domain"
FT /evidence="ECO:0000305|PubMed:10585460"
FT ACT_SITE 106
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:10585460,
FT ECO:0000305|PubMed:14729668"
FT ACT_SITE 673
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:17302434"
FT ACT_SITE 707
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:17302434,
FT ECO:0000305|PubMed:21540484, ECO:0007744|PDB:2O2Q,
FT ECO:0007744|PDB:3RHO"
FT BINDING 88..90
FT /ligand="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
FT /evidence="ECO:0000250|UniProtKB:O75891"
FT BINDING 142
FT /ligand="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
FT /evidence="ECO:0000250|UniProtKB:O75891"
FT BINDING 571..573
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:17302434,
FT ECO:0000269|PubMed:21540484, ECO:0007744|PDB:2O2Q,
FT ECO:0007744|PDB:2O2R, ECO:0007744|PDB:3RHJ,
FT ECO:0007744|PDB:3RHL, ECO:0007744|PDB:3RHO,
FT ECO:0007744|PDB:3RHQ, ECO:0007744|PDB:3RHR"
FT BINDING 597..600
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:17302434,
FT ECO:0000269|PubMed:21540484, ECO:0007744|PDB:2O2Q,
FT ECO:0007744|PDB:2O2R, ECO:0007744|PDB:3RHJ,
FT ECO:0007744|PDB:3RHL, ECO:0007744|PDB:3RHO,
FT ECO:0007744|PDB:3RHQ, ECO:0007744|PDB:3RHR"
FT BINDING 630..635
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:17302434,
FT ECO:0000269|PubMed:21540484, ECO:0007744|PDB:2O2Q,
FT ECO:0007744|PDB:2O2R, ECO:0007744|PDB:3RHJ,
FT ECO:0007744|PDB:3RHL, ECO:0007744|PDB:3RHO,
FT ECO:0007744|PDB:3RHQ, ECO:0007744|PDB:3RHR"
FT BINDING 650..651
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:17302434,
FT ECO:0000269|PubMed:21540484, ECO:0007744|PDB:2O2Q,
FT ECO:0007744|PDB:2O2R, ECO:0007744|PDB:3RHJ,
FT ECO:0007744|PDB:3RHL, ECO:0007744|PDB:3RHO,
FT ECO:0007744|PDB:3RHQ, ECO:0007744|PDB:3RHR"
FT BINDING 673..674
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:17302434,
FT ECO:0000269|PubMed:21540484, ECO:0007744|PDB:2O2Q,
FT ECO:0007744|PDB:3RHJ, ECO:0007744|PDB:3RHL,
FT ECO:0007744|PDB:3RHO, ECO:0007744|PDB:3RHQ,
FT ECO:0007744|PDB:3RHR"
FT BINDING 757
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:21540484,
FT ECO:0007744|PDB:3RHO"
FT BINDING 804..806
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:17302434,
FT ECO:0000269|PubMed:21540484, ECO:0007744|PDB:2O2Q,
FT ECO:0007744|PDB:3RHJ, ECO:0007744|PDB:3RHL,
FT ECO:0007744|PDB:3RHO, ECO:0007744|PDB:3RHQ,
FT ECO:0007744|PDB:3RHR"
FT SITE 142
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000269|PubMed:10585460"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75891"
FT MOD_RES 38
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8R0Y6"
FT MOD_RES 354
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000269|PubMed:17884809"
FT MOD_RES 629
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75891"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75891"
FT MOD_RES 660
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8K009"
FT MOD_RES 767
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8R0Y6"
FT MOD_RES 825
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75891"
FT MOD_RES 882
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q3SY69"
FT MUTAGEN 142
FT /note="D->A: Loss of formyltetrahydrofolate dehydrogenase
FT activity. Loss of formyltetrahydrofolate hydrolase
FT activity. No effect on aldehyde dehydrogenase activity."
FT /evidence="ECO:0000269|PubMed:10585460"
FT MUTAGEN 354
FT /note="S->A: Loss of phosphopantetheinylation. Loss of
FT formyltetrahydrofolate dehydrogenase activity. No effect on
FT hydrolase and aldehyde dehydrogenase activities in vitro."
FT /evidence="ECO:0000269|PubMed:17884809"
FT MUTAGEN 673
FT /note="E->A: Loss of aldehyde dehydrogenase activity."
FT /evidence="ECO:0000269|PubMed:17302434"
FT MUTAGEN 707
FT /note="C->A: Loss of formyltetrahydrofolate dehydrogenase
FT activity. No effect on formyltetrahydrofolate hydrolase
FT activity. No effect on NADP binding. No effect on
FT homotetramerization."
FT /evidence="ECO:0000269|PubMed:7822273"
FT CONFLICT 51..52
FT /note="VP -> RA (in Ref. 1; AAA70429)"
FT /evidence="ECO:0000305"
FT CONFLICT 283..284
FT /note="DD -> EH (in Ref. 1; AAA70429)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="G -> E (in Ref. 1; AAA70429)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="K -> R (in Ref. 1; AAA70429)"
FT /evidence="ECO:0000305"
FT CONFLICT 511
FT /note="A -> R (in Ref. 1; AAA70429)"
FT /evidence="ECO:0000305"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:1S3I"
FT HELIX 10..21
FT /evidence="ECO:0007829|PDB:1S3I"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:1S3I"
FT HELIX 41..49
FT /evidence="ECO:0007829|PDB:1S3I"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:1S3I"
FT HELIX 67..74
FT /evidence="ECO:0007829|PDB:1S3I"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:1S3I"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:1S3I"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:1S3I"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:1S3I"
FT TURN 110..113
FT /evidence="ECO:0007829|PDB:1S3I"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:1S3I"
FT HELIX 118..124
FT /evidence="ECO:0007829|PDB:1S3I"
FT STRAND 128..136
FT /evidence="ECO:0007829|PDB:1S3I"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:1S3I"
FT STRAND 146..153
FT /evidence="ECO:0007829|PDB:1S3I"
FT HELIX 160..166
FT /evidence="ECO:0007829|PDB:1S3I"
FT HELIX 168..185
FT /evidence="ECO:0007829|PDB:1S3I"
FT HELIX 206..209
FT /evidence="ECO:0007829|PDB:1S3I"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:1S3I"
FT HELIX 217..225
FT /evidence="ECO:0007829|PDB:1S3I"
FT TURN 226..231
FT /evidence="ECO:0007829|PDB:1S3I"
FT STRAND 233..237
FT /evidence="ECO:0007829|PDB:1S3I"
FT STRAND 240..249
FT /evidence="ECO:0007829|PDB:1S3I"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:1S3I"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:1S3I"
FT STRAND 276..280
FT /evidence="ECO:0007829|PDB:1S3I"
FT STRAND 286..294
FT /evidence="ECO:0007829|PDB:1S3I"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:1S3I"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:1S3I"
FT HELIX 318..334
FT /evidence="ECO:0007829|PDB:7RLU"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:7RLU"
FT HELIX 347..351
FT /evidence="ECO:0007829|PDB:7RLU"
FT HELIX 354..367
FT /evidence="ECO:0007829|PDB:7RLU"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:7RLU"
FT HELIX 375..380
FT /evidence="ECO:0007829|PDB:7RLU"
FT HELIX 384..395
FT /evidence="ECO:0007829|PDB:7RLU"
FT STRAND 409..413
FT /evidence="ECO:0007829|PDB:2O2P"
FT STRAND 416..420
FT /evidence="ECO:0007829|PDB:2O2P"
FT STRAND 423..426
FT /evidence="ECO:0007829|PDB:2O2P"
FT STRAND 429..431
FT /evidence="ECO:0007829|PDB:2O2P"
FT HELIX 434..436
FT /evidence="ECO:0007829|PDB:2O2P"
FT STRAND 438..442
FT /evidence="ECO:0007829|PDB:2O2P"
FT TURN 444..446
FT /evidence="ECO:0007829|PDB:2O2P"
FT STRAND 449..454
FT /evidence="ECO:0007829|PDB:2O2P"
FT HELIX 458..473
FT /evidence="ECO:0007829|PDB:2O2P"
FT HELIX 476..478
FT /evidence="ECO:0007829|PDB:2O2P"
FT HELIX 482..498
FT /evidence="ECO:0007829|PDB:2O2P"
FT HELIX 500..511
FT /evidence="ECO:0007829|PDB:2O2P"
FT HELIX 515..520
FT /evidence="ECO:0007829|PDB:2O2P"
FT TURN 521..523
FT /evidence="ECO:0007829|PDB:2O2P"
FT HELIX 524..536
FT /evidence="ECO:0007829|PDB:2O2P"
FT HELIX 537..539
FT /evidence="ECO:0007829|PDB:2O2P"
FT STRAND 542..545
FT /evidence="ECO:0007829|PDB:2O2P"
FT STRAND 553..563
FT /evidence="ECO:0007829|PDB:2O2P"
FT STRAND 566..570
FT /evidence="ECO:0007829|PDB:2O2P"
FT STRAND 573..575
FT /evidence="ECO:0007829|PDB:2O2P"
FT HELIX 576..589
FT /evidence="ECO:0007829|PDB:2O2P"
FT STRAND 593..597
FT /evidence="ECO:0007829|PDB:2O2P"
FT HELIX 604..615
FT /evidence="ECO:0007829|PDB:2O2P"
FT STRAND 622..625
FT /evidence="ECO:0007829|PDB:2O2P"
FT HELIX 630..639
FT /evidence="ECO:0007829|PDB:2O2P"
FT STRAND 645..650
FT /evidence="ECO:0007829|PDB:2O2P"
FT HELIX 652..664
FT /evidence="ECO:0007829|PDB:2O2P"
FT STRAND 669..673
FT /evidence="ECO:0007829|PDB:2O2P"
FT STRAND 678..682
FT /evidence="ECO:0007829|PDB:2O2P"
FT STRAND 684..686
FT /evidence="ECO:0007829|PDB:7RLU"
FT HELIX 688..700
FT /evidence="ECO:0007829|PDB:2O2P"
FT HELIX 701..704
FT /evidence="ECO:0007829|PDB:2O2P"
FT STRAND 710..716
FT /evidence="ECO:0007829|PDB:2O2P"
FT HELIX 717..731
FT /evidence="ECO:0007829|PDB:2O2P"
FT HELIX 752..767
FT /evidence="ECO:0007829|PDB:2O2P"
FT STRAND 771..774
FT /evidence="ECO:0007829|PDB:2O2P"
FT STRAND 780..783
FT /evidence="ECO:0007829|PDB:2O2P"
FT STRAND 789..793
FT /evidence="ECO:0007829|PDB:2O2P"
FT STRAND 796..798
FT /evidence="ECO:0007829|PDB:7RLU"
FT HELIX 799..801
FT /evidence="ECO:0007829|PDB:2O2P"
FT STRAND 807..815
FT /evidence="ECO:0007829|PDB:2O2P"
FT HELIX 821..827
FT /evidence="ECO:0007829|PDB:2O2P"
FT STRAND 830..834
FT /evidence="ECO:0007829|PDB:3RHM"
FT STRAND 837..839
FT /evidence="ECO:0007829|PDB:2O2P"
FT HELIX 843..852
FT /evidence="ECO:0007829|PDB:2O2P"
FT STRAND 855..861
FT /evidence="ECO:0007829|PDB:2O2P"
FT STRAND 868..870
FT /evidence="ECO:0007829|PDB:7RLU"
FT HELIX 876..878
FT /evidence="ECO:0007829|PDB:2O2P"
FT STRAND 879..881
FT /evidence="ECO:0007829|PDB:3RHQ"
FT HELIX 885..890
FT /evidence="ECO:0007829|PDB:2O2P"
FT STRAND 893..902
FT /evidence="ECO:0007829|PDB:2O2P"
SQ SEQUENCE 902 AA; 98874 MW; 562A8CBD73D6474A CRC64;
MKIAVIGQSL FGQEVYCQLR KEGHEVVGVF TIPDKDGKAD PLGLEAEKDG VPVFKFPRWR
ARGQALPEVV AKYQALGAEL NVLPFCSQFI PMEVINAPRH GSIIYHPSLL PRHRGASAIN
WTLIHGDKKG GFTIFWADDG LDTGDLLLQK ECEVLPDDTV STLYNRFLFP EGIKGMVQAV
RLIAEGTAPR CPQSEEGATY EGIQKKETAK INWDQPAEAI HNWIRGNDKV PGAWTEACGQ
KLTFFNSTLN TSGLSTQGEA LPIPGAHRPG VVTKAGLILF GNDDRMLLVK NIQLEDGKMM
PASQFFKGSA SSDLELTEAE LATAEAVRSS WMRILPNVPE VEDSTDFFKS GAASVDVVRL
VEEVKELCDG LELENEDVYM ATTFRGFIQL LVRKLRGEDD ESECVINYVE KAVNKLTLQM
PYQLFIGGEF VDAEGSKTYN TINPTDGSVI CQVSLAQVSD VDKAVAAAKE AFENGLWGKI
NARDRGRLLY RLADVMEQHQ EELATIEALD AGAVYTLALK THVGMSIQTF RYFAGWCDKI
QGATIPINQA RPNRNLTLTK KEPVGVCGIV IPWNYPLMML SWKTAACLAA GNTVVIKPAQ
VTPLTALKFA ELTLKAGIPK GVVNILPGSG SLVGQRLSDH PDVRKIGFTG STEVGKHIMK
SCALSNVKKV SLELGGKSPL IIFADCDLNK AVQMGMSSVF FNKGENCIAA GRLFVEESIH
NQFVQKVVEE VEKMKIGNPL ERDTNHGPQN HEAHLRKLVE YCQRGVKEGA TLVCGGNQVP
RPGFFFQPTV FTDVEDHMYI AKEESFGPIM IISRFADGDV DAVLSRANAT EFGLASGVFT
RDINKALYVS DKLQAGTVFI NTYNKTDVAA PFGGFKQSGF GKDLGEAALN EYLRIKTVTF
EY
