ID AL1L2_MOUSE Reviewed; 923 AA. AC Q8K009; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 16-JUN-2009, entry version 52. DE RecName: Full=Probable 10-formyltetrahydrofolate dehydrogenase ALDH1L2; DE EC=1.5.1.6; DE AltName: Full=Aldehyde dehydrogenase family 1 member L2; GN Name=Aldh1l2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Salivary gland; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- CATALYTIC ACTIVITY: 10-formyltetrahydrofolate + NADP(+) + H(2)O = CC tetrahydrofolate + CO(2) + NADPH. CC -!- SIMILARITY: In the N-terminal section; belongs to the GART family. CC -!- SIMILARITY: In the C-terminal section; belongs to the aldehyde CC dehydrogenase family. ALDH1L subfamily. CC -!- SIMILARITY: Contains 1 acyl carrier domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BC034531; AAH34531.1; -; mRNA. DR IPI; IPI00169472; -. DR RefSeq; NP_705771.1; -. DR UniGene; Mm.263138; -. DR HSSP; P28037; 1S3I. DR SMR; Q8K009; 426-923. DR PRIDE; Q8K009; -. DR Ensembl; ENSMUSG00000020256; Mus musculus. DR GeneID; 216188; -. DR KEGG; mmu:216188; -. DR MGI; MGI:2444680; Aldh1l2. DR HOGENOM; Q8K009; -. DR HOVERGEN; Q8K009; -. DR BRENDA; 1.5.1.6; 244. DR NextBio; 375062; -. DR ArrayExpress; Q8K009; -. DR Bgee; Q8K009; -. DR CleanEx; MM_ALDH1L2; -. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0000036; F:acyl carrier activity; IEA:InterPro. DR GO; GO:0016155; F:formyltetrahydrofolate dehydrogenase activity; IEA:EC. DR GO; GO:0016742; F:hydroxymethyl-, formyl- and related transfe...; IEA:InterPro. DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro. DR GO; GO:0009258; P:10-formyltetrahydrofolate catabolic process; IEA:InterPro. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR GO; GO:0006730; P:one-carbon compound metabolic process; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR011407; 10_FTHF_DH. DR InterPro; IPR009081; Acyl_carrier_prot-like. DR InterPro; IPR016160; Ald_DH_CS. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH. DR InterPro; IPR005793; Formyl_trans_C. DR InterPro; IPR002376; Formyl_transf_N. DR InterPro; IPR001555; GART_AS. DR InterPro; IPR006162; Ppantne_S. DR Gene3D; G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1. DR Gene3D; G3DSA:3.10.25.10; Formyl_trans_C; 1. DR Gene3D; G3DSA:3.40.50.170; Formyl_transf_N; 1. DR PANTHER; PTHR11699; Aldehyde_dehyd; 1. 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 PROSITE; PS50075; ACP_DOMAIN; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. DR PROSITE; PS00373; GART; 1. DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1. PE 2: Evidence at transcript level; KW NADP; One-carbon metabolism; Oxidoreductase; Phosphopantetheine. FT CHAIN 1 923 Probable 10-formyltetrahydrofolate FT dehydrogenase ALDH1L2. FT /FTId=PRO_0000316002. FT DOMAIN 344 413 Acyl carrier. FT REGION 23 225 GART. FT REGION 438 923 Aldehyde dehydrogenase. FT ACT_SITE 128 128 Proton donor (By similarity). FT ACT_SITE 694 694 By similarity. FT ACT_SITE 728 728 By similarity. FT SITE 164 164 Essential for catalytic activity (By FT similarity). FT MOD_RES 375 375 O-(pantetheine 4'-phosphoryl)serine (By FT similarity). SQ SEQUENCE 923 AA; 101564 MW; 441D57CAF3D11303 CRC64; MLWRGSQALR HFSTSRVYFK NKLKLALIGQ SLFGQEVYSQ LLKEGHRVVG VFTVPDKDGK ADPLALAAEK DGTPVFKFPR WRLKGKTIKE VAEAYQSVGA ELNVLPFCTQ FIPMDVIDSP KHGSIIYHPS LLPRHRGASA INWTLIMGDK KAGFSVFWAD DGLDTGPILL QRSCDVKPND TVDSLYNRFL FPEGIKAMVE AVQLIADGKA PRTPQPEEGA TYEGIQKKEN AEVSWDQPAE GLHNWIRGHD KVPGAWAEIN GQMVTFYGSS LLTSSVPSGE PLDIRGAKKP GLVTKNGLVL FGNDGKALMV RNLQFEDGKM IPASQYFSAG ETSVVELTAE ELKVAETIKV IWARILSNTP VIEDSTDFFK SGASSMDVVR LVEEIRQSCG GLQLQNEDVY MATKFGDFIQ KVVRRLRGED EEAEMVVDYV SKEVNGMTVK IPYQCFINGQ FVDAEDGETY ATVNPTDGTT ICRVSHASLA DVDRAVAAAK DAFENGEWGR MNARDRGRLM YRLADLMEEN QEELATIEAL DSGAVYTLAL KTHIGMSVQT FRYFAGWCDK IQGSTIPINQ ARPNYNLTFT KKEPLGACAI IIPWNYPLMM LAWKSAACLA AGNTLVLKPA QVTPLTALKF AELTVKAGFP KGVINIIPGS GGVAGQRLSQ HPDIRKLGFT GSTSVGKQIM KSCAVSNLKK VSLELGGKSP LIIFSDCDLE KAVRMGMGAV FFNKGENCIA AGRLFVEEAI HDEFVTRVVE EIKKMKIGDP LDRSTDHGPQ NHRAHLEKLL QYCETGVQEG ATLVYGGRQV QRPGFFMEPT VFTGVEDHMY LAKEESFGPI MVISKFQNGD IDGVLQRANN TEYGLASGVF TRDINKAMYV SDKLEAGTVF INTYNKTDVA APFGGMKQSG FGKDLGEEAL NEYLKIKTVT LEY //