ID P5CR_CAEEL Reviewed; 299 AA. AC Q20848; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 25-NOV-2008, entry version 51. DE RecName: Full=Putative pyrroline-5-carboxylate reductase; DE Short=P5C reductase; DE Short=P5CR; DE EC=1.5.1.2; GN ORFNames=F55G1.9; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for RT investigating biology."; RL Science 282:2012-2018(1998). CC -!- CATALYTIC ACTIVITY: L-proline + NAD(P)(+) = 1-pyrroline-5- CC carboxylate + NAD(P)H. CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L- CC proline from L-glutamate 5-semialdehyde: step 1/1. CC -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase CC family. 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; U58750; AAB00645.1; -; Genomic_DNA. DR PIR; T29226; T29226. DR RefSeq; NP_501199.1; -. DR UniGene; Cel.12859; -. DR Ensembl; F55G1.9; Caenorhabditis elegans. DR GeneID; 177519; -. DR KEGG; cel:F55G1.9; -. DR NMPDR; fig|6239.3.peg.13938; -. DR WormBase; WBGene00018904; F55G1.9. DR WormPep; F55G1.9; CE07286. DR NextBio; 897180; -. DR ArrayExpress; Q20848; -. DR GO; GO:0005488; F:binding; IEA:InterPro. DR GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0006561; P:proline biosynthetic process; IEA:InterPro. DR InterPro; IPR004455; NADP_OxRdtase_F420. DR InterPro; IPR000304; P5CR. DR PANTHER; PTHR11645; P5CR; 1. DR Pfam; PF03807; F420_oxidored; 1. DR PIRSF; PIRSF000193; Pyrrol-5-carb_rd; 1. DR TIGRFAMs; TIGR00112; proC; 1. DR PROSITE; PS00521; P5CR; 1. PE 2: Evidence at transcript level; KW Amino-acid biosynthesis; Complete proteome; NADP; Oxidoreductase; KW Proline biosynthesis. FT CHAIN 1 299 Putative pyrroline-5-carboxylate FT reductase. FT /FTId=PRO_0000187321. SQ SEQUENCE 299 AA; 32057 MW; 75D2D6D32E0A5670 CRC64; MTIDTELTNG SSESVPFVFI GGGNMAAAII KGCQNKGFTP KSNIVIGVQT EKSAEKWRQL GYKNVFTNTL EMLERYSTAI YVICVKPQVF EEVVSSWPVN SRPEFIISVM AGVPLKVLNA KLPFVSGNTT IVRLMPNVAS SIGAGASTMC YEKNEKIMNQ DSHIELAREF AECVGTVELI PERCFNPAMA IGGSSPAWTF MYIESLADGA VAQGLGRAEA KRLAAQAVLG AAQMVLNSNS GFDIETQHFG SLKDMVCSPG GTTIEGVRAL EKNGFRYAVM EAVVAASTKA DEMAKSLAK //