ID   P5CR1_HUMAN             Reviewed;         319 AA.
AC   P32322; Q6FHI4; Q96DI6;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 2.
DT   25-NOV-2008, entry version 74.
DE   RecName: Full=Pyrroline-5-carboxylate reductase 1, mitochondrial;
DE            Short=P5C reductase 1;
DE            Short=P5CR 1;
DE            EC=1.5.1.2;
DE   Flags: Precursor;
GN   Name=PYCR1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=92112821; PubMed=1730675;
RA   Dougherty K.M., Brandriss M.C., Valle D.;
RT   "Cloning human pyrroline-5-carboxylate reductase cDNA by
RT   complementation in Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 267:871-875(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
RA   Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA   Korn B., Zuo D., Hu Y., LaBaer J.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lymph, and Placenta;
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).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS), AND SUBUNIT.
RX   PubMed=16730026; DOI=10.1016/j.jmb.2006.04.053;
RA   Meng Z., Lou Z., Liu Z., Li M., Zhao X., Bartlam M., Rao Z.;
RT   "Crystal structure of human pyrroline-5-carboxylate reductase.";
RL   J. Mol. Biol. 359:1364-1377(2006).
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   -!- SUBUNIT: Homodecamer; composed of 5 homodimers.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity).
CC   -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase
CC       family.
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DR   EMBL; M77836; AAA36407.1; -; mRNA.
DR   EMBL; CR541769; CAG46568.1; -; mRNA.
DR   EMBL; BC001504; AAH01504.1; -; mRNA.
DR   EMBL; BC071842; AAH71842.1; -; mRNA.
DR   PIR; A41770; A41770.
DR   RefSeq; NP_008838.2; -.
DR   UniGene; Hs.458332; -.
DR   PDB; 2GER; X-ray; 3.10 A; A/B/C/D/E=1-319.
DR   PDB; 2GR9; X-ray; 3.10 A; A/B/C/D/E=1-275.
DR   PDB; 2GRA; X-ray; 3.10 A; A/B/C/D/E=1-275.
DR   PDB; 2IZZ; X-ray; 1.95 A; A/B/C/D/E=1-300.
DR   PDBsum; 2GER; -.
DR   PDBsum; 2GR9; -.
DR   PDBsum; 2GRA; -.
DR   PDBsum; 2IZZ; -.
DR   Ensembl; ENSG00000183010; Homo sapiens.
DR   GeneID; 5831; -.
DR   KEGG; hsa:5831; -.
DR   H-InvDB; HIX0014258; -.
DR   HGNC; HGNC:9721; PYCR1.
DR   MIM; 179035; gene.
DR   PharmGKB; PA34064; -.
DR   HOGENOM; P32322; -.
DR   HOVERGEN; P32322; -.
DR   BioCyc; MetaCyc:MON-11444; -.
DR   Reactome; REACT_13; Metabolism of amino acids.
DR   DrugBank; DB00172; L-Proline.
DR   DrugBank; DB00157; NADH.
DR   NextBio; 22720; -.
DR   ArrayExpress; P32322; -.
DR   CleanEx; HS_PYCR1; -.
DR   GermOnline; ENSG00000183010; Homo sapiens.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; TAS:ProtInc.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006561; P:proline biosynthetic process; TAS:ProtInc.
DR   InterPro; IPR016040; NAD(P)-bd.
DR   InterPro; IPR004455; NADP_OxRdtase_F420.
DR   InterPro; IPR000304; P5CR.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
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   1: Evidence at protein level;
KW   3D-structure; Amino-acid biosynthesis; Mitochondrion; NADP;
KW   Oxidoreductase; Proline biosynthesis; Transit peptide.
FT   TRANSIT       1     26       Mitochondrion (Potential).
FT   CHAIN        27    319       Pyrroline-5-carboxylate reductase 1,
FT                                mitochondrial.
FT                                /FTId=PRO_0000187314.
FT   CONFLICT    155    155       S -> T (in Ref. 1; AAA36407).
FT   CONFLICT    317    317       G -> S (in Ref. 2; CAG46568).
FT   STRAND        3      7
FT   HELIX        10     21
FT   HELIX        27     29
FT   STRAND       30     33
FT   HELIX        40     48
FT   STRAND       51     54
FT   HELIX        56     62
FT   STRAND       64     68
FT   HELIX        72     74
FT   HELIX        75     82
FT   HELIX        83     85
FT   STRAND       91     94
FT   HELIX       101    109
FT   STRAND      116    121
FT   HELIX       124    128
FT   STRAND      131    137
FT   HELIX       143    154
FT   STRAND      157    161
FT   HELIX       164    166
FT   HELIX       167    173
FT   TURN        174    176
FT   HELIX       177    194
FT   HELIX       199    219
FT   HELIX       224    231
FT   HELIX       237    247
FT   HELIX       250    270
SQ   SEQUENCE   319 AA;  33361 MW;  9E8C4DED0638EFC5 CRC64;
     MSVGFIGAGQ LAFALAKGFT AAGVLAAHKI MASSPDMDLA TVSALRKMGV KLTPHNKETV
     QHSDVLFLAV KPHIIPFILD EIGADIEDRH IVVSCAAGVT ISSIEKKLSA FRPAPRVIRC
     MTNTPVVVRE GATVYATGTH AQVEDGRLME QLLSSVGFCT EVEEDLIDAV TGLSGSGPAY
     AFTALDALAD GGVKMGLPRR LAVRLGAQAL LGAAKMLLHS EQHPGQLKDN VSSPGGATIH
     ALHVLESGGF RSLLINAVEA SCIRTRELQS MADQEQVSPA AIKKTILDKV KLDSPAGTAL
     SPSGHTKLLP RSLAPAGKD
//