Pyrroline-5-carboxylate reductase 1, mitochondrial

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Reviewed, UniProtKB/Swiss-Prot P32322 (P5CR1_HUMAN)

Last modified June 16, 2009. Version 81. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Pyrroline-5-carboxylate reductase 1, mitochondrial
      Short name=P5C reductase 1
      Short name=P5CR 1
    EC=1.5.1.2

Gene names

Name:

PYCR1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	319 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Catalytic activity	L-proline + NAD(P)⁺ = 1-pyrroline-5-carboxylate + NAD(P)H.
Pathway	Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step 1/1.
Subunit structure	Homodecamer; composed of 5 homodimers. Ref.7
Subcellular location	Mitochondrion By similarity.
Sequence similarities	Belongs to the pyrroline-5-carboxylate reductase family.

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Ontologies

Keywords
Biological process	Amino-acid biosynthesis Proline biosynthesis
Cellular component	Mitochondrion
Ligand	NADP
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW proline biosynthetic process Ref.1 Traceable author statement. Source: ProtInc
Cellular component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	binding Inferred from electronic annotation. Source: InterPro pyrroline-5-carboxylate reductase activity Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.4 Ref.5

Chain

2 – 319

318

Pyrroline-5-carboxylate reductase 1, mitochondrial

PRO_0000187314

Amino acid modifications

Modified residue

N-acetylserine Ref.4 Ref.5

Experimental info

Sequence conflict

155

S → T in AAA36407. Ref.1

Sequence conflict

317

G → S in CAG46568. Ref.2

Secondary structure

319

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P32322-1 [UniParc].

Last modified March 1, 2005. Version 2.
Checksum: 9E8C4DED0638EFC5
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FASTA

319

33,361

        10         20         30         40         50         60 
MSVGFIGAGQ LAFALAKGFT AAGVLAAHKI MASSPDMDLA TVSALRKMGV KLTPHNKETV 

        70         80         90        100        110        120 
QHSDVLFLAV KPHIIPFILD EIGADIEDRH IVVSCAAGVT ISSIEKKLSA FRPAPRVIRC 

       130        140        150        160        170        180 
MTNTPVVVRE GATVYATGTH AQVEDGRLME QLLSSVGFCT EVEEDLIDAV TGLSGSGPAY 

       190        200        210        220        230        240 
AFTALDALAD GGVKMGLPRR LAVRLGAQAL LGAAKMLLHS EQHPGQLKDN VSSPGGATIH 

       250        260        270        280        290        300 
ALHVLESGGF RSLLINAVEA SCIRTRELQS MADQEQVSPA AIKKTILDKV KLDSPAGTAL 

       310 
SPSGHTKLLP RSLAPAGKD

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning human pyrroline-5-carboxylate reductase cDNA by complementation in Saccharomyces cerevisiae." Dougherty K.M., Brandriss M.C., Valle D. J. Biol. Chem. 267:871-875(1992) [PubMed: 1730675] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lymph and Placenta.
[4]	Bienvenut W.V., Zebisch A., Kolch W. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-17 AND 205-215, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, MASS SPECTROMETRY. Tissue: Colon carcinoma.
[5]	Bienvenut W.V., Waridel P., Quadroni M. Submitted (MAR-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-46; 130-147; 205-215 AND 252-264, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[6]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[7]	"Crystal structure of human pyrroline-5-carboxylate reductase." Meng Z., Lou Z., Liu Z., Li M., Zhao X., Bartlam M., Rao Z. J. Mol. Biol. 359:1364-1377(2006) [PubMed: 16730026] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS), SUBUNIT.

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Cross-references

Sequence databases

M77836 mRNA. Translation: AAA36407.1.
CR541769 mRNA. Translation: CAG46568.1.
BC001504 mRNA. Translation: AAH01504.1.
BC071842 mRNA. Translation: AAH71842.1.

IPI

IPI00550882.

PIR

A41770.

RefSeq

NP_008838.2.

UniGene

Hs.458332

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2GER	X-ray	3.10	A/B/C/D/E	1-319	[»]
2GR9	X-ray	3.10	A/B/C/D/E	1-275	[»]
2GRA	X-ray	3.10	A/B/C/D/E	1-275	[»]
2IZZ	X-ray	1.95	A/B/C/D/E	1-300	[»]

ModBase

Search...

Proteomic databases

PRIDE

P32322.

Genome annotation databases

Ensembl

ENSG00000183010. Homo sapiens. [Contig view]

GeneID

5831.

KEGG

hsa:5831.

Organism-specific databases

GeneCards

GC17M077484.

H-InvDB

HIX0014258.

HGNC

HGNC:9721. PYCR1.

MIM

179035. gene.

PharmGKB

PA34064.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P32322.

HOVERGEN

P32322.

OMA

P32322. APSGHSK.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-11444.

BRENDA

1.5.1.2. 247.

Reactome

REACT_13. Metabolism of amino acids.

Gene expression databases

ArrayExpress

P32322.

Bgee

P32322.

CleanEx

HS_PYCR1.

GermOnline

ENSG00000183010. Homo sapiens.

Family and domain databases

InterPro

IPR016040. NAD(P)-bd_dom.
IPR004455. NADP_OxRdtase_F420.
IPR000304. P5CR.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

PANTHER

PTHR11645. P5CR. 1 hit.

Pfam

PF03807. F420_oxidored. 1 hit.
[Graphical view]

PIRSF

PIRSF000193. Pyrrol-5-carb_rd. 1 hit.

TIGRFAMs

TIGR00112. proC. 1 hit.

PROSITE

PS00521. P5CR. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00172. L-Proline.
DB00157. NADH.

NextBio

22720.

SOURCE

Search...

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Entry information

Entry name

P5CR1_HUMAN

Accession

Primary (citable) accession number: P32322
Secondary accession number(s): Q6FHI4, Q96DI6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	March 1, 2005
Last modified:	June 16, 2009
This is version 81 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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