Q58DT4 (P5CR1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

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

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	320 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Housekeeping enzyme that catalyzes the last step in proline biosynthesis. Can utilize both NAD and NADP, but has higher affinity for NAD. Involved in the cellular response to oxidative stress By similarity.
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 By similarity.
Subcellular location	Mitochondrion By similarity.
Sequence similarities	Belongs to the pyrroline-5-carboxylate reductase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Proline biosynthesis Stress response
Cellular component	Mitochondrion
Ligand	NADP
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cellular response to oxidative stress Inferred from sequence or structural similarity. Source: UniProtKB proline biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	mitochondrion Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	nucleotide binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Inferred from electronic annotation. Source: InterPro pyrroline-5-carboxylate reductase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 320	319	Pyrroline-5-carboxylate reductase 1, mitochondrial		PRO_0000270817
Regions
	Nucleotide binding	6 – 11	6	NADP By similarity
	Nucleotide binding	69 – 72	4	NADP By similarity
	Nucleotide binding	95 – 97	3	NADP By similarity
Sites
	Binding site	34	1	NADP; via carbonyl oxygen By similarity
	Binding site	56	1	NADP By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q58DT4 [UniParc]. Last modified April 26, 2005. Version 1. Checksum: 0265F89F283CA765	FASTA	320	33,454
	10 20 30 40 50 60 MSVGFIGAGQ LAFALAKGFT AAGVVAAHKI MASSPDMDLA TVSALRKMGV NLTHHNKETV 70 80 90 100 110 120 QHSDVLFLAV KPHIIPFILD EIAANIEARH IVVSCAAGVT ISSIEKKLTA FQPAPKVIRC 130 140 150 160 170 180 MTNTPVVVRE GATVYATGTH AQVEDGRLLE QLMSSVGFCT EVEEDLIDAV TGLSGSGPAY 190 200 210 220 230 240 AFTALDALAD GGVKMGLPRR LAVRLGAQAL LGAAKMLLDS EQHPGQLKDN VCSPGGATIH 250 260 270 280 290 300 ALHVLESGGF RSLLIKAVEA SCTRTRELQS MADQEKVSPA AIKKTILDKV KLDSPPGTSL 310 320 APSGHSKLLP RSMAPAGKQD

References

[1]	"Characterization of 954 bovine full-CDS cDNA sequences." Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L. BMC Genomics 6:166-166(2005) [PubMed: 16305752] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]	NIH - Mammalian Gene Collection (MGC) project Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Fetal muscle.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BT021513 mRNA. Translation: AAX46360.1. BC123510 mRNA. Translation: AAI23511.1.
IPI	IPI00694230.
RefSeq	NP_001014957.1. NM_001014957.1.
UniGene	Bt.12489.
3D structure databases
ProteinModelPortal	Q58DT4.
SMR	Q58DT4. Positions 1-275.
ModBase	Search...
Protein-protein interaction databases
STRING	Q58DT4.
Proteomic databases
PRIDE	Q58DT4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSBTAT00000000046; ENSBTAP00000000046; ENSBTAG00000000042.
GeneID	539606.
KEGG	bta:539606.
Organism-specific databases
CTD	5831.
Phylogenomic databases
eggNOG	maNOG15544.
GeneTree	ENSGT00390000007443.
HOVERGEN	HBG053399.
InParanoid	Q58DT4.
OMA	SSGLVAW.
OrthoDB	EOG4PZJ76.
PhylomeDB	Q58DT4.
Family and domain databases
InterPro	IPR008927. 6-PGluconate_DH_C-like. IPR016040. NAD(P)-bd_dom. IPR004455. NADP_OxRdtase_F420. IPR000304. Pyrroline-COOH_reductase. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KO	K00286.
PANTHER	PTHR11645. P5CR. 1 hit.
Pfam	PF03807. F420_oxidored. 1 hit. [Graphical view]
PIRSF	PIRSF000193. Pyrrol-5-carb_rd. 1 hit.
SUPFAM	SSF48179. 6DGDH_C_like. 1 hit.
TIGRFAMs	TIGR00112. ProC. 1 hit.
PROSITE	PS00521. P5CR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

P5CR1_BOVIN

Accession

Primary (citable) accession number: Q58DT4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 9, 2007
Last sequence update:	April 26, 2005
Last modified:	December 14, 2011
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program