NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=VF5;
DOI=10.1038/32831; PubMed=9537320 [NCBI, ExPASy, EBI, Israel, Japan]
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
Nature 392:353-358(1998).

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 .
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AE000657; AAC06504.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

F70315; F70315.

RefSeq

NP_213113.1; -.

3D structure databases

ModBase

O66553.

Enzyme and pathway databases

BioCyc

AAEO224324:AQ_166-MON; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0005488;	Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0004735;	Molecular function: pyrroline-5-carboxylate reductase activity (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006561;	Biological process: proline biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR016040; NAD(P)-bd.
IPR004455; NADP_OxRdtase_F420.
IPR000304; P5CR.
Graphical view of domain structure.

Gene3D

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

PANTHER

PTHR11645; P5CR; 1.

Pfam

PF03807; F420_oxidored; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000193; Pyrrol-5-carb_rd; 1.

TIGRFAMs

TIGR00112; proC; 1.

PROSITE

PS00521; P5CR; 1.

Genome annotation databases

1192696; -.

AE000657_GR; aq_166.

aae:aq_166; -.

fig|224324.1.peg.128; -.

Phylogenomic databases

HOGENOM

O66553; -.

Other

LinkHub

O66553; -.

Genome annotation databases

CMR

O66553; aq_166.

Other

ProtoNet

O66553.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Amino-acid biosynthesis; Complete proteome; Cytoplasm; NADP; Oxidoreductase; Proline biosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 265`	`265`		`Pyrroline-5-carboxylate reductase.`	`PRO_0000187284`

Sequence information

Length: 265 AA [This is the length of the unprocessed precursor]

Molecular weight: 28814 Da [This is the MW of the unprocessed precursor]

CRC64: 32DD6B49EDDCF403 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MHAIILTMRV GIVGFGNMGQ AFALCFSKKL GKENIIVTDK VQEKRNLATE MGIAFASDVK 

        70         80         90        100        110        120 
FLADNSDVVL VAVKPKDSQE VLQKLKDYKG IILSIMAGVS IEKMEKILGK DKKIVRVMPN 

       130        140        150        160        170        180 
VNVAVGSGVM AITDNGNLSE EERSKVEELL LSCGTLYRIE ERLFDAFTAL AGSGPAFVFS 

       190        200        210        220        230        240 
FIDALALAGV HQGFSYEQAL RIALDTVMGS AKLLKEFQVN PNELIAKVTS PGGTTIEGIK 

       250        260 
YLEEKGFKGT VMECINRTSQ KAKKL

O66553 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools