NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=301 / Serotype 2a;
DOI=10.1093/nar/gkf566; PubMed=12384590 [NCBI, ExPASy, EBI, Israel, Japan]
Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
"Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157.";
Nucleic Acids Res. 30:4432-4441(2002).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700930 / 2457T / Serotype 2a;
DOI=10.1128/IAI.71.5.2775-2786.2003; PubMed=12704152 [NCBI, ExPASy, EBI, Israel, Japan]
Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
"Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T.";
Infect. Immun. 71:2775-2786(2003).

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

AE005674; AAN41981.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014073; AAP15859.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_706274.1; -.
NP_836053.1; -.

3D structure databases

ModBase

P0A9L9.

Enzyme and pathway databases

BioCyc

SFLE198214:AAN41981.1-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

GeneID

1027435; -.
1076763; -.

GenomeReviews

AE005674_GR; SF0322.
AE014073_GR; S0330.

KEGG

sfl:SF0322; -.
sfx:S0330; -.

Phylogenomic databases

HOGENOM

P0A9L9; -.

Genome annotation databases

CMR

P0A9L9; SF0322.

Other

ProtoNet

P0A9L9.

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`	`1 269`	`269`		`Pyrroline-5-carboxylate reductase.`	`PRO_0000187297`

Sequence information

Length: 269 AA [This is the length of the unprocessed precursor]

Molecular weight: 28145 Da [This is the MW of the unprocessed precursor]

CRC64: C5E2CED36BCC508D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEKKIGFIGC GNMGKAILGG LIASGQVLPG QIWVYTPSPD KVAALHDQFG INAAESAQEV 

        70         80         90        100        110        120 
AQIADIIFAA VKPGIMIKVL SEITSSLNKD SLVVSIAAGV TLDQLARALG HDRKIIRAMP 

       130        140        150        160        170        180 
NTPALVNAGM TSVTPNALVT PEDTADVLNI FRCFGEAEVI AEPMIHPVVG VSGSSPAYVF 

       190        200        210        220        230        240 
MFIEAMADAA VLGGMPRAQA YKFAAQAVMG SAKMVLETGE HPGALKDMVC SPGGTTIEAV 

       250        260 
RVLEEKGFRA AVIEAMTKCM EKSEKLSKS

P0A9L9 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