[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1016/S0140-6736(00)04403-2; PubMed=11418146 [NCBI, ExPASy, EBI, Israel, Japan] Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y., Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., Hiramatsu K.; "Whole genome sequencing of meticillin-resistant Staphylococcus aureus."; Lancet 357:1225-1240(2001).
[2]	IDENTIFICATION BY MASS SPECTROMETRY. DOI=10.1016/j.mimet.2004.09.017; PubMed=15590099 [NCBI, ExPASy, EBI, Israel, Japan] Scherl A., Francois P., Bento M., Deshusses J.M., Charbonnier Y., Converset V., Huyghe A., Walter N., Hoogland C., Appel R.D., Sanchez J.-C., Zimmermann-Ivol C.G., Corthals G.L., Hochstrasser D.F., Schrenzel J.; "Correlation of proteomic and transcriptomic profiles of Staphylococcus aureus during the post-exponential phase of growth."; J. Microbiol. Methods 60:247-257(2005).
[3]	IDENTIFICATION BY MASS SPECTROMETRY. Vaezzadeh A.R., Deshusses J., Lescuye P., Hochstrasser D.F.; "Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315."; Submitted (OCT-2007) to UniProtKB.

Comments

CATALYTIC ACTIVITY: (S)-1-pyrroline-5-carboxylate + NAD(P)⁺ + 2 H₂O = L-glutamate + NAD(P)H.
PATHWAY: Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 2/2 .
SIMILARITY: Belongs to the aldehyde dehydrogenase family. RocA subfamily.

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

BA000018; BAB43645.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

C90060; C90060.

RefSeq

NP_375666.1; -.

3D structure databases

HSSP

Q28399; 1O9J. [HSSP ENTRY / PDB]

ModBase

P99076.

Enzyme and pathway databases

BioCyc

SAUR158879:SA2341-MON; -.

2D gel databases

SWISS-2DPAGE

P99076; -.

Ontologies

GO:0003842;	Molecular function: 1-pyrroline-5-carboxylate dehydrogenase activity (inferred from electronic annotation from HAMAP).
GO:0006537;	Biological process: glutamate biosynthetic process (inferred from electronic annotation from HAMAP).
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

HAMAP

MF_00733; -; 1.
PBIL [Tree]

InterPro

IPR016160; Ald_DHase_CS.
IPR016162; Ald_DHase_N.
IPR015590; Aldehyde_DHase.
IPR005932; d-1-pyrroline-5-COlate_DHase-2.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.

PANTHER

PTHR11699; Aldehyde_dehyd; 1.

Pfam

PF00171; Aldedh; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR01237; D1pyr5carbox2; 1.

PROSITE

PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PS00687; ALDEHYDE_DEHYDR_GLU; 1.

ProtoNet

P99076.

Genome annotation databases

GeneID

1125269; -.

GenomeReviews

BA000018_GR; SA2341.

KEGG

sau:SA2341; -.

Phylogenomic databases

HOGENOM

P99076; -.

Genome annotation databases

CMR

P99076; SA2341.

Other

UniRef

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

Keywords

Complete proteome; NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 514`	`514`	`1-pyrroline-5-carboxylate dehydrogenase.`	`PRO_0000056516`
`ACT_SITE`	`286 286`		`By similarity.`
`ACT_SITE`	`320 320`		`By similarity.`

Sequence information

Length: 514 AA [This is the length of the unprocessed precursor]

Molecular weight: 56868 Da [This is the MW of the unprocessed precursor]

CRC64: 117DF65C22339CDB [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVVEFKNEPG YDFSVQENVD MFKKALKDVE KELGQDIPLV INGEKIFKDD KIKSINPADT 

        70         80         90        100        110        120 
SQVIANASKA TKQDVEDAFK AANEAYKSWK TWSANDRAEL MLRVSAIIRR RKAEIAAIMV 

       130        140        150        160        170        180 
YEAGKPWDEA VGDAAEGIDF IEYYARSMMD LAQGKPVLDR EGEHNKYFYK SIGTGVTIPP 

       190        200        210        220        230        240 
WNFPFAIMAG TTLAPVVAGN TVLLKPAEDT PYIAYKLMEI LEEAGLPKGV VNFVPGDPKE 

       250        260        270        280        290        300 
IGDYLVDHKD THFVTFTGSR ATGTRIYERS AVVQEGQNFL KRVIAEMGGK DAIVVDENID 

       310        320        330        340        350        360 
TDMAAEAIVT SAFGFSGQKC SACSRAIVHK DVYDEVLEKS IKLTKELTLG NTVDNTYMGP 

       370        380        390        400        410        420 
VINKKQFDKI KNYIEIGKEE GKLEQGGGTD DSKGYFVEPT IISGLKSKDR IMQEEIFGPV 

       430        440        450        460        470        480 
VGFVKVNDFD EAIEVANDTD YGLTGAVITN NREHWIKAVN EFDVGNLYLN RGCTSAVVGY 

       490        500        510 
HPFGGFKMSG TDAKTGSPDY LLHFLEQKVV SEMF

P99076 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