NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1159/000079829; PubMed=15383718 [NCBI, ExPASy, EBI, Israel, Japan]
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential.";
J. Mol. Microbiol. Biotechnol. 7:204-211(2004).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1186/gb-2004-5-10-r77; PubMed=15461803 [NCBI, ExPASy, EBI, Israel, Japan]
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species.";
Genome Biol. 5:RESEARCH077.1-RESEARCH077.12(2004).

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

AE017333; AAU39332.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000002; AAU21978.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_077616.1; -.
YP_090025.1; -.

3D structure databases

ModBase

Q65NN2.

Enzyme and pathway databases

BioCyc

BLIC279010:BL01710-MON; -.

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).
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.

BLOCKS

Q65NN2.

Genome annotation databases

GeneID

3027308; -.
3097821; -.

GenomeReviews

CP000002_GR; BL01710.
AE017333_GR; BLi00374.

KEGG

bld:BLi00374; -.
bli:BL01710; -.

NMPDR

fig|279010.5.peg.2227; -.

Phylogenomic databases

HOGENOM

Q65NN2; -.

Genome annotation databases

CMR

Q65NN2; BLi00374.

Other

ProtoNet

Q65NN2.

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`	`1 516`	`516`	`1-pyrroline-5-carboxylate dehydrogenase.`	`PRO_0000056510`
`ACT_SITE`	`287 287`		`By similarity.`
`ACT_SITE`	`321 321`		`By similarity.`

Sequence information

Length: 516 AA [This is the length of the unprocessed precursor]

Molecular weight: 56655 Da [This is the MW of the unprocessed precursor]

CRC64: 9BB008CC70ABBFDB [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTTPYKHEPF TNFGIEENRK AFEKALETVN NEWLGQSYPL VIDGERYETE NKIVSINPAN 

        70         80         90        100        110        120 
KEEVVGTVSK ATQDHAEKAI QAAAKAFETW RYTDPEERAA VLFRAVAKVR RKKHEFSALL 

       130        140        150        160        170        180 
VKEAGKPWNE ADADTAEAID FMEYYARQMI ELAKGKPVNS REGERNQYVY TPTGVTVVIP 

       190        200        210        220        230        240 
PWNFLFAIMA GTTVAPIVTG NTVVLKPASA APVIAAKFVE VLEESGLPKG VVNFVPGSGA 

       250        260        270        280        290        300 
EVGDYLVDHP KTSIITFTGS REVGTRIFER AAKVQPGQTH LKQVIAEMGG KDTVVVDEDC 

       310        320        330        340        350        360 
DIELAAQSIF TSAFGFAGQK CSAGSRAVVH EKVYDEVLKR VIEITESKKV GEPDSADVYM 

       370        380        390        400        410        420 
GPVIDQASFN KIMDYIEIGK EEGRLVSGGK GDDSKGYFIE PTIFADLDPK ARLMQEEIFG 

       430        440        450        460        470        480 
PVVAFSKVSS FDEALEVANN TEYGLTGAVI TKNRDHINRA KQEFHVGNLY FNRNCTGAIV 

       490        500        510 
GYHPFGGFKM SGTDSKAGGP DYLALHMQAK TISEMF

Q65NN2 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