O74766 (PUT2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable delta-1-pyrroline-5-carboxylate dehydrogenase
Short name=P5C dehydrogenase
EC=1.5.1.12

Gene names

ORF Names:

SPBC24C6.04

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	548 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (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.
Sequence similarities	Belongs to the aldehyde dehydrogenase family.

Ontologies

Keywords
Biological process	Proline metabolism
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	glutamate biosynthetic process Inferred from sequence or structural similarity. Source: GeneDB_Spombe proline biosynthetic process Inferred from sequence or structural similarity. Source: GeneDB_Spombe
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_Spombe mitochondrial matrix Inferred from electronic annotation. Source: InterPro
Molecular function	1-pyrroline-5-carboxylate dehydrogenase activity Inferred from sequence or structural similarity. Source: GeneDB_Spombe oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 548	548	Probable delta-1-pyrroline-5-carboxylate dehydrogenase		PRO_0000056502
Sites
	Active site	298	1	Proton acceptor By similarity
	Active site	332	1	Nucleophile By similarity
	Site	193	1	Transition state stabilizer By similarity
Amino acid modifications
	Modified residue	391	1	Phosphoserine Ref.3
	Modified residue	394	1	Phosphoserine Ref.3
	Modified residue	396	1	Phosphoserine Ref.3
Experimental info
	Sequence conflict	210	1	N → K in BAA13891. Ref.2
	Sequence conflict	264	1	L → F in BAA13891. Ref.2
	Sequence conflict	273 – 274	2	FR → IC in BAA13891. Ref.2
	Sequence conflict	294	1	K → N in BAA13891. Ref.2
	Sequence conflict	502	1	E → G in BAA13891. Ref.2
	Sequence conflict	516	1	K → E in BAA13891. Ref.2
	Sequence conflict	526	1	F → Y in BAA13891. Ref.2
	Sequence conflict	531	1	S → Y in BAA13891. Ref.2
	Sequence conflict	536	1	F → L in BAA13891. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O74766 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: E14D37E32A0B4B6E	FASTA	548	60,219
	10 20 30 40 50 60 MSQFAEFKLP AIKNEPPKHY GPNSADREGI VKAYKELEAE LPVTIPVIID GKEVETNTIG 70 80 90 100 110 120 EQRCPFEHKK VVARYHRAGA KHVEDAIEAA LRGKKVWESL PFADRSAIFL KAAHLISTKY 130 140 150 160 170 180 RYKLMAATMI GQGKNIWQAE IDAGMEIIDF LRFNTKYASE LYASQPPENT PGVWNRMEYR 190 200 210 220 230 240 PLEGFVYAIT PFNFTAIAGN LAAAPLLMGN VVLMKPSDHA VLSSYIVYQI FREAGLPAGA 250 260 270 280 290 300 LQFIPGDAVE VSKVCFNHPE FAGLHFTGST AVFRSLWGTI GENVANGKYR TYPKIVGETG 310 320 330 340 350 360 GKNFHLVHSS AEIKSAVVNA VRAAFEYQGQ KCSALSRLYV SKYAWENGFR DELTKQVKSL 370 380 390 400 410 420 KVGAPLTDFA NFVGPVIHQA SFNKLKKVLE SAASDSEIEV LAGGKADDSE GFFVEPTVLL 430 440 450 460 470 480 SKNPKHDIFV NELFGPVLSV YVYEDDNLDA VCDLIDTTTP YGLTGSIFAQ DRVVVRKLTD 490 500 510 520 530 540 RLRNAAGNFY INDKCTGAVV GEQPFGGARA SGTNDKAGSG MILSRFVSPR SIKDTFAYAD SVLYPSNF

References

[1]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.
[2]	"Identification of open reading frames in Schizosaccharomyces pombe cDNAs." Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H. DNA Res. 4:363-369(1997) [PubMed: 9501991] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 189-548. Strain: PR745.
[3]	"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391; SER-394 AND SER-396, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329671 Genomic DNA. Translation: CAA21148.1. D89230 mRNA. Translation: BAA13891.1.
PIR	T39968.
RefSeq	NP_595958.1. NM_001021867.1.
3D structure databases
ProteinModelPortal	O74766.
ModBase	Search...
Protein-protein interaction databases
STRING	O74766.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPBC24C6.04.1; SPBC24C6.04.1:pep; SPBC24C6.04.
GeneID	2540387.
KEGG	spo:SPBC24C6.04.
NMPDR	fig|4896.1.peg.1824.
Organism-specific databases
GeneDB_Spombe	SPBC24C6.04.
Phylogenomic databases
eggNOG	fuNOG06074.
GeneTree	EFGT00050000002268.
HOGENOM	HBG752218.
OMA	HLVHPSA.
OrthoDB	EOG4350FG.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-004021-MONOMER.
Gene expression databases
ArrayExpress	O74766.
Family and domain databases
InterPro	IPR016161. Ald_DH/histidinol_DH. IPR016163. Ald_DH_C. IPR016160. Ald_DH_CS. IPR016162. Ald_DH_N. IPR015590. Aldehyde_DH_dom. IPR005931. Delta1-pyrroline-5-COlate_DH-1. [Graphical view]
Gene3D	G3DSA:3.40.309.10. Aldehyde_dehydrogenase_C. 1 hit. G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
KO	K00294.
Pfam	PF00171. Aldedh. 1 hit. [Graphical view]
SUPFAM	SSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
TIGRFAMs	TIGR01236. D1pyr5carbox1. 1 hit.
PROSITE	PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit. PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PUT2_SCHPO

Accession

Primary (citable) accession number: O74766
Secondary accession number(s): P78880

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2003
Last sequence update:	November 1, 1998
Last modified:	December 14, 2011
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program