Q54RA2 (AL4A1_DICDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial
Short name=P5C dehydrogenase
EC=1.5.1.12

Alternative name(s):
Aldehyde dehydrogenase family 4 member A1 homolog

Gene names

ORF Names:

DDB_G0283293

Organism

Dictyostelium discoideum (Slime mold)

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	558 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Irreversible conversion of delta-1-pyrroline-5-carboxylate (P5C), derived either from proline or ornithine, to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles By similarity.
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.
Subcellular location	Mitochondrion matrix By similarity.
Sequence similarities	Belongs to the aldehyde dehydrogenase family.

Ontologies

Keywords
Biological process	Proline metabolism
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	proline biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	1-pyrroline-5-carboxylate dehydrogenase activity Inferred from electronic annotation. Source: EC 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
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 558		Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial		PRO_0000342183
Regions
	Nucleotide binding	286 – 291	6	NAD By similarity
Sites
	Active site	306	1	By similarity
	Active site	340	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q54RA2 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: 6F6ACCB3479EB1AA	FASTA	558	61,633
	10 20 30 40 50 60 MLRNTSRVLM SHFARANIPT PVNQPMLNYE VGSTHRKLLK EACAKFRNTT IDIPCVVGGK 70 80 90 100 110 120 EIRTGDVQKQ LICSDHNKVL ATFHQANAEL LKLAVENSME SKAQWESLPF EARSAVFLKA 130 140 150 160 170 180 ADLLNTKYRY DVLASTMLGQ GKTVWQAEID AAAEGIDFLR FNVKYAQEIY QQQPPANSAG 190 200 210 220 230 240 CWNILTYQPL EGYVVAISPF NFTAIGLNLS SAPALMGNVV LWKPASTAVL SNWIVYKALL 250 260 270 280 290 300 EAGLPAGVIQ FLPGSGRLVG EHLFNNRNFS GLHFTGSTGV FNDIYKKTAD NLVAGVYKGY 310 320 330 340 350 360 PRIVGETGGK DFHFLHNSGD VENFVNNTLR GAFEYQGQKC SACSRAYIPQ SLWPQIKDRL 370 380 390 400 410 420 VTGVKSMKMG QSDDFSSFVS AVIDKNSFNN IQSYIEHAKA SPDAEIIVGG KCDSSVGWFV 430 440 450 460 470 480 EPTIILAKDP HYKSMEEEIF GPVLTIYVYE DSKFEETLKI CDETSPYALT GSIFSTCRYA 490 500 510 520 530 540 IETAHKYLKN AAGNFYINDK CTGAVVGQQP FGGSRASGTN DKAGSSLNLL RWISARTIKE 550 NFVPLTSFTY PYMIDPEN

References

[1]

"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFI02000052 Genomic DNA. Translation: EAL65787.1.
RefSeq	XP_639145.1. XM_634053.1.
3D structure databases
HSSP	HSSP built from PDB template 2BJK based on UniProtKB Q5SI02.
ProteinModelPortal	Q54RA2.
ModBase	Search...
Protein-protein interaction databases
STRING	Q54RA2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0229934; DDB0229934; DDB_G0283293.
GeneID	8624016.
KEGG	ddi:DDB_G0283293.
Organism-specific databases
dictyBase	DDB_G0283293.
Phylogenomic databases
eggNOG	KOG2455.
GeneTree	EPrGT00050000005093.
HOGENOM	HBG752218.
OMA	CELVDFW.
PhylomeDB	Q54RA2.
ProtClustDB	CLSZ2430386.
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

AL4A1_DICDI

Accession

Primary (citable) accession number: Q54RA2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 2008
Last sequence update:	May 24, 2005
Last modified:	November 16, 2011
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)