AL4A1_DICDI
ID AL4A1_DICDI Reviewed; 558 AA.
AC Q54RA2;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial;
DE Short=P5C dehydrogenase;
DE EC=1.2.1.88;
DE AltName: Full=Aldehyde dehydrogenase family 4 member A1 homolog;
DE AltName: Full=L-glutamate gamma-semialdehyde dehydrogenase;
DE Flags: Precursor;
GN ORFNames=DDB_G0283293;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Irreversible conversion of delta-1-pyrroline-5-carboxylate
CC (P5C), derived either from proline or ornithine, to glutamate. This is
CC a necessary step in the pathway interconnecting the urea and
CC tricarboxylic acid cycles (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamate 5-semialdehyde + NAD(+) = 2 H(+) + L-
CC glutamate + NADH; Xref=Rhea:RHEA:30235, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58066; EC=1.2.1.88;
CC -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC glutamate; L-glutamate from L-proline: step 2/2.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000052; EAL65787.1; -; Genomic_DNA.
DR RefSeq; XP_639145.1; XM_634053.1.
DR AlphaFoldDB; Q54RA2; -.
DR SMR; Q54RA2; -.
DR STRING; 44689.DDB0229934; -.
DR PaxDb; Q54RA2; -.
DR EnsemblProtists; EAL65787; EAL65787; DDB_G0283293.
DR GeneID; 8624016; -.
DR KEGG; ddi:DDB_G0283293; -.
DR dictyBase; DDB_G0283293; -.
DR eggNOG; KOG2455; Eukaryota.
DR HOGENOM; CLU_005391_4_1_1; -.
DR InParanoid; Q54RA2; -.
DR OMA; FAGIHFT; -.
DR PhylomeDB; Q54RA2; -.
DR UniPathway; UPA00261; UER00374.
DR PRO; PR:Q54RA2; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0010133; P:proline catabolic process to glutamate; IBA:GO_Central.
DR CDD; cd07123; ALDH_F4-17_P5CDH; 1.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR005931; P5CDH/ALDH4A1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR TIGRFAMs; TIGR01236; D1pyr5carbox1; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW Mitochondrion; NAD; Oxidoreductase; Proline metabolism; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..558
FT /note="Delta-1-pyrroline-5-carboxylate dehydrogenase,
FT mitochondrial"
FT /id="PRO_0000342183"
FT ACT_SITE 306
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT ACT_SITE 340
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 198
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 223
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 276..280
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 438
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 201
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 558 AA; 61633 MW; 6F6ACCB3479EB1AA CRC64;
MLRNTSRVLM SHFARANIPT PVNQPMLNYE VGSTHRKLLK EACAKFRNTT IDIPCVVGGK
EIRTGDVQKQ LICSDHNKVL ATFHQANAEL LKLAVENSME SKAQWESLPF EARSAVFLKA
ADLLNTKYRY DVLASTMLGQ GKTVWQAEID AAAEGIDFLR FNVKYAQEIY QQQPPANSAG
CWNILTYQPL EGYVVAISPF NFTAIGLNLS SAPALMGNVV LWKPASTAVL SNWIVYKALL
EAGLPAGVIQ FLPGSGRLVG EHLFNNRNFS GLHFTGSTGV FNDIYKKTAD NLVAGVYKGY
PRIVGETGGK DFHFLHNSGD VENFVNNTLR GAFEYQGQKC SACSRAYIPQ SLWPQIKDRL
VTGVKSMKMG QSDDFSSFVS AVIDKNSFNN IQSYIEHAKA SPDAEIIVGG KCDSSVGWFV
EPTIILAKDP HYKSMEEEIF GPVLTIYVYE DSKFEETLKI CDETSPYALT GSIFSTCRYA
IETAHKYLKN AAGNFYINDK CTGAVVGQQP FGGSRASGTN DKAGSSLNLL RWISARTIKE
NFVPLTSFTY PYMIDPEN
