ID   AL4A1_DANRE             Reviewed;         556 AA.
AC   Q7SY23;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 110.
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;
DE   AltName: Full=L-glutamate gamma-semialdehyde dehydrogenase;
DE   Flags: Precursor;
GN   Name=aldh4a1; ORFNames=zgc:63592;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=SJD;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
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; BC055155; AAH55155.1; -; mRNA.
DR   RefSeq; NP_957452.1; NM_201158.1.
DR   AlphaFoldDB; Q7SY23; -.
DR   SMR; Q7SY23; -.
DR   STRING; 7955.ENSDARP00000055709; -.
DR   PaxDb; Q7SY23; -.
DR   PRIDE; Q7SY23; -.
DR   GeneID; 394133; -.
DR   KEGG; dre:394133; -.
DR   CTD; 8659; -.
DR   ZFIN; ZDB-GENE-040426-1179; aldh4a1.
DR   eggNOG; KOG2455; Eukaryota.
DR   InParanoid; Q7SY23; -.
DR   OrthoDB; 454791at2759; -.
DR   PhylomeDB; Q7SY23; -.
DR   Reactome; R-DRE-389661; Glyoxylate metabolism and glycine degradation.
DR   Reactome; R-DRE-70688; Proline catabolism.
DR   UniPathway; UPA00261; UER00374.
DR   PRO; PR:Q7SY23; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-UniPathway.
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; IPR029510; Ald_DH_CS_GLU.
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   2: Evidence at transcript level;
KW   Mitochondrion; NAD; Oxidoreductase; Proline metabolism; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..17
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           18..556
FT                   /note="Delta-1-pyrroline-5-carboxylate dehydrogenase,
FT                   mitochondrial"
FT                   /id="PRO_0000007175"
FT   ACT_SITE        307
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008"
FT   ACT_SITE        341
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008"
FT   BINDING         226
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         279..283
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         440
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         506
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            204
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   556 AA;  61587 MW;  E7973E9787CEA358 CRC64;
     MLRARSAVSQ SWKGFKTFSC VAVEVKNEPV LEFKEGSKER AELEEALRNL KGKTEEIPCV
     IGNEEVWTKD IRFQLSPFNH SHQVAKFCYA DKDLLNKAIE ASVAARREWD LKPVSDRAQI
     FFKAADIISG PKRAEVLAKT MIGQGKTVVQ AEIDAAPELI DFFRFNAKHA IELEDQQPLD
     SDGSTNTMLY RGLEGFVAAV APFNFTAIGG NLAGTPALMG NVVLWKPSDT AMSASYAVYK
     ILRESGLPPN IIQFVPADGP VFGDTVTSSE HLAGINFTGS VPTFKRLWKQ VAQNLDIYKN
     FPRVAGECGG KNFHFVHKSA DVRSVVTGTI RSAFEYGGQK CSACSRMYVP DSLWPQIRQG
     LLDVYKQIKV GDPVEDFSTF FSAVIDDKSF SRIKGWLEHA RSSPHLKIIA GGNCDDKKGY
     FVEPTIIETT DPQEKIMNEE IFGPVLTVYV YPENDYKKVL HLIDNTSPYA LTGAIFPQDK
     SVIEEAGKAL RNAAGNYYIN DKSTGSIVAQ QPFGGARASG TNDKPGGPHY VLRWTSPQVV
     KQTHVPLTEW KYPYMS