ID A0A3B4ENF6_PYGNA Unreviewed; 556 AA.
AC A0A3B4ENF6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|RuleBase:RU366016, ECO:0000256|RuleBase:RU366030};
DE Includes:
DE RecName: Full=Delta-1-pyrroline-5-carboxylate dehydrogenase {ECO:0000256|RuleBase:RU366030};
DE Short=P5C dehydrogenase {ECO:0000256|RuleBase:RU366030};
DE AltName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000256|RuleBase:RU366030};
DE Includes:
DE RecName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000256|RuleBase:RU366016};
DE EC=1.2.1.88 {ECO:0000256|RuleBase:RU366016};
OS Pygocentrus nattereri (Red-bellied piranha).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Pygocentrus.
OX NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000036711.1, ECO:0000313|Proteomes:UP000261440};
RN [1] {ECO:0000313|Ensembl:ENSPNAP00000036711.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 Evidence={ECO:0000256|ARBA:ARBA00001468,
CC ECO:0000256|RuleBase:RU366016};
CC -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC glutamate; L-glutamate from L-proline: step 2/2.
CC {ECO:0000256|ARBA:ARBA00004786, ECO:0000256|RuleBase:RU366016}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|ARBA:ARBA00004305}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}.
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DR RefSeq; XP_017560380.1; XM_017704891.1.
DR AlphaFoldDB; A0A3B4ENF6; -.
DR STRING; 42514.ENSPNAP00000036711; -.
DR Ensembl; ENSPNAT00000040230.1; ENSPNAP00000036711.1; ENSPNAG00000027764.1.
DR GeneID; 108431622; -.
DR CTD; 8659; -.
DR GeneTree; ENSGT00560000077335; -.
DR OMA; FAGIHFT; -.
DR OrthoDB; 4536at2759; -.
DR UniPathway; UPA00261; UER00374.
DR Proteomes; UP000261440; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0010133; P:proline catabolic process to glutamate; IEA:UniProtKB-UniRule.
DR CDD; cd07123; ALDH_F4-17_P5CDH; 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 NCBIfam; TIGR01236; D1pyr5carbox1; 1.
DR PANTHER; PTHR14516; 1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE FAMILY MEMBER; 1.
DR PANTHER; PTHR14516:SF3; DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU366016};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003345};
KW Proline metabolism {ECO:0000256|ARBA:ARBA00023062,
KW ECO:0000256|RuleBase:RU366016}.
FT DOMAIN 75..539
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 307
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 556 AA; 61176 MW; CA5F67B58150E335 CRC64;
MLRVRAALGQ SWRGFKTFPY AAVEVKNEPI LGFKEGSKER AELEKALQDL KGKTEEIPCV
IGDEQVWTKD IRYQLSPFNH SHKVAKFCYA DKELLNKAIL ASVAARREWD LKPVADRAQI
LFKAADAISG PKRAEVLAKT MIGQGKTVVQ AEIDAAAELI DFFRFNAKHA IELEQQQPLD
SDGSTNTMLY RGLEGFVAAV APFNFTAIGG NLAGTPTLMG NVVLWKPSDT AMSASYAVYK
ILRESGLPPN IIQFVPADGP VFGDTVTSSE HLAGINFTGS VPTFKRLWKQ VAQNLDIYRN
FPRVAGECGG KNFHFVHKSA DVHSVVTGTI RSAFEYGGQK CSACSRMYVP DSLWPQIKQD
LLAIHKQIIL GDPVEDFGTF FSAVIDDKSF ARIKGWLSHA KASPSLTVIA GGNCDDKKGY
YVEPTIIETK DPQDKIMNEE IFGPVLTVYV YPENDYKKVL ELIDSTSPYA LTGAVFSQDK
AVVAEAAKLL RNAAGNYYVN DKSTGSVVAQ QPFGGSRASG TNDKPGGPHY ILRWTSPQVV
KETHVPLTEW KYPYMG
//
