AL4A1_BOVIN
ID AL4A1_BOVIN Reviewed; 563 AA.
AC A7YWE4;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 93.
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAR-2007) 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. The preferred substrate is glutamic gamma-
CC semialdehyde, other substrates include succinic, glutaric and adipic
CC semialdehydes (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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; BC134524; AAI34525.1; -; mRNA.
DR RefSeq; NP_001099116.1; NM_001105646.1.
DR AlphaFoldDB; A7YWE4; -.
DR SMR; A7YWE4; -.
DR STRING; 9913.ENSBTAP00000020285; -.
DR PaxDb; A7YWE4; -.
DR PeptideAtlas; A7YWE4; -.
DR PRIDE; A7YWE4; -.
DR Ensembl; ENSBTAT00000020285; ENSBTAP00000020285; ENSBTAG00000030335.
DR GeneID; 100126042; -.
DR KEGG; bta:100126042; -.
DR CTD; 8659; -.
DR VEuPathDB; HostDB:ENSBTAG00000030335; -.
DR VGNC; VGNC:25815; ALDH4A1.
DR eggNOG; KOG2455; Eukaryota.
DR GeneTree; ENSGT00560000077335; -.
DR HOGENOM; CLU_005391_4_1_1; -.
DR InParanoid; A7YWE4; -.
DR OrthoDB; 454791at2759; -.
DR TreeFam; TF300481; -.
DR SABIO-RK; A7YWE4; -.
DR UniPathway; UPA00261; UER00374.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000030335; Expressed in cortex of kidney and 106 other tissues.
DR ExpressionAtlas; A7YWE4; baseline and differential.
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 Acetylation; Mitochondrion; NAD; Oxidoreductase; Phosphoprotein;
KW Proline metabolism; Reference proteome; Transit peptide.
FT TRANSIT 1..24
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 25..563
FT /note="Delta-1-pyrroline-5-carboxylate dehydrogenase,
FT mitochondrial"
FT /id="PRO_0000342182"
FT ACT_SITE 314
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT ACT_SITE 348
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 208
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 286..290
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 447
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 513
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 211
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30038"
FT MOD_RES 52
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8CHT0"
FT MOD_RES 93
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8CHT0"
FT MOD_RES 93
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8CHT0"
FT MOD_RES 99
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8CHT0"
FT MOD_RES 99
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8CHT0"
FT MOD_RES 114
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8CHT0"
FT MOD_RES 114
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8CHT0"
FT MOD_RES 130
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8CHT0"
FT MOD_RES 130
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8CHT0"
FT MOD_RES 175
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8CHT0"
FT MOD_RES 175
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8CHT0"
FT MOD_RES 318
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8CHT0"
FT MOD_RES 347
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8CHT0"
FT MOD_RES 365
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8CHT0"
FT MOD_RES 376
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8CHT0"
FT MOD_RES 395
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8CHT0"
FT MOD_RES 509
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8CHT0"
FT MOD_RES 509
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8CHT0"
FT MOD_RES 531
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8CHT0"
SQ SEQUENCE 563 AA; 61495 MW; E45B568B4844FEF0 CRC64;
MLLRSAALCR ALLARRGRAA GLCRRCVSSL QVANEPVLAF TQGSPERDAL QKALKELKGR
TEAIPCVVGD EEVWTSDVRY QASPFNHGHK VAKFCYADKA LLHRAIGAAL AARKEWDLKP
VADRAQVFLK AADLLSGPRR AEVLAKTMVG QGKTVIQAEI DAAAELIDFF RFNAKFAMEL
EGEQPLSVPP STNSMLYRGL EGFVAAISPF NFTAIGGNLA GAPALMGNVV LWKPSDTAML
ASYAVYRILR EAGLPPNIIQ FVPADGPTFG DTVTSSEHLC GINFTGSVPT FKHLWKQVAQ
NLDRFRTFPR LAGECGGKNF HFVHRSADVD SVVSGTLRSA FEYGGQKCSA CSRLYAPRSL
WPQIKGRLLE ELGGIKVGNP AEDFGTFFSA VIDAKSFGRI RKWLEHARSS PSLTILAGGH
CDDSVGYFVE PCIVETKDPQ DPIMKEEIFG PVLAVYVYPD EEYKETLRLV DSTTSYGLTG
AVFAQDKDVL REATELLRHA AGNFYINDKS TGSVVGQQPF GGARASGTND KPGGPHYVLR
WTSPQVIKET HGPLGDWRYP YMQ
