AL4A1_RAT
ID AL4A1_RAT Reviewed; 563 AA.
AC P0C2X9;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP PROTEIN SEQUENCE OF 79-89 AND 318-337, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
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; AABR03107656; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P0C2X9; -.
DR SMR; P0C2X9; -.
DR STRING; 10116.ENSRNOP00000062857; -.
DR iPTMnet; P0C2X9; -.
DR PhosphoSitePlus; P0C2X9; -.
DR SwissPalm; P0C2X9; -.
DR jPOST; P0C2X9; -.
DR PRIDE; P0C2X9; -.
DR UCSC; RGD:1624206; rat.
DR RGD; 1624206; Aldh4a1.
DR eggNOG; KOG1056; Eukaryota.
DR eggNOG; KOG2455; Eukaryota.
DR InParanoid; P0C2X9; -.
DR PhylomeDB; P0C2X9; -.
DR Reactome; R-RNO-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-RNO-70688; Proline catabolism.
DR SABIO-RK; P0C2X9; -.
DR UniPathway; UPA00261; UER00374.
DR PRO; PR:P0C2X9; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; ISO:RGD.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
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 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Mitochondrion; NAD; Oxidoreductase;
KW Phosphoprotein; Proline metabolism; Reference proteome; Transit peptide.
FT TRANSIT 1..23
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 24..563
FT /note="Delta-1-pyrroline-5-carboxylate dehydrogenase,
FT mitochondrial"
FT /id="PRO_0000287827"
FT ACT_SITE 313
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT ACT_SITE 347
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 207
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 285..289
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 446
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 512
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 210
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 30
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8CHT0"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30038"
FT MOD_RES 51
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8CHT0"
FT MOD_RES 92
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8CHT0"
FT MOD_RES 92
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8CHT0"
FT MOD_RES 98
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8CHT0"
FT MOD_RES 98
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8CHT0"
FT MOD_RES 113
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8CHT0"
FT MOD_RES 113
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8CHT0"
FT MOD_RES 129
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8CHT0"
FT MOD_RES 129
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8CHT0"
FT MOD_RES 174
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8CHT0"
FT MOD_RES 174
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8CHT0"
FT MOD_RES 317
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8CHT0"
FT MOD_RES 346
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8CHT0"
FT MOD_RES 364
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8CHT0"
FT MOD_RES 375
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8CHT0"
FT MOD_RES 394
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8CHT0"
FT MOD_RES 461
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8CHT0"
FT MOD_RES 508
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8CHT0"
FT MOD_RES 508
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8CHT0"
SQ SEQUENCE 563 AA; 61869 MW; AF19417D93825EA5 CRC64;
MLPPALLRRS LLSYAWRGSG LRWKHASSLK VANEPILAFT QGSPERDALQ KALNDLKDQT
EAIPCVVGDE EVWTSDVRYQ LSPFNHGHKV AKFCYADKAL LNKAIEAAVL ARKEWDLKPV
ADRAQIFLKA ADMLSGPRRA EILAKTMVGQ GKTVIQAEID AAAELIDFFR FNAKFAVELE
GEQPISVPPS TNHVVYRGLE GFVAAISPFN FTAIGGNLAG APALMGNVVL WKPSDTAMLA
SYAVYRILRE AGLPPNVIQF VPADGPTFGD TVTSSEHLCG INFTGSVPTF KHLWKQVAQN
LDRFRTFPRL AGECGGKNFH FVHSSADVDS VVSGTLRSAF EYGGQKCSAC SRLYVPQSLW
PQIKGRLLEE HSRIKVGNPA EDFGTFFSAV IDAKAFARIK KWLEHARSSP SLSILAGGQC
NESVGYFVEP CIIESKDPQE PIMKEEIFGP VLTVYVYPDE KYRETLQLVD STTSYGLTGA
VFAQDKTIVQ EATRMLRNAA GNFYINDKST GSVVGQQPFG GARASGERDI PGQPRLVQLW
TEPPFTPLAV SPPLGDWRYS YMQ
