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   16-JUN-2009, entry version 19.
DE   RecName: Full=Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial;
DE            Short=P5C dehydrogenase;
DE            EC=1.5.1.12;
DE   AltName: Full=Aldehyde dehydrogenase family 4 member A1;
DE   Flags: Precursor;
GN   Name=Aldh4a1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; 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.,
RA   Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
RA   Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
RA   Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
RA   Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
RA   Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
RA   Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
RA   Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
RA   Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
RA   D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
RA   Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
RA   Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
RA   Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
RA   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.,
RA   Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
RA   Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
RA   Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
RA   Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
RA   Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
RA   Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
RA   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.,
RA   Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
RA   Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
RA   Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
RA   Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
RA   Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
RA   Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
RA   Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
RA   Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
RA   Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
RA   Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
RA   Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
RA   Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
RA   Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
RA   Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into
RT   mammalian evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 79-89 AND 318-337, AND MASS 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-
CC       carboxylate (P5C), derived either from proline or ornithine, to
CC       glutamate. This is a necessary step in the pathway interconnecting
CC       the urea and tricarboxylic acid cycles. The preferred substrate is
CC       glutamic gamma-semialdehyde, other substrates include succinic,
CC       glutaric and adipic semialdehydes (By similarity).
CC   -!- CATALYTIC ACTIVITY: (S)-1-pyrroline-5-carboxylate + NAD(P)(+) + 2
CC       H(2)O = L-glutamate + NAD(P)H.
CC   -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC       glutamate; L-glutamate from L-proline: step 2/2.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
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DR   EMBL; AABR03107656; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00475676; -.
DR   UniGene; Rn.203318; -.
DR   Ensembl; ENSRNOG00000018608; Rattus norvegicus.
DR   BRENDA; 1.5.1.12; 248.
DR   ArrayExpress; P0C2X9; -.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase act...; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006561; P:proline biosynthetic process; IEA:InterPro.
DR   InterPro; IPR016160; Ald_DH_CS.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH.
DR   InterPro; IPR005931; d-1-pyrroline-5-COlate_DH-1.
DR   Gene3D; G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
DR   PANTHER; PTHR11699; Aldehyde_dehyd; 1.
DR   Pfam; PF00171; Aldedh; 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;
KW   Oxidoreductase; Phosphoprotein; Proline metabolism; Transit peptide.
FT   TRANSIT       1     23       Mitochondrion (By similarity).
FT   CHAIN        24    563       Delta-1-pyrroline-5-carboxylate
FT                                dehydrogenase, mitochondrial.
FT                                /FTId=PRO_0000287827.
FT   NP_BIND     295    300       NAD (By similarity).
FT   ACT_SITE    313    313       By similarity.
FT   ACT_SITE    347    347       By similarity.
FT   MOD_RES      98     98       N6-acetyllysine (By similarity).
FT   MOD_RES     113    113       N6-acetyllysine (By similarity).
FT   MOD_RES     401    401       N6-acetyllysine (By similarity).
FT   MOD_RES     504    504       Phosphotyrosine (By similarity).
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
//