PUT2_EMENI
ID PUT2_EMENI Reviewed; 572 AA.
AC Q9P8I0; C8VP34; Q5BCJ7;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial;
DE Short=P5C dehydrogenase;
DE EC=1.2.1.88;
DE AltName: Full=L-glutamate gamma-semialdehyde dehydrogenase;
DE Flags: Precursor;
GN Name=prnC; ORFNames=AN1733;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Demais S., Gavrias V., Scazzocchio C.;
RT "Primary structure of the nuclear prnC gene involved in the mitochondrial
RT pathway for proline utilization in Aspergillus nidulans.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AF252630; AAF72527.1; -; Genomic_DNA.
DR EMBL; AACD01000027; EAA64019.1; -; Genomic_DNA.
DR EMBL; BN001307; CBF85458.1; -; Genomic_DNA.
DR RefSeq; XP_659337.1; XM_654245.1.
DR AlphaFoldDB; Q9P8I0; -.
DR SMR; Q9P8I0; -.
DR STRING; 162425.CADANIAP00008378; -.
DR EnsemblFungi; CBF85458; CBF85458; ANIA_01733.
DR EnsemblFungi; EAA64019; EAA64019; AN1733.2.
DR GeneID; 2875278; -.
DR KEGG; ani:AN1733.2; -.
DR VEuPathDB; FungiDB:AN1733; -.
DR eggNOG; KOG2455; Eukaryota.
DR HOGENOM; CLU_005391_4_1_1; -.
DR InParanoid; Q9P8I0; -.
DR OMA; FAGIHFT; -.
DR OrthoDB; 454791at2759; -.
DR UniPathway; UPA00261; UER00374.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
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:0034198; P:cellular response to amino acid starvation; IEP:AspGD.
DR GO; GO:0010133; P:proline catabolic process to glutamate; IBA:GO_Central.
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 3: Inferred from homology;
KW Mitochondrion; NAD; Oxidoreductase; Proline metabolism; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..572
FT /note="Delta-1-pyrroline-5-carboxylate dehydrogenase,
FT mitochondrial"
FT /id="PRO_0000007176"
FT ACT_SITE 320
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT ACT_SITE 354
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 300..305
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 215
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CONFLICT 149
FT /note="L -> V (in Ref. 1; AAF72527)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 572 AA; 61936 MW; 249FBB3461A9C3DD CRC64;
MQSSMLLRVR ALPKTASVLS RTKTATYATY KVPRIDNEPN KHYAAGSPDR KALQEALART
QRNAPLSVPL VIAGKEVKSS SSLTQSNPAS HGPVATYSNA TAKDVQAAIE SALEARKSWA
STPFADRASV FLKAADLIST KYRYDVMALT MHGQGKNAWQ AEIDSAAELC DFFRFGVKYA
EDLYAQQPVH HAPGVWNRVE YRPLEGFVYA ISPFNFTAIG GNLAGAPALM GNVVVWKPSP
SAIASNWLVH QILLEAGLPK NVIQFVPGEA EEVTKTVLDH PDFAALHFTG STNVFRNLYG
QISTRVAAGK YRSYPRIVGE TGGKNFHLIH KSADIRNAAV QTVRGAFEYQ GQKCSATSRV
YVASSIADSF LEQVASEAKS LKVGPPSDFT NFCGPVIHEA SFTKLAKVID EAKNDPELEL
LAGGSYDSSK GWYIQPTVYR TTNPDHPLLT RELFGPILVV YAYPDATEAD FARIAQKIDA
TGEYGLTGSV FAQDREALAV ANDVLRNAAG NFYINCKSTG AVVGQQPFGG ARASGTNDKA
GSGNLLSRFV SLRSIKEEFV PTYKVAYPSN EA
