ID D4DEH8_TRIVH Unreviewed; 665 AA.
AC D4DEH8;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
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};
DE Flags: Fragment;
GN ORFNames=TRV_05545 {ECO:0000313|EMBL:EFE39734.1};
OS Trichophyton verrucosum (strain HKI 0517).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663202 {ECO:0000313|EMBL:EFE39734.1, ECO:0000313|Proteomes:UP000008383};
RN [1] {ECO:0000313|Proteomes:UP000008383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HKI 0517 {ECO:0000313|Proteomes:UP000008383};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
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 -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFE39734.1}.
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DR EMBL; ACYE01000295; EFE39734.1; -; Genomic_DNA.
DR RefSeq; XP_003020352.1; XM_003020306.1.
DR AlphaFoldDB; D4DEH8; -.
DR GeneID; 9584102; -.
DR KEGG; tve:TRV_05545; -.
DR HOGENOM; CLU_005391_4_1_1; -.
DR OrthoDB; 4536at2759; -.
DR UniPathway; UPA00261; UER00374.
DR Proteomes; UP000008383; Unassembled WGS sequence.
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 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; PTHR42862; DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE 1, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR42862:SF1; DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE 2, ISOFORM A-RELATED; 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 46..513
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 287
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EFE39734.1"
SQ SEQUENCE 665 AA; 73392 MW; 8800A8C08674276C CRC64;
KHYAKGSPDR EQLACALEQF KKSAPLEVPV MIGGKAITTS PIQTQQNPSD HAVCVAKYHT
ASDEDIKAAI DNALEAKKKW EAMPFSDRAS IFLKAADLVG TKYRYEMMAA TMLGQGKNAW
QAEIDAAAEL CDFLSQFTTP PESGSKYPYY QNIMQIHSLT TYCSRVEYRP LEGFVYAISP
FNFSAIGGNL PAAPALMGNV VLWKPSPFAI ASNYLIYNIL AEAGLPAGVI QFVPGDAERI
TSLVLDNKHF SSLHFTGSTA VFRSLYGKIA QGVADGKYRS YPRIVGETGG KNFHLLHPSA
DTDNAAIHTV RGAFEFQGQK CSACSRAYVP QSKWESFRNK LVEETEKLKI GPPEDFTNFI
GPVIHEASFK KLAKVIDDAK NDKELTLLAG GKYDCSKGYF IHPTIYSTTN PEHHLLNTEL
FGPVLVILVY PDEAADAFEK ICETIDNTGA YGLTGAVFSQ DRAAVHYAEN ALRGTAGNFY
INCKCTGAVV GQQPFGGARA SGTNDKAGSA ALMGRFVNDA MEYDKLINYN TTLCPYDRAS
MLNVFVNQNL KDKGTYEMLS RIGVSFALFY LRSGYKKHAQ YLPRQREGKV NEDLEELKGK
CFFIIVSPKT KEKGAKLKKY WVVEGISNSQ LIMFCYHSVT NTDLPQNEHA GWGIIKQTRE
QRVGA
//
