ID D4B2V2_ARTBC Unreviewed; 656 AA.
AC D4B2V2;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
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};
GN ORFNames=ARB_02785 {ECO:0000313|EMBL:EFE30413.1};
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331 {ECO:0000313|EMBL:EFE30413.1, ECO:0000313|Proteomes:UP000008866};
RN [1] {ECO:0000313|Proteomes:UP000008866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371 {ECO:0000313|Proteomes:UP000008866};
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:EFE30413.1}.
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DR EMBL; ABSU01000030; EFE30413.1; -; Genomic_DNA.
DR RefSeq; XP_003011053.1; XM_003011007.1.
DR AlphaFoldDB; D4B2V2; -.
DR STRING; 663331.D4B2V2; -.
DR GeneID; 9525170; -.
DR KEGG; abe:ARB_02785; -.
DR eggNOG; KOG2455; Eukaryota.
DR HOGENOM; CLU_005391_4_1_1; -.
DR OMA; WNRFDHR; -.
DR OrthoDB; 4536at2759; -.
DR UniPathway; UPA00261; UER00374.
DR Proteomes; UP000008866; 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 CDD; cd07123; ALDH_F4-17_P5CDH; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000008866}.
FT DOMAIN 168..639
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 404
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 656 AA; 71439 MW; 5499E8D52712144D CRC64;
MYLFYSFLRS KKKVLGVAAS FAGQIGSKSI GAREAELFLL SCPGVFSLSI SQLSCYLASI
CPKPASNNLS YRIQETSNEE QRAKLPSDHV FIAALPLGSS GPGPSAVGRQ RHPIQSSVQL
QGTHHRQRTQ CKNPIDLGDA ALESLKASLP VQVPYHFKDS SSATADVQRN PSAHAETVAK
YFNATEADVS RMIEDALKAK PAWESLPFAD RASVFLKAAD LVAGKYRYEI MAATMLGQGK
NAWQAEIDAA AELADFLRFN VQYAEELYAQ QPEHHAPGVW NRSEYRPLEG FVYAISPFNF
TAIGGNLAGA PALMGNVVLW KPSPHAVYAN YLTHKILLEA GLPKDVIQFV PGDAQMVTKV
ALAHRDFAGL HYTGSTAVFR ELYGKIGQGI AAGTYRSYPR VVGETGGKNF HLIHSSADIH
SAAINTVRGA FEFQGQKCSA TSRVYVPQSR WTEFRDILVR ETEKLKMGPP EEFANFIGPV
IHEASFDKLA GVIDAAKQDS GVKLLAGGNH DKKQGYYVQP TVLQVSDAEH ELMKKEFFGP
VLAVYVYDDA AGESAFREMC SLIDRTTDYG LTGAVFAQDR NVLRLAEDAL RHSAGNFYLN
VKSTGAVVGQ QAFGGARASG TNDKAGSANL LTRFVNIRSI KEDFLGCSEV EYPSNK
//
