ID A0A0V1HQY6_9BILA Unreviewed; 1039 AA.
AC A0A0V1HQY6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00012884};
DE EC=1.2.1.88 {ECO:0000256|ARBA:ARBA00012884};
DE AltName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00032259};
GN Name=aldh4a1 {ECO:0000313|EMBL:KRZ12921.1};
GN ORFNames=T11_10601 {ECO:0000313|EMBL:KRZ12921.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ12921.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ12921.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ12921.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC glutamate; L-glutamate from L-proline: step 2/2.
CC {ECO:0000256|ARBA:ARBA00004786}.
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:KRZ12921.1}.
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DR EMBL; JYDP01000036; KRZ12920.1; -; Genomic_DNA.
DR EMBL; JYDP01000036; KRZ12921.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1HQY6; -.
DR UniPathway; UPA00261; UER00374.
DR Proteomes; UP000055024; Unassembled WGS sequence.
DR GO; GO:0016593; C:Cdc73/Paf1 complex; IEA:InterPro.
DR GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0010133; P:proline catabolic process to glutamate; IEA:UniProtKB-UniPathway.
DR GO; GO:0006368; P:transcription elongation by RNA polymerase II; IEA:InterPro.
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 InterPro; IPR007133; RNA_pol_II-assoc_Paf1.
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 Pfam; PF03985; Paf1; 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};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003345};
KW Proline metabolism {ECO:0000256|ARBA:ARBA00023062};
KW Reference proteome {ECO:0000313|Proteomes:UP000055024}.
FT DOMAIN 560..1017
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 791
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 1039 AA; 117724 MW; 24D9DFB8979CF2BE CRC64;
MSAVNKNNLH QPGTSSSRSV NSTSRNEVRY DIPFQPMYSN TLPDVPFEAK FLPHPFPADR
HVKYETTMME RAYTGELVTE DDVGIFIDLV LIDKYEPNPN EPVELHPTDE LLCSDEDALS
STMKKSRHGG KAVPWMRRTE YISTDYSRFG VQTERQETKL GYHIQKVLKE ASLYRDRESQ
LTAINKTFED AKKPVREHFS KRGVYAMEEL PLFPDFDAWK YPFAQVIFDV DPAPRDKTSL
EETLAADQIC RAMIRGMMDE KGEQFVAYFV PTLETIRKLK SVEGKDISEI DLSTTFDFKL
LREYNWSVKN KASVGYEENH FFSFRDGRAY YNELETRVRL NRRRVKDGHV HSAVPNSRLI
VRYRDLNDQE LAALSARSMV VNPLEEEDDD EDEAEAEKHA DDTAAEKKLD TDPSKLPPAK
DNNQWSDNEV KSEEGSPVVE EETEEEIESL LLFFKLYFKE ALKTGKSCSL FYLVMTPMFN
PMKKLISGSR FALGTFFRTL TSAEFLKTPQ NEPVLSYAPG SDERIQLDQA IARLTKQVNN
IHAVIGNEMF DCGFTGEQRM PFDHKTMLAR VAVCDKNLIR KAIDVALDSR LAWERMPLEK
RAEIFFKAAD LASTKYRMDL NAATMLGQGK TVVQAEIDAA CELIDFWRFN AYYALQLEKV
RLISSKDIQN ELLLRGLQGF VAAISPFNFT AIGSNMSSCP ALMGNVVLWK PARTAVLSNY
ISFKILREAG LPDGVINFIP SKSETFGEVV LPSKHLAGVG FVGSLPVFQH IWKVVGNNVE
NYYNFPRLSG ECGGKNFHFI HPSADFKTAV ACTARAAFEY QGQKCSACSR LYLPQSMWPE
FKDALIEICK EIKIGDPRDY SVFMSAVIDR PAFENICSYI EHAKSSPSLK ILYGGDYDDE
KGYFIHPTLL LCSDPNDRIM KEEIFGPVLT VITYPDPHCN EVLASIKDST EYALTGAIFA
QDMNFVKQAR MDLREACGNF YVNDKCTGAV VGQQPFGGSR KSGTNDKAGG PYYVLKWVSH
LAVKSTLTPI HEWKYPSMG
//
