ALH13_CAEEL
ID ALH13_CAEEL Reviewed; 802 AA.
AC P54889; Q9BI69;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Probable delta-1-pyrroline-5-carboxylate synthase;
DE Short=P5CS;
DE Includes:
DE RecName: Full=Glutamate 5-kinase;
DE Short=GK;
DE EC=2.7.2.11;
DE AltName: Full=Gamma-glutamyl kinase;
DE Includes:
DE RecName: Full=Gamma-glutamyl phosphate reductase;
DE Short=GPR;
DE EC=1.2.1.41;
DE AltName: Full=Aldehyde dehydrogenase family 13;
DE AltName: Full=Glutamate-5-semialdehyde dehydrogenase;
DE AltName: Full=Glutamyl-gamma-semialdehyde dehydrogenase;
GN Name=alh-13; ORFNames=T22H6.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate = ADP + L-glutamyl 5-phosphate;
CC Xref=Rhea:RHEA:14877, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:58274, ChEBI:CHEBI:456216; EC=2.7.2.11;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + L-
CC glutamyl 5-phosphate + NADPH; Xref=Rhea:RHEA:19541,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58066, ChEBI:CHEBI:58274, ChEBI:CHEBI:58349; EC=1.2.1.41;
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC 5-semialdehyde from L-glutamate: step 1/2.
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC 5-semialdehyde from L-glutamate: step 2/2.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b;
CC IsoId=P54889-1; Sequence=Displayed;
CC Name=a;
CC IsoId=P54889-2; Sequence=VSP_047890;
CC -!- SIMILARITY: In the N-terminal section; belongs to the glutamate 5-
CC kinase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the gamma-glutamyl
CC phosphate reductase family. {ECO:0000305}.
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DR EMBL; Z50797; CAA90672.2; -; Genomic_DNA.
DR EMBL; Z50797; CAC35828.2; -; Genomic_DNA.
DR PIR; T25140; T25140.
DR RefSeq; NP_510132.2; NM_077731.4. [P54889-1]
DR RefSeq; NP_510133.2; NM_077732.6. [P54889-2]
DR AlphaFoldDB; P54889; -.
DR SMR; P54889; -.
DR BioGRID; 46321; 7.
DR STRING; 6239.T22H6.2b; -.
DR EPD; P54889; -.
DR PaxDb; P54889; -.
DR PeptideAtlas; P54889; -.
DR PRIDE; P54889; -.
DR EnsemblMetazoa; T22H6.2a.1; T22H6.2a.1; WBGene00011938. [P54889-2]
DR EnsemblMetazoa; T22H6.2b.1; T22H6.2b.1; WBGene00011938. [P54889-1]
DR GeneID; 181417; -.
DR KEGG; cel:CELE_T22H6.2; -.
DR UCSC; T22H6.2b; c. elegans.
DR CTD; 181417; -.
DR WormBase; T22H6.2a; CE47944; WBGene00011938; alh-13. [P54889-2]
DR WormBase; T22H6.2b; CE47964; WBGene00011938; alh-13. [P54889-1]
DR eggNOG; KOG1154; Eukaryota.
DR eggNOG; KOG4165; Eukaryota.
DR GeneTree; ENSGT00500000044903; -.
DR InParanoid; P54889; -.
DR OMA; EGRECIM; -.
DR OrthoDB; 832430at2759; -.
DR PhylomeDB; P54889; -.
DR Reactome; R-CEL-8964539; Glutamate and glutamine metabolism.
DR UniPathway; UPA00098; UER00359.
DR UniPathway; UPA00098; UER00360.
DR PRO; PR:P54889; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00011938; Expressed in embryo and 3 other tissues.
DR GO; GO:0005739; C:mitochondrion; HDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004349; F:glutamate 5-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004350; F:glutamate-5-semialdehyde dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd04256; AAK_P5CS_ProBA; 1.
DR CDD; cd07079; ALDH_F18-19_ProA-GPR; 1.
DR Gene3D; 3.40.1160.10; -; 1.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR HAMAP; MF_00412; ProA; 1.
DR HAMAP; MF_00456; ProB; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR020593; G-glutamylP_reductase_CS.
DR InterPro; IPR041744; G5K_ProBA.
DR InterPro; IPR001057; Glu/AcGlu_kinase.
DR InterPro; IPR005715; Glu_5kinase/COase_Synthase.
DR InterPro; IPR019797; Glutamate_5-kinase_CS.
DR InterPro; IPR000965; GPR_dom.
DR InterPro; IPR005766; P5_carboxy_syn.
DR Pfam; PF00696; AA_kinase; 1.
DR Pfam; PF00171; Aldedh; 1.
DR PIRSF; PIRSF036429; P5C_syn; 1.
DR PRINTS; PR00474; GLU5KINASE.
DR SUPFAM; SSF53633; SSF53633; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR TIGRFAMs; TIGR01092; P5CS; 1.
DR TIGRFAMs; TIGR00407; proA; 1.
DR TIGRFAMs; TIGR01027; proB; 1.
DR PROSITE; PS00902; GLUTAMATE_5_KINASE; 1.
DR PROSITE; PS01223; PROA; 1.
PE 3: Inferred from homology;
KW Alternative splicing; Amino-acid biosynthesis; ATP-binding; Kinase;
KW Multifunctional enzyme; NADP; Nucleotide-binding; Oxidoreductase;
KW Proline biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..802
FT /note="Probable delta-1-pyrroline-5-carboxylate synthase"
FT /id="PRO_0000109771"
FT REGION 1..354
FT /note="Glutamate 5-kinase"
FT REGION 355..802
FT /note="Gamma-glutamyl phosphate reductase"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 242
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 262..263
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 301..307
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT VAR_SEQ 61..62
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_047890"
SQ SEQUENCE 802 AA; 86694 MW; 9342768572E138E9 CRC64;
MFRATRCLRL PLRNSHINIL RPTQTELIKT RSSALAPYEK VSPITAVGAT PVGVGNGNYC
YSTKTRQKHP LINTRNDLKK AQRVVVKLGS AVITREDECG LALGRLASIV EQVSELQQSG
RQMLIVSSGA VAFGRQKLRQ ELVMSMSMRQ TLRGPSGMTA DKRACAASGM PGLMSLYEQL
FQQYGITVAQ VLLTKPDIDD DQRRKNLQAT IESLLSLNII PIVNANDAVA PDPKLNMHIS
DNDSLAARLS AEIEAELLII LSNVNGVYTG PPDLEGSRLL YTYVPSENSG VTFGANSKFG
TGGMESKVTA CVNALNNGVT TVITNGLAQD AITDAVAGKK IGTMFCNTKG YEGPPIEEVA
EKCRDAGRQL AALSNKERGA MVRHLAALLV DKEKYIIEAN QTDLANAKSA GLDPQLLNRL
KMTPEKIQDL HAGLNTIADS AETLVGRVLK KVKISEGLFL EQVTVPIGSL MVIFESRPDC
LPQVASLAMA SGNALLLKGG KEAEESNKAL HALVQEALGT HGFEMRDAVT LVRSREDVAD
LLQLKDLIDL IIPRGSSDLV RSMQEKSKGI PVLGHAEGVC HVYIDKDCDE QKAIQIVRDS
KCDYPSACNA AETILIHKDL ATAPFFDSLC SMFKAEGVKL HAGPKLAALL KFAPPPAESM
SFEYGSLECT LEVVDNVEEA VAHIIRYGSG HTESIITENT NTAEHFLKHV DSACAFHNAS
TRFADGYRFG LGAEVGISTG RIHARGPVGV EGLLTTKWLL RGEGHLVEDF KNGKYSYLHE
NLNPSEVYRA LDAAGELKKA TA
