(data stored in ACNUC7421 zone)

SWISSPROT: PROA_ANADE

ID   PROA_ANADE              Reviewed;         427 AA.
AC   Q2IMG0;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   08-MAY-2019, entry version 91.
DE   RecName: Full=Gamma-glutamyl phosphate reductase {ECO:0000255|HAMAP-Rule:MF_00412};
DE            Short=GPR {ECO:0000255|HAMAP-Rule:MF_00412};
DE            EC=1.2.1.41 {ECO:0000255|HAMAP-Rule:MF_00412};
DE   AltName: Full=Glutamate-5-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00412};
DE   AltName: Full=Glutamyl-gamma-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00412};
DE            Short=GSA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00412};
GN   Name=proA {ECO:0000255|HAMAP-Rule:MF_00412};
GN   OrderedLocusNames=Adeh_0212;
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of L-glutamate
CC       5-phosphate into L-glutamate 5-semialdehyde and phosphate. The
CC       product spontaneously undergoes cyclization to form 1-pyrroline-5-
CC       carboxylate. {ECO:0000255|HAMAP-Rule:MF_00412}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) +
CC         L-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;
CC         EC=1.2.1.41; Evidence={ECO:0000255|HAMAP-Rule:MF_00412};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-
CC       glutamate 5-semialdehyde from L-glutamate: step 2/2.
CC       {ECO:0000255|HAMAP-Rule:MF_00412}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00412}.
CC   -!- SIMILARITY: Belongs to the gamma-glutamyl phosphate reductase
CC       family. {ECO:0000255|HAMAP-Rule:MF_00412}.
DR   EMBL; CP000251; ABC79989.1; -; Genomic_DNA.
DR   RefSeq; WP_011419272.1; NC_007760.1.
DR   SMR; Q2IMG0; -.
DR   STRING; 290397.Adeh_0212; -.
DR   EnsemblBacteria; ABC79989; ABC79989; Adeh_0212.
DR   KEGG; ade:Adeh_0212; -.
DR   eggNOG; ENOG4105C2S; Bacteria.
DR   eggNOG; COG0014; LUCA.
DR   HOGENOM; HOG000246356; -.
DR   KO; K00147; -.
DR   OMA; CNAIETL; -.
DR   BioCyc; ADEH290397:G1G5W-219-MONOMER; -.
DR   UniPathway; UPA00098; UER00360.
DR   Proteomes; UP000001935; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004350; F:glutamate-5-semialdehyde dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd07079; ALDH_F18-19_ProA-GPR; 1.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 1.
DR   HAMAP; MF_00412; ProA; 1.
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; IPR020593; G-glutamylP_reductase_CS.
DR   InterPro; IPR012134; Glu-5-SA_DH.
DR   InterPro; IPR000965; GPR_dom.
DR   Pfam; PF00171; Aldedh; 1.
DR   PIRSF; PIRSF000151; GPR; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   TIGRFAMs; TIGR00407; proA; 1.
DR   PROSITE; PS01223; PROA; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q2IMG0.
DR   SWISS-2DPAGE; Q2IMG0.
KW   Amino-acid biosynthesis; Complete proteome; Cytoplasm; NADP;
KW   Oxidoreductase; Proline biosynthesis; Reference proteome.
FT   CHAIN         1    427       Gamma-glutamyl phosphate reductase.
FT                                /FTId=PRO_0000252563.
SQ   SEQUENCE   427 AA;  45377 MW;  EA1F4626CCDB8EEB CRC64;
     MRKEKSLGLA AEMRKLAEAS REAARALSHA DPRRKDAALR AAAEAIGRRE RRILSENARD
     VAAARAAGQN AAYLDRLKLD PKRLAGIAAS LREIAGLRDP VGEVTASWRR PNGLEIRKVR
     IPLGVVLMVY EARPNVTVDA AALCLKSGNA AILRPGSDAL RSSLALAEAF AEGLEKAGLP
     AASAQVVPTP DREATYELLA LDDLIDLAIP RGGPSLIRAV AERSRVPVLK HYQGVCHLYL
     DASAPPQQAV DLALNGKVQR PGVCNATECL LVHRAAAGKL LPPVGRALAD AGVELRCDPT
     ALTILKRAGV AAVPARPDDF GKEFLDKILA VRVVADLDGA LDHIARYGSL HTEAIVTRDL
     ASARRFQREV DASAVMVNAS TRFNDGGELG LGAEIGISTT KLHAFGPMGL AELTTQKFLV
     EGEGHVR
//

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