(data stored in ACNUC7421 zone)

HOGENOM: DEHSV_1_PE1008

ID   DEHSV_1_PE1008                       STANDARD;      PRT;   425 AA.
AC   DEHSV_1_PE1008; D2BIN8;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Gamma-glutamyl phosphate reductase; Short=GPR; EC=1.2.1
DE   41;AltName: Full=Glutamate-5-semialdehyde dehydrogenase;AltName:
DE   Full=Glutamyl-gamma-semialdehyde dehydrogenase; (DEHSV_1.PE1008).
GN   Name=proA; OrderedLocusNames=DhcVS_1071;
OS   DEHALOCOCCOIDES SP. VS.
OC   Bacteria; Chloroflexi; Dehalococcoidetes; Dehalococcoides.
OX   NCBI_TaxID=311424;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS DEHSV_1.PE1008.
CC       Dehalococcoides sp. VS chromosome, complete genome.
CC       / IFO 0083) chromosome G, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:D2BIN8_DEHSV
CC   -!- FUNCTION: Catalyzes the NADPH dependent reduction of L-gamma-
CC       glutamyl 5-phosphate into L-glutamate 5-semialdehyde and
CC       phosphate. The product spontaneously undergoes cyclization to form
CC       1-pyrroline-5-carboxylate (By similarity).
CC   -!- CATALYTIC ACTIVITY: L-glutamate 5-semialdehyde + phosphate +
CC       NADP(+) = L-glutamyl 5-phosphate + NADPH.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-
CC       glutamate 5-semialdehyde from L-glutamate: step 2/2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the gamma-glutamyl phosphate reductase
CC       family.
CC   -!- GENE_FAMILY: HOG000246356 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; D2BIN8; -.
DR   EMBL; CP001827; ACZ62188.1; -; Genomic_DNA.
DR   RefSeq; YP_003330516.1; NC_013552.1.
DR   ProteinModelPortal; D2BIN8; -.
DR   GeneID; 8658002; -.
DR   GenomeReviews; CP001827_GR; DhcVS_1071.
DR   KEGG; dev:DhcVS_1071; -.
DR   OMA; QYPAACN; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004350; F:glutamate-5-semialdehyde dehydrogenase activity; IEA:HAMAP.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0006561; P:proline biosynthetic process; IEA:HAMAP.
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; IPR000965; G-glutamylP_reductase.
DR   InterPro; IPR020593; G-glutamylP_reductase_CS.
DR   InterPro; IPR012134; Glu-5-SA_DH.
DR   Gene3D; G3DSA:3.40.309.10; Aldehyde_dehydrogenase_C; 1.
DR   Gene3D; G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 2.
DR   PANTHER; PTHR11063:SF1; GSA_DH; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   PIRSF; PIRSF000151; GPR; 1.
DR   SUPFAM; SSF53720; Aldehyde_DH/Histidinol_DH; 1.
DR   TIGRFAMs; TIGR00407; ProA; 1.
DR   PROSITE; PS01223; PROA; 1.
DR   HOGENOMDNA; DEHSV_1.PE1008; -.
KW   gamma-glutamyl phosphate reductase;
KW   Amino-acid biosynthesis; Complete proteome; Cytoplasm; NADP;
KW   Oxidoreductase; Proline biosynthesis.
SQ   SEQUENCE   425 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MMEKALLEIE EKARLARAAS RPLSYTSSAQ KDATLKNIAA CLLNNAPAIL EANLKDQTEA
     KAAGMTAAML DRLIINQSRL EGIAKDTLAI AALPDPVGEV FDMNTMPNGL VIGKKRVPLG
     VIAAIYESRP NVTVDIAALC LKAGNAVILR GGKETIHSNT ILARLIRQAV ADAGLPKEAI
     QFIENTDRSL VNHLLKLSEQ IDLVIPRGGA GLISYVKQNS FIPVVAGGIG VVHVYVDADA
     KIADAVNIAY NSKVQRPTVC NAMDTLLVHK DIASTFLPAV AAEWSKAGVE IRADKTAMEI
     LENTFGCKLI PATADDWGKE FLALVAAVKV VDSLDEALSH IAKYGSGHTE SIVTQNYTSS
     QRFLNEVDAA AVMVNASTRF TDGSQFGLGA ELGISTQKMH ARGPMGLKEI TSYKWIVYGN
     GQIRG
//

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