(data stored in ACNUC7421 zone)

HOGENOM: DEHSV_1_PE1002

ID   DEHSV_1_PE1002                       STANDARD;      PRT;   373 AA.
AC   DEHSV_1_PE1002; D2BIN2;
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=Glutamate 5-kinase; EC=2.7.2 11;AltName:
DE   Full=Gamma-glutamyl kinase; (DEHSV_1.PE1002).
GN   Name=proB; OrderedLocusNames=DhcVS_1065;
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.PE1002.
CC       Dehalococcoides sp. VS chromosome, complete genome.
CC       / IFO 0083) chromosome G, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:D2BIN2_DEHSV
CC   -!- FUNCTION: Catalyzes the transfer of a phosphate group to glutamate
CC       to form glutamate 5-phosphate which rapidly cyclizes to 5-
CC       oxoproline (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamate = ADP + L-glutamate 5-
CC       phosphate.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-
CC       glutamate 5-semialdehyde from L-glutamate: step 1/2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the glutamate 5-kinase family.
CC   -!- SIMILARITY: Contains 1 PUA domain.
CC   -!- GENE_FAMILY: HOG000246368 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; D2BIN2; -.
DR   EMBL; CP001827; ACZ62182.1; -; Genomic_DNA.
DR   RefSeq; YP_003330510.1; NC_013552.1.
DR   ProteinModelPortal; D2BIN2; -.
DR   GeneID; 8657996; -.
DR   GenomeReviews; CP001827_GR; DhcVS_1065.
DR   KEGG; dev:DhcVS_1065; -.
DR   OMA; TFGDNDM; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004349; F:glutamate 5-kinase activity; IEA:HAMAP.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0006561; P:proline biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00456; ProB; 1; -.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR001057; Glu/AcGlu_kinase.
DR   InterPro; IPR011529; Glu_5kinase.
DR   InterPro; IPR005715; Glu_5kinase/COase_Synthase.
DR   InterPro; IPR019797; Glutamate_5-kinase_CS.
DR   InterPro; IPR002478; PUA.
DR   InterPro; IPR015947; PUA-like_domain.
DR   Gene3D; G3DSA:3.40.1160.10; Aa_kinase; 1.
DR   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF01472; PUA; 1.
DR   PIRSF; PIRSF000729; GK; 1.
DR   PRINTS; PR00474; GLU5KINASE.
DR   SMART; SM00359; PUA; 1.
DR   SUPFAM; SSF53633; Aa_kinase; 1.
DR   SUPFAM; SSF88697; PUA-like; 1.
DR   TIGRFAMs; TIGR01027; ProB; 1.
DR   PROSITE; PS00902; GLUTAMATE_5_KINASE; 1.
DR   PROSITE; PS50890; PUA; 1.
DR   HOGENOMDNA; DEHSV_1.PE1002; -.
KW   gamma-glutamyl kinase;
KW   Amino-acid biosynthesis; ATP-binding; Complete proteome; Cytoplasm;
KW   Kinase; Nucleotide-binding; Proline biosynthesis; Transferase.
SQ   SEQUENCE   373 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MNGNCYKRVV IKLGTSLLTG GTGKLDHERM ADLCRQIAEL TRLGTEIIIV SSGAIAAGRS
     KMGLRHILKD VPFKQVLAAI GQSQLMNYYD QLFSPYGLTI AQGLLTKNDL SDRSGYLNAR
     NTLLALMELG VITIVNENDV VAVDEIQQAK FGDNDNLSAM VANLIEADLL LILTNIRGLY
     TADPTLHPDA TLITEVKEIT EDLEHLAAGS SNKLGTGGMV TKLEAARLAT SSGVNVIIAD
     GHIPDIILKL ANGETEGTRF IPTLHKPDSR QRWMMSGLCT RGSICIDDGA AKALRENQKS
     LLAAGVQQAE GKFGRGDIVK LNDSRGKRLG YGITNYSSDD IAKIKGLHTN EINAVLEGNQ
     GPEIIHRNNL VVI
//

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