(data stored in SCRATCH zone)

HOGENOM: SACD2_1_PE1009

ID   SACD2_1_PE1009                       STANDARD;      PRT;   373 AA.
AC   SACD2_1_PE1009; Q21M06;
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; Short=GK; (SACD2_1.PE1009).
GN   Name=proB; OrderedLocusNames=Sde_1011;
OS   SACCHAROPHAGUS DEGRADANS 2-40.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Saccharophagus.
OX   NCBI_TaxID=203122;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS SACD2_1.PE1009.
CC       Saccharophagus degradans 2-40 chromosome, complete genome.
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:PROB_SACD2
CC   -!- FUNCTION: Catalyzes the transfer of a phosphate group to glutamate
CC       to form glutamate 5-phosphate which rapidly cyclizes to 5-
CC       oxoproline.
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; Q21M06; -.
DR   EMBL; CP000282; ABD80273.1; -; Genomic_DNA.
DR   RefSeq; YP_526485.1; NC_007912.1.
DR   ProteinModelPortal; Q21M06; -.
DR   STRING; Q21M06; -.
DR   GeneID; 3965136; -.
DR   GenomeReviews; CP000282_GR; Sde_1011.
DR   KEGG; sde:Sde_1011; -.
DR   NMPDR; fig|203122.1.peg.3530; -.
DR   eggNOG; COG0263; -.
DR   OMA; TFGDNDM; -.
DR   PhylomeDB; Q21M06; -.
DR   ProtClustDB; PRK05429; -.
DR   BioCyc; SDEG203122:SDE_1011-MON; -.
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:EC.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0006561; P:proline biosynthetic process; IEA:UniProtKB-KW.
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; SACD2_1.PE1009; -.
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;
     MSKRQLVKQS RRWVIKIGSA LLTNNGRGLD REEMAVWVKQ MAALSKRGYE VVLVSSGAVA
     AGMTRLGWAE RPKALHELQA AAAVGQSSLI QAYEQEFQKY SIKTAQILLD HDDLSNRQRY
     LNARSTLRTL TKLGVIPIVN ENDTVVTDEI RFGDNDTLGA LVANLIEADT LCILTDQKAM
     FDSDPRQNAL AKMLIERSAF DPGLDAMAGD GGALGRGGMI SKVRAARLAA RSGANTIVVG
     GKVFDVIPRV ASGEILGTLL YSESQPIAAR KRWLAGNMQP RGRLTLDDGA VKVLREQGKS
     LLPVGVRAVE GYFTRGELVL CEDTAGREIA RGLVNYSSDE TNKIKGASSS RIDSLLGYKD
     YDELIHRDNL VLV
//

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