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UniProtKB/Swiss-Prot entry Q3AF39

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PROA_CARHZ
Primary accession number Q3AF39
Secondary accession numbers None
Integrated into Swiss-Prot on April 4, 2006
Sequence was last modified on November 22, 2005 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 22)
Name and origin of the protein
Protein name Gamma-glutamyl phosphate reductase
Synonyms GPR
EC 1.2.1.41
Glutamate-5-semialdehyde dehydrogenase
Glutamyl-gamma-semialdehyde dehydrogenase
GSA dehydrogenase
Gene name
Name: proA
OrderedLocusNames: CHY_0383
From
Carboxydothermus hydrogenoformans (strain Z-2901 / DSM 6008) [TaxID: 246194] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; Thermoanaerobacteraceae; Carboxydothermus.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1371/journal.pgen.0010065; PubMed=16311624 [NCBI, ExPASy, EBI, Israel, Japan]
Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J., Madupu R., Sullivan S.A., Kolonay J.F., Nelson W.C., Tallon L.J., Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B., Robb F.T., Eisen J.A.;
"Life in hot carbon monoxide: the complete genome sequence of Carboxydothermus hydrogenoformans Z-2901.";
PLoS Genet. 1:563-574(2005).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
CP000141; ABB13750.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_359245.1; -.
3D structure databases
ModBase Q3AF39.
Enzyme and pathway databases
BioCyc CHYD246194:CHY_0383-MON; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0004350; Molecular function: glutamate-5-semialdehyde dehydrogenase activity (inferred from electronic annotation from HAMAP).
GO:0006561; Biological process: proline biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00412; -; 1.
PBIL [Tree]
InterPro IPR016163; Ald_DHase_C.
IPR016162; Ald_DHase_N.
IPR015590; Aldehyde_DHase.
IPR000965; Gglut_pp_reduct.
IPR012134; Glu-5-SA_DHase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.309.10; Aldehyde_dehydrogenase_C; 1.
G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
PANTHER PTHR11063:SF1; GSA_DH; 1.
Pfam PF00171; Aldedh; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000151; GPR; 1.
TIGRFAMs TIGR00407; proA; 1.
PROSITE PS01223; PROA; 1.
BLOCKS Q3AF39.
Genome annotation databases
GeneID 3726908; -.
GenomeReviews CP000141_GR; CHY_0383.
KEGG chy:CHY_0383; -.
NMPDR fig|246194.3.peg.599; -.
TIGR CHY_0383; -.
Phylogenomic databases
HOGENOM Q3AF39; -.
Other
ProtoNet Q3AF39.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Complete proteome; Cytoplasm; NADP; Oxidoreductase; Proline biosynthesis.
Features
SEVIEWER logo Feature table viewer
KeyFrom To Length Description FTId
CHAIN   1   415  415     Gamma-glutamyl phosphate reductase. PRO_0000229996
Sequence information
Length: 415 AA [This is the length of the unprocessed precursor] Molecular weight: 45489 Da [This is the MW of the unprocessed precursor] CRC64: 2F0BED5AA870B69D [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MDEVLNLAKK AKEASKKLAQ LSTEQKNRAL LKIAQYLEEN MEKILTENQK DLAEAKKGGL 

        70         80         90        100        110        120 
SPAFIERLTL NEKRILDMAE GVRQVAKLPD PVGEVLGMTR RPNGLVIGQV RVPLGVVGII 

       130        140        150        160        170        180 
YESRPNVTVD AAALCLKAGN AVILRGGKEA FNSNLALVTL MEEALRSEEI PEGAVGMIKT 

       190        200        210        220        230        240 
TSRDAANYLM RLNGYLDVLI PRGGAGLIKT VVENSTVPVI ETGVGNCHVY VEEDADLEMA 

       250        260        270        280        290        300 
ERIIINAKCQ RPAVCNAMET LLVHEKIAPV FLPQIGKALK ENGVEIRGCE VTRRYIPDAL 

       310        320        330        340        350        360 
PATEEDYYTE FLDLILAVRV VRDLDEAIAH ITKYGSGHSE AIVTRDYFKA RRFTEEVDAA 

       370        380        390        400        410 
AVYVNASTRF TDGFEFGFGA EIGISTQKLH ARGPMGLKEL TTTKYVIYGT GQIRG
Q3AF39 in FASTA format

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