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Q15MX1 (Q15MX1_PSEA6) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Gamma-glutamyl phosphate reductase 2 HAMAP MF_00412
Short name=GPR 2 HAMAP MF_00412
EC=1.2.1.41 HAMAP MF_00412
Alternative name(s):
Glutamate-5-semialdehyde dehydrogenase 2 HAMAP MF_00412
Glutamyl-gamma-semialdehyde dehydrogenase 2 HAMAP MF_00412
Gene names
Name:proA2 HAMAP MF_00412
Ordered Locus Names:Patl_4268
OrganismPseudoalteromonas atlantica (strain T6c / ATCC BAA-1087) [Complete proteome] [HAMAP] EMBL ABG42767.1
Taxonomic identifier342610 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Pseudoalteromonadaceae › Pseudoalteromonas

Protein attributes

Sequence length416 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the NADPH dependent reduction of L-gamma-glutamyl 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate By similarity. HAMAP MF_00412

Catalytic activity

L-glutamate 5-semialdehyde + phosphate + NADP+ = L-glutamyl 5-phosphate + NADPH. HAMAP MF_00412

Pathway

Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2. HAMAP MF_00412

Subcellular location

Cytoplasm By similarity HAMAP MF_00412.

Sequence similarities

Belongs to the gamma-glutamyl phosphate reductase family. HAMAP MF_00412

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Proline biosynthesis HAMAP MF_00412
   Cellular componentCytoplasm HAMAP MF_00412
   LigandNADP HAMAP MF_00412
   Molecular functionOxidoreductase HAMAP MF_00412 EMBL ABG42767.1
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processproline biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionNADP binding

Inferred from electronic annotation. Source: InterPro

glutamate-5-semialdehyde dehydrogenase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
Q15MX1 [UniParc].

Last modified July 25, 2006. Version 1.
Checksum: F517C5774DE24C1A

FASTA41645,168
        10         20         30         40         50         60 
MEFSIAQAAK AARIASRQVA KLSATQKETL LKDIAERMLG QTETIIVANE KDLAAGRDNN 

        70         80         90        100        110        120 
LDDAMLDRLL LTPQRIQGIA NAVFDIAAQA DPVGSIDHMQ QMPSGIQVGR MRIPLGVIAM 

       130        140        150        160        170        180 
IYESRPNVTI DAAALCLKAG NAVVLRGGKE ALHSNLALAA CISYALEKHE IDPAAVVVVP 

       190        200        210        220        230        240 
NPDRAVMNEL MTLNEDIDLI IPRGGEGLIR FVSENSRIPV IQHYKGVCHL YVDDAADENK 

       250        260        270        280        290        300 
ALNLLKNGKT QRTGVCNSLE TLLVHQDIAP TFMPKVKALF NEHKVKVHGC ERSLQYFDNA 

       310        320        330        340        350        360 
SLATQDDWHA EYLAMEIAVR IVDDFDTAIE HIETYSSGHT EVIATQDFSR AQQFIRTLNS 

       370        380        390        400        410 
AVVMANASSR FSDGGELGLG AEIGISTSKL HAYGPMGAES LTTQKFIVLG DGEVRG

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References

[1]"Complete sequence of Pseudoalteromonas atlantica T6c."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Karls A.C., Bartlett D., Higgins B.P., Richardson P.
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: T6c / ATCC BAA-1087.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000388 Genomic DNA. Translation: ABG42767.1.
RefSeqYP_663821.1. NC_008228.1.

3D structure databases

ProteinModelPortalQ15MX1.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ15MX1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4176058.
GenomeReviewsGene locus Patl_4268 in contig CP000388_GR.
KEGGpat:Patl_4268.
NMPDRfig|342610.3.peg.1020.
PATRIC23054004. VBIPseAtl25434_4542.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0014.
HOGENOMHBG318080.
OMAIEKIRVP.
PhylomeDBQ15MX1.
ProtClustDBPRK00197.

Enzyme and pathway databases

BioCycPATL342610:PATL_4268-MONOMER.

Family and domain databases

HAMAPMF_00412. ProA.
[Tree]
InterProIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR000965. G-glutamylP_reductase.
IPR020593. G-glutamylP_reductase_CS.
IPR012134. Glu-5-SA_DH.
[Graphical view]
Gene3DG3DSA:3.40.309.10. Aldehyde_dehydrogenase_C. 1 hit.
G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 2 hits.
KOK00147.
PANTHERPTHR11063:SF1. GSA_DH. 1 hit.
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
PIRSFPIRSF000151. GPR. 1 hit.
SUPFAMSSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
TIGRFAMsTIGR00407. ProA. 1 hit.
PROSITEPS01223. PROA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ15MX1_PSEA6
AccessionPrimary (citable) accession number: Q15MX1
Entry history
Integrated into UniProtKB/TrEMBL: July 25, 2006
Last sequence update: July 25, 2006
Last modified: December 14, 2011
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry info