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Reviewed, UniProtKB/Swiss-Prot P95629 (PUTA_RHIME)

Last modified June 16, 2009. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Bifunctional protein putA
Including the following 2 domains:
    1- Recommended name:
            Proline dehydrogenase
              EC=1.5.99.8
        Alternative name(s):
            Proline oxidase
    2- Recommended name:
            Delta-1-pyrroline-5-carboxylate dehydrogenase
                Short name=P5C dehydrogenase
              EC=1.5.1.12
Gene names
Name: putA
OrganismRhizobium meliloti (Sinorhizobium meliloti)
Taxonomic identifier382 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium

Protein attributes

Sequence length1224 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Oxidizes proline to glutamate for use as a carbon and nitrogen source, and also functions as a transcriptional repressor of its own gene.

Catalytic activity

L-proline + acceptor = (S)-1-pyrroline-5-carboxylate + reduced acceptor.

(S)-1-pyrroline-5-carboxylate + NAD(P)+ + 2 H2O = L-glutamate + NAD(P)H.

Cofactor

FAD.

Pathway

Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 1/2.

Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 2/2.

Sequence similarities

In the N-terminal section; belongs to the proline dehydrogenase family.

In the C-terminal section; belongs to the aldehyde dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12241224Bifunctional protein putA
PRO_0000056527

Regions

Region164 – 501338Proline dehydrogenase
Region576 – 1032457Aldehyde dehydrogenase

Sites

Active site8001 By similarity
Active site8341 By similarity

Sequences

Sequence LengthMass (Da)Tools
P95629-1 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: BEC655494FCE98D1

FASTA1,224131,191
        10         20         30         40         50         60 
MSPNPLQKPA IDAAPAPFAD FAPPVRPQST LRRAITAAYR RPETECLPPL VEAATQSKEI 

        70         80         90        100        110        120 
RDAAASTARK LIEALRGKHS GSGVEGLVQE YSLSSQEGVA LMCLAERPVR IPDTATRDAL 

       130        140        150        160        170        180 
IRDKIADGNW KSHLGRSRSL FVNAATWGLV VTGKLTSTVN DRTLAARVTR LISRCGEPVI 

       190        200        210        220        230        240 
RRGVDMAMRM MGEQFVTGET IEALKRSKEL EEKGFSYSYD MLRERPTAAD AERYYRDYES 

       250        260        270        280        290        300 
AIHATAKPRG RGIYEGPGIS IKLSALHPRY RQAARVMGEL LPRVKALALL AKNYDIGLNI 

       310        320        330        340        350        360 
DAEEADRLEL SLDLLEVLCL DGDLSGWNGM GFVVQAYGKR CPFVLDFIID LARRSGRRIM 

       370        380        390        400        410        420 
VRLVKGAYWD AEIKRAQLDG LADFPVFTRK IHTDVSYMPR TQAACRDRCG VPQFATHNAQ 

       430        440        450        460        470        480 
TLAAIYHMAG KDFHVGKYEF QCLHGMGEPL YEEVVGRGKL DRPCRIYAPV GTHETLLAYL 

       490        500        510        520        530        540 
VRRLLENGAN SSFVHRINDP KVSIDELIAD PVEVVRAMPV VGAKHDRIAL PAVLFGDART 

       550        560        570        580        590        600 
NSAGFDLSNE ETLASLTEAL RESAAMKWTA LPQFATGPAA GETRTVLNPG DHRDVVGSVT 

       610        620        630        640        650        660 
ETRKRTHGAP CACRRRGAGL GGRLAERAAC LDRAAELMQA RMPTLLGLII REAGKSALNA 

       670        680        690        700        710        720 
IAEVREAIDF LRYYAEQTRR TLGPATPLGP IVCISPWNFP LAIFTGQIAA ALVAGNPVLA 

       730        740        750        760        770        780 
KPAEETPLIA AEGVRILREA GIPASALQLL PGDGRVGAAL VAGRDAGVMF TGSTEVARLI 

       790        800        810        820        830        840 
QAQLADRLSP AGRPVPLIAE TGGQNAMIVD SSALAGQVVG DVITSAFDSA GQRCSALRVL 

       850        860        870        880        890        900 
CLQEDVAGPH PDDAEGRAAR HCISAAPIVF SVDVGPVITS EAKDNIEKHI ERMRGLGRKV 

       910        920        930        940        950        960 
EQIGLASETG VGTFVPPTII ELEKLSDLQR EVFGPVLHVI RYRRDDLDRL VDDVNATGYG 

       970        980        990       1000       1010       1020 
LTFGLHTRLD ETIAHVTSRI KAGNLYINRN IIGAVVGVQP FGGRGLSGTG PKAGGPLYLG 

      1030       1040       1050       1060       1070       1080 
RLVTTAPVPP QHSSVHTDPV LLDFAKWLDG KGARAEVEAA RNAGSSSALG LDLELPGPVG 

      1090       1100       1110       1120       1130       1140 
ERNLYTLHAR GRILLVPATE SGLYHQLAAA LATGNSVAID AASGLQASLK NLPQTVGLRV 

      1150       1160       1170       1180       1190       1200 
SWSKDWAADG PFAGALVEGD AERIRAVNKA IAALPGPLLL VQAASSGEIA RNPDAYCLNW 

      1210       1220 
LVEEVSASIN TAAAGGNASL MAIG 

« Hide

References

[1]"The Rhizobium meliloti putA gene: its role in the establishment of the symbiotic interaction with alfalfa."
Jimenez-Zurdo J.I., Garcia-Rodriguez F.M., Toro N.
Mol. Microbiol. 23:85-93(1997) [PubMed: 9004223] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: GR4.
[2]"Sinorhizobium meliloti putA gene regulation: a new model within the family rhizobiaceae."
Soto M.J., Jimenez-Zurdo J.I., van Dillewijn P., Toro N.
J. Bacteriol. 182:1935-1941(2000) [PubMed: 10715000] [Abstract]
Cited for: AUTOREGULATORY ROLE.

Cross-references

Sequence databases

Y08500 Genomic DNA. Translation: CAA69727.1.
PIRT43218.

3D structure databases

HSSPHSSP built from PDB template 1K87 based on UniProtKB P09546.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.5.1.12. 142.
1.5.99.8. 142.

Family and domain databases

InterProIPR016160. Ald_DH_CS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH.
IPR005933. d-1-pyrroline-5-COlate_DH-3.
IPR002872. Proline_DH.
[Graphical view]
Gene3DG3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
PANTHERPTHR11699. Aldehyde_dehyd. 1 hit.
PfamPF00171. Aldedh. 1 hit.
PF01619. Pro_dh. 1 hit.
[Graphical view]
TIGRFAMsTIGR01238. D1pyr5carbox3. 1 hit.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePUTA_RHIME
AccessionPrimary (citable) accession number: P95629
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1997
Last modified: June 16, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents