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Reviewed, UniProtKB/Swiss-Prot O32179 (PROD1_BACSU)

Last modified November 3, 2009. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
    Proline dehydrogenase 1
      Short name=PRODH 1
    EC=1.5.99.8
Alternative name(s):
    Proline oxidase 1
Gene names
Name: fadM
Synonyms: yusM
Ordered Locus Names: BSU32850
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length302 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Catalyzes the oxidation of L-proline to delta-1-pyrroline-5-carboxylate (P5C) By similarity.

Catalytic activity

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

Cofactor

FAD By similarity.

Pathway

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

Induction

Repressed by fadR in the absence of LCFAs (fatty acids of 14-20 carbon atoms). When LCFAs are present in the medium, they are converted to long-chain acyl-CoAs, which antagonize fadR as to its binding to fadR boxes on target DNA and thus derepress transcription. Ref.2

Sequence similarities

Belongs to the proline dehydrogenase family.

Ontologies

Keywords
   Biological processProline metabolism
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processglutamate biosynthetic process

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

proline catabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionproline dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 302302Proline dehydrogenase 1
PRO_0000360508

Sequences

Sequence LengthMass (Da)Tools
O32179-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 7606141E776B4A2B

FASTA30234,452
        10         20         30         40         50         60 
MLRHVFLFLS QNKTLTKFAK AYGTRLGARR FVAGDTIESA VKTVKRLNRS GLCATIDYLG 

        70         80         90        100        110        120 
EYAASEKEAN QVAEECKKAI QAIAEHQLNS ELSLKLTSIG LDLSEELALT HLRAILSVAK 

       130        140        150        160        170        180 
QYDVAVTIDM EDYSHYEQTL SIYRQCKQEF EKLGTVIQAY LYRAAEDIRK MRDLKPNLRL 

       190        200        210        220        230        240 
VKGAYKESAA VAFPDKRGTD LHFQSLIKLQ LLSGNYTAVA THDDDIIAFT KQLVAEHQIP 

       250        260        270        280        290        300 
ASQFEFQMLY GIRPERQKEL AKEGYRMRVY VPYGTDWFSY FMRRIAERPA NAAFVLKGIL 


KK 

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[2]"Organization and function of the YsiA regulon of Bacillus subtilis involved in fatty acid degradation."
Matsuoka H., Hirooka K., Fujita Y.
J. Biol. Chem. 282:5180-5194(2007) [PubMed: 17189250] [Abstract]
Cited for: GENE NAME, INDUCTION.
Strain: 168.

Cross-references

Sequence databases

AL009126 Genomic DNA. Translation: CAB15274.1.
PIRF70021.
RefSeqNP_391164.1.

3D structure databases

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

Genome annotation databases

GeneID937064.
GenomeReviewsGene locus BSU32850 in contig AL009126_GR.
KEGGbsu:BSU32850.
NMPDRfig|224308.1.peg.3290.

Organism-specific databases

SubtiListBG14025. fadM. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMO32179.
OMAVAFPDKR.

Enzyme and pathway databases

BioCycBSUB224308:BSU3281-MON.

Family and domain databases

InterProIPR015590. Aldehyde_DH.
IPR002872. Proline_DH.
IPR008219. Proline_DH_pred.
[Graphical view]
PANTHERPTHR11699. Aldehyde_dehyd. 1 hit.
PfamPF01619. Pro_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000196. Pro_dehydrog. 1 hit.
ProtoNetSearch...

Entry information

Entry namePROD1_BACSU
AccessionPrimary (citable) accession number: O32179
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: January 1, 1998
Last modified: November 3, 2009
This is version 48 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

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

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