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Protein

1-pyrroline-5-carboxylate dehydrogenase 2

Gene

putC

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Important for the use of proline as a sole carbon and energy source or a sole nitrogen source.1 Publication

Catalytic activityi

L-glutamate 5-semialdehyde + NAD+ + H2O = L-glutamate + NADH.UniRule annotation

Pathwayi: L-proline degradation into L-glutamate

This protein is involved in step 2 of the subpathway that synthesizes L-glutamate from L-proline.UniRule annotation1 Publication
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Proline dehydrogenase 2 (putB), Proline dehydrogenase 1 (fadM)
  2. 1-pyrroline-5-carboxylate dehydrogenase (rocA), 1-pyrroline-5-carboxylate dehydrogenase 2 (putC)
This subpathway is part of the pathway L-proline degradation into L-glutamate, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-glutamate from L-proline, the pathway L-proline degradation into L-glutamate and in Amino-acid degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei286 – 2861UniRule annotation
Active sitei320 – 3201UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciBSUB:BSU03210-MONOMER.
UniPathwayiUPA00261; UER00374.

Names & Taxonomyi

Protein namesi
Recommended name:
1-pyrroline-5-carboxylate dehydrogenase 2Curated (EC:1.2.1.88UniRule annotation)
Short name:
P5C dehydrogenase 2Curated
Alternative name(s):
L-glutamate gamma-semialdehyde dehydrogenaseUniRule annotation
Gene namesi
Name:putC1 Publication
Synonyms:ycgN
Ordered Locus Names:BSU03210
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Pathology & Biotechi

Disruption phenotypei

Deletion of the putBCP operon abolishes L-proline utilization.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 5155151-pyrroline-5-carboxylate dehydrogenase 2PRO_0000056512Add
BLAST

Proteomic databases

PaxDbiP94391.

Expressioni

Inductioni

The expression of the putBCP operon is induced in a PutR-dependent fashion by very low concentrations of L-proline in the growth medium. CodY represses the operon by displacing PutR from DNA.3 Publications

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100001793.

Structurei

3D structure databases

ProteinModelPortaliP94391.
SMRiP94391. Positions 1-515.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family. RocA subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C26. Bacteria.
COG1012. LUCA.
HOGENOMiHOG000271511.
InParanoidiP94391.
KOiK00294.
OMAiRYDYIPL.
OrthoDBiEOG6BS8QW.
PhylomeDBiP94391.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
HAMAPiMF_00733. RocA.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS_CYS.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR005932. RocA.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR01237. D1pyr5carbox2. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P94391-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTPYKHEPF TNFQDQNNVE AFKKALATVS EYLGKDYPLV INGERVETEA
60 70 80 90 100
KIVSINPADK EEVVGRVSKA SQEHAEQAIQ AAAKAFEEWR YTSPEERAAV
110 120 130 140 150
LFRAAAKVRR RKHEFSALLV KEAGKPWNEA DADTAEAIDF MEYYARQMIE
160 170 180 190 200
LAKGKPVNSR EGEKNQYVYT PTGVTVVIPP WNFLFAIMAG TTVAPIVTGN
210 220 230 240 250
TVVLKPASAT PVIAAKFVEV LEESGLPKGV VNFVPGSGAE VGDYLVDHPK
260 270 280 290 300
TSLITFTGSR EVGTRIFERA AKVQPGQQHL KRVIAEMGGK DTVVVDEDAD
310 320 330 340 350
IELAAQSIFT SAFGFAGQKC SAGSRAVVHE KVYDQVLERV IEITESKVTA
360 370 380 390 400
KPDSADVYMG PVIDQGSYDK IMSYIEIGKQ EGRLVSGGTG DDSKGYFIKP
410 420 430 440 450
TIFADLDPKA RLMQEEIFGP VVAFCKVSDF DEALEVANNT EYGLTGAVIT
460 470 480 490 500
NNRKHIERAK QEFHVGNLYF NRNCTGAIVG YHPFGGFKMS GTDSKAGGPD
510
YLALHMQAKT ISEMF
Length:515
Mass (Da):56,424
Last modified:June 16, 2009 - v2
Checksum:i937CAAFF1F97A009
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 181N → Y in BAA08955 (PubMed:8969502).Curated
Sequence conflicti239 – 2391A → S in BAA08955 (PubMed:8969502).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50453 Genomic DNA. Translation: BAA08955.1.
AL009126 Genomic DNA. Translation: CAB12115.2.
PIRiA69759.
RefSeqiNP_388203.2. NC_000964.3.
WP_003234655.1. NZ_JNCM01000030.1.

Genome annotation databases

EnsemblBacteriaiCAB12115; CAB12115; BSU03210.
GeneIDi938333.
KEGGibsu:BSU03210.
PATRICi18972201. VBIBacSub10457_0329.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50453 Genomic DNA. Translation: BAA08955.1.
AL009126 Genomic DNA. Translation: CAB12115.2.
PIRiA69759.
RefSeqiNP_388203.2. NC_000964.3.
WP_003234655.1. NZ_JNCM01000030.1.

3D structure databases

ProteinModelPortaliP94391.
SMRiP94391. Positions 1-515.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100001793.

Proteomic databases

PaxDbiP94391.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12115; CAB12115; BSU03210.
GeneIDi938333.
KEGGibsu:BSU03210.
PATRICi18972201. VBIBacSub10457_0329.

Phylogenomic databases

eggNOGiENOG4105C26. Bacteria.
COG1012. LUCA.
HOGENOMiHOG000271511.
InParanoidiP94391.
KOiK00294.
OMAiRYDYIPL.
OrthoDBiEOG6BS8QW.
PhylomeDBiP94391.

Enzyme and pathway databases

UniPathwayiUPA00261; UER00374.
BioCyciBSUB:BSU03210-MONOMER.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
HAMAPiMF_00733. RocA.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS_CYS.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR005932. RocA.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR01237. D1pyr5carbox2. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome: determination of the sequence of a 146 kb segment and identification of 113 genes."
    Yamane K., Kumano M., Kurita K.
    Microbiology 142:3047-3056(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  2. "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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  3. "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
    Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
    Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO 18 AND 239.
  4. "Indirect repression by Bacillus subtilis CodY via displacement of the activator of the proline utilization operon."
    Belitsky B.R.
    J. Mol. Biol. 413:321-336(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  5. "PrcR, a PucR-type transcriptional activator, is essential for proline utilization and mediates proline-responsive expression of the proline utilization operon putBCP in Bacillus subtilis."
    Huang S.C., Lin T.H., Shaw G.C.
    Microbiology 157:3370-3377(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
    Strain: 168.
  6. Cited for: FUNCTION, PATHWAY, INDUCTION, DISRUPTION PHENOTYPE.
    Strain: 168 / JH642.

Entry informationi

Entry nameiROCA2_BACSU
AccessioniPrimary (citable) accession number: P94391
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: June 16, 2009
Last modified: February 17, 2016
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.