(data stored in SCRATCH zone)

SWISSPROT: PROD2_BACSU

ID   PROD2_BACSU             Reviewed;         303 AA.
AC   P94390; Q797Q5;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   11-DEC-2019, entry version 115.
DE   RecName: Full=Proline dehydrogenase 2 {ECO:0000305};
DE            Short=PRODH 2 {ECO:0000305};
DE            EC=1.5.5.2 {ECO:0000269|PubMed:22139509};
DE   AltName: Full=Proline oxidase 2 {ECO:0000305};
GN   Name=putB {ECO:0000303|PubMed:22139509}; Synonyms=ycgM;
GN   OrderedLocusNames=BSU03200;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8969502; DOI=10.1099/13500872-142-11-3047;
RA   Yamane K., Kumano M., Kurita K.;
RT   "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome:
RT   determination of the sequence of a 146 kb segment and identification of 113
RT   genes.";
RL   Microbiology 142:3047-3056(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   INDUCTION.
RX   PubMed=21840319; DOI=10.1016/j.jmb.2011.08.003;
RA   Belitsky B.R.;
RT   "Indirect repression by Bacillus subtilis CodY via displacement of the
RT   activator of the proline utilization operon.";
RL   J. Mol. Biol. 413:321-336(2011).
RN   [4]
RP   INDUCTION.
RC   STRAIN=168;
RX   PubMed=21964733; DOI=10.1099/mic.0.054197-0;
RA   Huang S.C., Lin T.H., Shaw G.C.;
RT   "PrcR, a PucR-type transcriptional activator, is essential for proline
RT   utilization and mediates proline-responsive expression of the proline
RT   utilization operon putBCP in Bacillus subtilis.";
RL   Microbiology 157:3370-3377(2011).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168 / JH642;
RX   PubMed=22139509; DOI=10.1128/jb.06380-11;
RA   Moses S., Sinner T., Zaprasis A., Stoeveken N., Hoffmann T., Belitsky B.R.,
RA   Sonenshein A.L., Bremer E.;
RT   "Proline utilization by Bacillus subtilis: uptake and catabolism.";
RL   J. Bacteriol. 194:745-758(2012).
CC   -!- FUNCTION: Converts proline to delta-1-pyrroline-5-carboxylate.
CC       Important for the use of proline as a sole carbon and energy source or
CC       a sole nitrogen source. {ECO:0000269|PubMed:22139509}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + L-proline = (S)-1-pyrroline-5-carboxylate + a
CC         quinol + H(+); Xref=Rhea:RHEA:23784, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17388, ChEBI:CHEBI:24646, ChEBI:CHEBI:60039,
CC         ChEBI:CHEBI:132124; EC=1.5.5.2;
CC         Evidence={ECO:0000269|PubMed:22139509};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC       glutamate; L-glutamate from L-proline: step 1/2.
CC       {ECO:0000269|PubMed:22139509}.
CC   -!- INDUCTION: The expression of the putBCP operon is induced in a PutR-
CC       dependent fashion by very low concentrations of L-proline in the growth
CC       medium. CodY represses the operon by displacing PutR from DNA.
CC       {ECO:0000269|PubMed:21840319, ECO:0000269|PubMed:21964733,
CC       ECO:0000269|PubMed:22139509}.
CC   -!- DISRUPTION PHENOTYPE: Deletion of the putBCP operon abolishes L-proline
CC       utilization. {ECO:0000269|PubMed:22139509}.
CC   -!- SIMILARITY: Belongs to the proline dehydrogenase family. {ECO:0000305}.
DR   EMBL; D50453; BAA08954.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12114.1; -; Genomic_DNA.
DR   PIR; H69758; H69758.
DR   RefSeq; NP_388202.1; NC_000964.3.
DR   RefSeq; WP_003246421.1; NZ_JNCM01000030.1.
DR   SMR; P94390; -.
DR   STRING; 224308.BSU03200; -.
DR   PaxDb; P94390; -.
DR   PRIDE; P94390; -.
DR   EnsemblBacteria; CAB12114; CAB12114; BSU03200.
DR   GeneID; 938338; -.
DR   KEGG; bsu:BSU03200; -.
DR   PATRIC; fig|224308.43.peg.328; -.
DR   eggNOG; COG0506; LUCA.
DR   HOGENOM; HOG000019712; -.
DR   InParanoid; P94390; -.
DR   KO; K00318; -.
DR   OMA; EYEFQML; -.
DR   PhylomeDB; P94390; -.
DR   BioCyc; BSUB:BSU03200-MONOMER; -.
DR   UniPathway; UPA00261; UER00373.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0071949; F:FAD binding; ISS:UniProtKB.
DR   GO; GO:0004657; F:proline dehydrogenase activity; IDA:UniProtKB.
DR   GO; GO:0006562; P:proline catabolic process; IDA:UniProtKB.
DR   GO; GO:0010133; P:proline catabolic process to glutamate; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR029041; FAD-linked_oxidoreductase-like.
DR   InterPro; IPR008219; PRODH_bac_arc.
DR   InterPro; IPR002872; Proline_DH_dom.
DR   InterPro; IPR015659; Proline_oxidase.
DR   PANTHER; PTHR13914; PTHR13914; 2.
DR   Pfam; PF01619; Pro_dh; 1.
DR   PIRSF; PIRSF000196; Pro_dehydrog; 1.
DR   SUPFAM; SSF51730; SSF51730; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P94390.
DR   SWISS-2DPAGE; P94390.
KW   FAD; Flavoprotein; Nucleotide-binding; Oxidoreductase; Proline metabolism;
KW   Reference proteome.
FT   CHAIN           1..303
FT                   /note="Proline dehydrogenase 2"
FT                   /id="PRO_0000361669"
FT   NP_BIND         183..185
FT                   /note="FAD"
FT                   /evidence="ECO:0000250|UniProtKB:Q72IB8"
FT   NP_BIND         222..223
FT                   /note="FAD"
FT                   /evidence="ECO:0000250|UniProtKB:Q72IB8"
FT   REGION          284..285
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q9RW55"
FT   ACT_SITE        130
FT                   /evidence="ECO:0000250|UniProtKB:Q72IB8"
FT   ACT_SITE        180
FT                   /evidence="ECO:0000250|UniProtKB:Q72IB8"
FT   BINDING         96
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9RW55"
FT   BINDING         131
FT                   /note="FAD; via amide nitrogen and carbonyl oxygen"
FT                   /evidence="ECO:0000250|UniProtKB:Q72IB8"
FT   BINDING         159
FT                   /note="FAD"
FT                   /evidence="ECO:0000250|UniProtKB:Q72IB8"
FT   SITE            271
FT                   /note="Critical for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q72IB8"
SQ   SEQUENCE   303 AA;  35046 MW;  D2FBAD6E05947B97 CRC64;
     MITRDFFLFL SKSGFLNKMA RNWGSRVAAG KIIGGNDFNS SIPTIRQLNS QGLSVTVDHL
     GEFVNSAEVA RERTEECIQT IATIADQELN SHVSLKMTSL GLDIDMDLVY ENMTKILQTA
     EKHKIMVTID MEDEVRCQKT LDIFKDFRKK YEHVSTVLQA YLYRTEKDID DLDSLNPFLR
     LVKGAYKESE KVAFPEKSDV DENYKKIIRK QLLNGHYTAI ATHDDKMIDF TKQLAKEHGI
     ANDKFEFQML YGMRSQTQLS LVKEGYNMRV YLPYGEDWYG YFMRRLAERP SNIAFAFKGM
     TKK
//

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