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 03-AUG-2022, entry version 124.
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}.
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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 AlphaFoldDB; P94390; -.
DR SMR; P94390; -.
DR STRING; 224308.BSU03200; -.
DR PaxDb; P94390; -.
DR PRIDE; P94390; -.
DR EnsemblBacteria; CAB12114; CAB12114; BSU_03200.
DR GeneID; 938338; -.
DR KEGG; bsu:BSU03200; -.
DR PATRIC; fig|224308.43.peg.328; -.
DR eggNOG; COG0506; Bacteria.
DR InParanoid; P94390; -.
DR OMA; YPMIGSH; -.
DR PhylomeDB; P94390; -.
DR BioCyc; BSUB:BSU03200-MON; -.
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;
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 ACT_SITE 130
FT /evidence="ECO:0000250|UniProtKB:Q72IB8"
FT ACT_SITE 180
FT /evidence="ECO:0000250|UniProtKB:Q72IB8"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9RW55"
FT BINDING 131
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q72IB8"
FT BINDING 159
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q72IB8"
FT BINDING 183..185
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q72IB8"
FT BINDING 222..223
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q72IB8"
FT BINDING 284..285
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9RW55"
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
