PROD1_BACSU
ID PROD1_BACSU Reviewed; 302 AA.
AC O32179;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Proline dehydrogenase 1;
DE Short=PRODH 1;
DE EC=1.5.5.2;
DE AltName: Full=Proline oxidase 1;
GN Name=fadM; Synonyms=yusM; OrderedLocusNames=BSU32850;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
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 [2]
RP GENE NAME, AND INDUCTION.
RC STRAIN=168;
RX PubMed=17189250; DOI=10.1074/jbc.m606831200;
RA Matsuoka H., Hirooka K., Fujita Y.;
RT "Organization and function of the YsiA regulon of Bacillus subtilis
RT involved in fatty acid degradation.";
RL J. Biol. Chem. 282:5180-5194(2007).
CC -!- FUNCTION: Converts proline to delta-1-pyrroline-5-carboxylate.
CC {ECO:0000250|UniProtKB:Q8RMG1}.
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 -!- 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 -!- INDUCTION: Repressed by FadR in the absence of LCFAs (fatty acids of
CC 14-20 carbon atoms). When LCFAs are present in the medium, they are
CC converted to long-chain acyl-CoAs, which antagonize fadR as to its
CC binding to fadR boxes on target DNA and thus derepress transcription.
CC {ECO:0000269|PubMed:17189250}.
CC -!- SIMILARITY: Belongs to the proline dehydrogenase family. {ECO:0000305}.
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DR EMBL; AL009126; CAB15274.1; -; Genomic_DNA.
DR PIR; F70021; F70021.
DR RefSeq; NP_391164.1; NC_000964.3.
DR RefSeq; WP_003228569.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O32179; -.
DR SMR; O32179; -.
DR STRING; 224308.BSU32850; -.
DR PaxDb; O32179; -.
DR PRIDE; O32179; -.
DR EnsemblBacteria; CAB15274; CAB15274; BSU_32850.
DR GeneID; 937064; -.
DR KEGG; bsu:BSU32850; -.
DR PATRIC; fig|224308.179.peg.3560; -.
DR eggNOG; COG0506; Bacteria.
DR InParanoid; O32179; -.
DR OMA; YKESAAV; -.
DR PhylomeDB; O32179; -.
DR BioCyc; BSUB:BSU32850-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; ISS:UniProtKB.
DR GO; GO:0006562; P:proline catabolic process; ISS: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 2: Evidence at transcript level;
KW FAD; Flavoprotein; Nucleotide-binding; Oxidoreductase; Proline metabolism;
KW Reference proteome.
FT CHAIN 1..302
FT /note="Proline dehydrogenase 1"
FT /id="PRO_0000360508"
FT ACT_SITE 129
FT /evidence="ECO:0000250|UniProtKB:Q72IB8"
FT ACT_SITE 179
FT /evidence="ECO:0000250|UniProtKB:Q72IB8"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9RW55"
FT BINDING 130
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q72IB8"
FT BINDING 158
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q72IB8"
FT BINDING 182..184
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q72IB8"
FT BINDING 221..222
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q72IB8"
FT BINDING 283..284
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9RW55"
FT SITE 270
FT /note="Critical for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q72IB8"
SQ SEQUENCE 302 AA; 34452 MW; 7606141E776B4A2B CRC64;
MLRHVFLFLS QNKTLTKFAK AYGTRLGARR FVAGDTIESA VKTVKRLNRS GLCATIDYLG
EYAASEKEAN QVAEECKKAI QAIAEHQLNS ELSLKLTSIG LDLSEELALT HLRAILSVAK
QYDVAVTIDM EDYSHYEQTL SIYRQCKQEF EKLGTVIQAY LYRAAEDIRK MRDLKPNLRL
VKGAYKESAA VAFPDKRGTD LHFQSLIKLQ LLSGNYTAVA THDDDIIAFT KQLVAEHQIP
ASQFEFQMLY GIRPERQKEL AKEGYRMRVY VPYGTDWFSY FMRRIAERPA NAAFVLKGIL
KK
