ID D2PX19_KRIFD Unreviewed; 309 AA.
AC D2PX19;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=proline dehydrogenase {ECO:0000256|ARBA:ARBA00012695};
DE EC=1.5.5.2 {ECO:0000256|ARBA:ARBA00012695};
GN OrderedLocusNames=Kfla_6401 {ECO:0000313|EMBL:ADB35399.1};
OS Kribbella flavida (strain DSM 17836 / JCM 10339 / NBRC 14399).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Kribbellaceae; Kribbella.
OX NCBI_TaxID=479435 {ECO:0000313|EMBL:ADB35399.1, ECO:0000313|Proteomes:UP000007967};
RN [1] {ECO:0000313|Proteomes:UP000007967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17836 / JCM 10339 / NBRC 14399
RC {ECO:0000313|Proteomes:UP000007967};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M.,
RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA Pukall R., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Kribbella flavida DSM 17836.";
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADB35399.1, ECO:0000313|Proteomes:UP000007967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17836 / JCM 10339 / NBRC 14399
RC {ECO:0000313|Proteomes:UP000007967};
RX PubMed=21304701;
RA Pukall R., Lapidus A., Glavina Del Rio T., Copeland A., Tice H.,
RA Cheng J.-F., Lucas S., Chen F., Nolan M., LaButti K., Pati A., Ivanova N.,
RA Mavrommatis K., Mikhailova N., Pitluck S., Bruce D., Goodwin L., Land M.,
RA Hauser L., Chang Y.-J., Jeffries C.D., Chen A., Palaniappan K., Chain P.,
RA Rohde M., Goeker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.-P., Brettin T.;
RT "Complete genome sequence of Kribbella flavida type strain (IFO 14399).";
RL Stand. Genomic Sci. 2:186-193(2010).
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:0000256|ARBA:ARBA00000978};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000196-2};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000196-2};
CC -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC glutamate; L-glutamate from L-proline: step 1/2.
CC {ECO:0000256|ARBA:ARBA00004739}.
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DR EMBL; CP001736; ADB35399.1; -; Genomic_DNA.
DR RefSeq; WP_012923951.1; NC_013729.1.
DR AlphaFoldDB; D2PX19; -.
DR STRING; 479435.Kfla_6401; -.
DR KEGG; kfl:Kfla_6401; -.
DR eggNOG; COG0506; Bacteria.
DR HOGENOM; CLU_061158_0_1_11; -.
DR OrthoDB; 9773461at2; -.
DR UniPathway; UPA00261; UER00373.
DR Proteomes; UP000007967; Chromosome.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0004657; F:proline dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0010133; P:proline catabolic process to glutamate; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.220; -; 1.
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:SF0; PROLINE DEHYDROGENASE 1, MITOCHONDRIAL; 1.
DR PANTHER; PTHR13914; PROLINE OXIDASE; 1.
DR Pfam; PF01619; Pro_dh; 1.
DR PIRSF; PIRSF000196; Pro_dehydrog; 1.
DR SUPFAM; SSF51730; FAD-linked oxidoreductase; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|PIRSR:PIRSR000196-2};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000196-2};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000196-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000007967}.
FT DOMAIN 45..302
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000196-1"
FT BINDING 136
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000196-2"
FT BINDING 164
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000196-2"
FT BINDING 188..190
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000196-2"
FT BINDING 202
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000196-2"
FT BINDING 227..228
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000196-2"
FT BINDING 289
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000196-1"
FT BINDING 290
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000196-1"
SQ SEQUENCE 309 AA; 33555 MW; EBF9CC0ACED1FB4B CRC64;
MLRRVLLGVS RSPQIKNAVS SLPVSSGIVA RFVAGETAPE AVLATEKLVS NGLNVTLDHL
GEDTTDLATA SATADAYVEL LKQLAAAGLT QHAEVSVKLS AVGQALPGDG EKIALENART
ICLAARNAGT TVTLDMEDHT TTDSTLGILH ELRKDFPETG AVLQAYLRRT EADCVDLAYA
GSRVRLCKGA YKEPESVAFQ NKQAVDKAYV RAMKVLMNGD GYPMIASHDP RLIAIAGSLA
ARANRSRDSF EYQMLYGIRP EEQLRLAREG NTVRVYIPYG ADWYGYLVRR LAERPANLQF
FARSLISKK
//
