PRODH_DEIRA
ID PRODH_DEIRA Reviewed; 310 AA.
AC Q9RW55;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Proline dehydrogenase {ECO:0000303|PubMed:23151026, ECO:0000312|EMBL:AAF10393.1};
DE Short=PRODH {ECO:0000303|PubMed:23151026};
DE EC=1.5.5.2 {ECO:0000269|PubMed:23151026};
DE AltName: Full=DrPRODH {ECO:0000303|PubMed:23151026};
DE AltName: Full=Proline oxidase {ECO:0000305};
GN OrderedLocusNames=DR_0814 {ECO:0000312|EMBL:AAF10393.1};
GN ORFNames=A2G07_09440 {ECO:0000312|EMBL:ANC71972.1};
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230 {ECO:0000312|EMBL:AAF10393.1};
RN [1] {ECO:0000312|EMBL:AAF10393.1, ECO:0000312|Proteomes:UP000002524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422 {ECO:0000312|Proteomes:UP000002524};
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422 {ECO:0000312|EMBL:ANC71972.1};
RA Hua X., Hua Y.;
RT "Compelete genome sequence of the extremely radiation-resistant bacteria
RT Deinococcus radiodurans R1.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0007744|PDB:4H6Q, ECO:0007744|PDB:4H6R}
RP X-RAY CRYSTALLOGRAPHY (1.36 ANGSTROMS) IN COMPLEXES WITH FAD AND SUBSTRATE
RP ANALOG, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF GLY-63 AND GLU-64.
RX PubMed=23151026; DOI=10.1021/bi301312f;
RA Luo M., Arentson B.W., Srivastava D., Becker D.F., Tanner J.J.;
RT "Crystal structures and kinetics of monofunctional proline dehydrogenase
RT provide insight into substrate recognition and conformational changes
RT associated with flavin reduction and product release.";
RL Biochemistry 51:10099-10108(2012).
CC -!- FUNCTION: Converts proline to delta-1-pyrroline-5-carboxylate.
CC {ECO:0000269|PubMed:23151026}.
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:23151026};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:23151026};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=290 mM for proline (at 23 degrees Celsius and pH 7.5)
CC {ECO:0000269|PubMed:23151026};
CC KM=0.155 mM for coenzyme Q1 (at 23 degrees Celsius and pH 7.5)
CC {ECO:0000269|PubMed:23151026};
CC Note=kcat 8.7 sec(-1) is for proline. kcat is 14 sec(-1) for coenzyme
CC Q1. {ECO:0000269|PubMed:23151026};
CC -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC glutamate; L-glutamate from L-proline: step 1/2. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the proline dehydrogenase family. {ECO:0000305}.
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DR EMBL; AE000513; AAF10393.1; -; Genomic_DNA.
DR EMBL; CP015081; ANC71972.1; -; Genomic_DNA.
DR PIR; D75471; D75471.
DR RefSeq; NP_294538.1; NC_001263.1.
DR RefSeq; WP_010887460.1; NZ_CP015081.1.
DR PDB; 4H6Q; X-ray; 1.36 A; A/C=1-310.
DR PDB; 4H6R; X-ray; 1.75 A; A/C=1-310.
DR PDBsum; 4H6Q; -.
DR PDBsum; 4H6R; -.
DR AlphaFoldDB; Q9RW55; -.
DR SMR; Q9RW55; -.
DR STRING; 243230.DR_0814; -.
DR EnsemblBacteria; AAF10393; AAF10393; DR_0814.
DR KEGG; dra:DR_0814; -.
DR PATRIC; fig|243230.17.peg.995; -.
DR eggNOG; COG0506; Bacteria.
DR HOGENOM; CLU_061158_0_0_0; -.
DR InParanoid; Q9RW55; -.
DR OMA; YPMIGSH; -.
DR OrthoDB; 1746057at2; -.
DR BRENDA; 1.5.99.B2; 1856.
DR UniPathway; UPA00261; UER00373.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0071949; F:FAD binding; IDA: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 3D-structure; FAD; Flavoprotein; Nucleotide-binding; Oxidoreductase;
KW Proline metabolism; Reference proteome.
FT CHAIN 1..310
FT /note="Proline dehydrogenase"
FT /id="PRO_0000436838"
FT ACT_SITE 135
FT /evidence="ECO:0000250|UniProtKB:Q72IB8"
FT ACT_SITE 187
FT /evidence="ECO:0000250|UniProtKB:Q72IB8"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23151026,
FT ECO:0007744|PDB:4H6Q"
FT BINDING 136
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:23151026,
FT ECO:0007744|PDB:4H6Q"
FT BINDING 166
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:23151026,
FT ECO:0007744|PDB:4H6Q"
FT BINDING 187..192
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:23151026,
FT ECO:0007744|PDB:4H6Q"
FT BINDING 229..230
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:23151026,
FT ECO:0007744|PDB:4H6Q"
FT BINDING 291..292
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23151026,
FT ECO:0007744|PDB:4H6Q"
FT BINDING 292..295
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:23151026,
FT ECO:0007744|PDB:4H6Q"
FT SITE 278
FT /note="Critical for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q72IB8"
FT MUTAGEN 63
FT /note="G->A: 140-fold decrease in catalytic efficiency for
FT proline."
FT /evidence="ECO:0000269|PubMed:23151026"
FT MUTAGEN 64
FT /note="E->A: 27-fold decrease in catalytic efficiency for
FT proline."
FT /evidence="ECO:0000269|PubMed:23151026"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:4H6Q"
FT HELIX 21..31
FT /evidence="ECO:0007829|PDB:4H6Q"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:4H6Q"
FT HELIX 40..52
FT /evidence="ECO:0007829|PDB:4H6Q"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:4H6Q"
FT HELIX 69..88
FT /evidence="ECO:0007829|PDB:4H6Q"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:4H6Q"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:4H6Q"
FT TURN 102..105
FT /evidence="ECO:0007829|PDB:4H6Q"
FT HELIX 113..127
FT /evidence="ECO:0007829|PDB:4H6Q"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:4H6Q"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:4H6Q"
FT HELIX 142..156
FT /evidence="ECO:0007829|PDB:4H6Q"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:4H6Q"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:4H6Q"
FT HELIX 172..178
FT /evidence="ECO:0007829|PDB:4H6Q"
FT HELIX 179..182
FT /evidence="ECO:0007829|PDB:4H6Q"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:4H6Q"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:4H6Q"
FT HELIX 204..220
FT /evidence="ECO:0007829|PDB:4H6Q"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:4H6Q"
FT HELIX 232..244
FT /evidence="ECO:0007829|PDB:4H6Q"
FT STRAND 251..257
FT /evidence="ECO:0007829|PDB:4H6Q"
FT HELIX 262..270
FT /evidence="ECO:0007829|PDB:4H6Q"
FT STRAND 275..283
FT /evidence="ECO:0007829|PDB:4H6Q"
FT HELIX 286..294
FT /evidence="ECO:0007829|PDB:4H6Q"
SQ SEQUENCE 310 AA; 34927 MW; BFD5B7607E17B063 CRC64;
MIDQLYRKAV LTVAERPQVE QLARQKMWNL AERFVAGESI ESAIQAVQAL ERDGIAGNLD
LLGEFIDSPA KCTEFADDVI KLIEAAHAAG IKPYVSIKLS SVGQGKDENG EDLGLTNARR
IIAKAKEYGG FICLDMEDHT RVDVTLEQFR TLVGEFGAEH VGTVLQSYLY RSLGDRASLD
DLRPNIRMVK GAYLEPATVA YPDKADVDQN YRRLVFQHLK AGNYTNVATH DERIIDDVKR
FVLAHGIGKD AFEFQMLYGI RRDLQKQLAA EGYRVRVYLP YGRDWYAYFS RRIAETPRNA
AFVVQGMLKG
