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Database: UniProt
Entry: I1N4V3_SOYBN
LinkDB: I1N4V3_SOYBN
Original site: I1N4V3_SOYBN 
ID   I1N4V3_SOYBN            Unreviewed;       489 AA.
AC   I1N4V3;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 63.
DE   RecName: Full=Proline dehydrogenase {ECO:0000256|ARBA:ARBA00012695, ECO:0000256|RuleBase:RU364054};
DE            EC=1.5.5.2 {ECO:0000256|ARBA:ARBA00012695, ECO:0000256|RuleBase:RU364054};
GN   Name=100799876 {ECO:0000313|EnsemblPlants:KRH01467};
GN   ORFNames=GLYMA_18G278900 {ECO:0000313|EMBL:KRH01467.1};
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847 {ECO:0000313|EMBL:KRH01467.1};
RN   [1] {ECO:0000313|EMBL:KRH01467.1, ECO:0000313|EnsemblPlants:KRH01467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH01467};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH01467.1};
RX   PubMed=20075913; DOI=10.1038/nature08670;
RA   Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA   Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA   Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA   Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA   Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA   Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA   Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA   Stacey G., Shoemaker R.C., Jackson S.A.;
RT   "Genome sequence of the palaeopolyploid soybean.";
RL   Nature 463:178-183(2010).
RN   [2] {ECO:0000313|EnsemblPlants:KRH01467}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH01467};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:KRH01467.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH01467.1};
RA   Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA   Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA   Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA   Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA   Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA   Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA   Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA   Jackson S.;
RT   "WGS assembly of Glycine max.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Converts proline to delta-1-pyrroline-5-carboxylate.
CC       {ECO:0000256|RuleBase:RU364054}.
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|RuleBase:RU364054};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|RuleBase:RU364054};
CC   -!- SIMILARITY: Belongs to the proline oxidase family.
CC       {ECO:0000256|ARBA:ARBA00005869, ECO:0000256|RuleBase:RU364054}.
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DR   EMBL; CM000851; KRH01467.1; -; Genomic_DNA.
DR   RefSeq; XP_003552630.1; XM_003552582.3.
DR   AlphaFoldDB; I1N4V3; -.
DR   SMR; I1N4V3; -.
DR   STRING; 3847.I1N4V3; -.
DR   PaxDb; 3847-GLYMA18G51400-1; -.
DR   EnsemblPlants; KRH01467; KRH01467; GLYMA_18G278900.
DR   GeneID; 100799876; -.
DR   Gramene; KRH01467; KRH01467; GLYMA_18G278900.
DR   KEGG; gmx:100799876; -.
DR   eggNOG; KOG0186; Eukaryota.
DR   HOGENOM; CLU_018202_3_0_1; -.
DR   InParanoid; I1N4V3; -.
DR   OMA; WMQDAAD; -.
DR   OrthoDB; 5473051at2759; -.
DR   Proteomes; UP000008827; Chromosome 18.
DR   ExpressionAtlas; I1N4V3; baseline and differential.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0071949; F:FAD binding; IBA:GO_Central.
DR   GO; GO:0004657; F:proline dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0010133; P:proline catabolic process to glutamate; IBA:GO_Central.
DR   Gene3D; 3.20.20.220; -; 1.
DR   InterPro; IPR029041; FAD-linked_oxidoreductase-like.
DR   InterPro; IPR002872; Proline_DH_dom.
DR   InterPro; IPR015659; Proline_oxidase.
DR   PANTHER; PTHR13914:SF33; PROLINE DEHYDROGENASE; 1.
DR   PANTHER; PTHR13914; PROLINE OXIDASE; 1.
DR   Pfam; PF01619; Pro_dh; 1.
DR   SUPFAM; SSF51730; FAD-linked oxidoreductase; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|RuleBase:RU364054};
KW   Flavoprotein {ECO:0000256|RuleBase:RU364054};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU364054};
KW   Proline metabolism {ECO:0000256|ARBA:ARBA00023062,
KW   ECO:0000256|RuleBase:RU364054};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008827}.
FT   DOMAIN          138..465
FT                   /note="Proline dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF01619"
SQ   SEQUENCE   489 AA;  53996 MW;  43AFF66BC683A3B3 CRC64;
     MATRVIPPRI LRNLRYNTAT KPLNSSHPPL SPSLSPSLCI PAPPPISAVL PPSDDLSFRD
     VEKLFSSVPT TTLLRSTAVL HATALEPMVD FGTWLMRSNL MQVPGLSDLI LATVRNTFFD
     HFCAGEDATT TADSVRHLNK AGLRGMLVYG VEDANNNDAC HRNFKGFLHT IDVSRSLPPS
     SVSFVIVKIT AICPMSLLER MSDLLRWQHK DPSFSLPWKQ DCFPIFSESS PLYHTSKRPE
     PLTREEESDL QLAMQRFLEL CQKCVQANIP LLVDAEHTSV QPAIDYFTYS SAILHNKGDN
     PIVFGTIQTY LKDAKERLVL AAEAADNMGI PMGFKLVRGA YMSSETKLAE SLGYSSPIHN
     TIEDTHKCFN DCSSFMLEKV ANGPGGVVLA THNVESGKLA AAKAHELGVG KVNHKLEFAQ
     LHGMSEALSF GLSNAGFQVS KYMPFGPVET VMPYLLRRAE ENRGMLAASG FDRQLMRKEL
     GRRLKAAFF
//
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