ID A0A022RKE0_ERYGU Unreviewed; 564 AA.
AC A0A022RKE0;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
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 ORFNames=MIMGU_mgv1a003788mg {ECO:0000313|EMBL:EYU39360.1};
OS Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU39360.1, ECO:0000313|Proteomes:UP000030748};
RN [1] {ECO:0000313|EMBL:EYU39360.1, ECO:0000313|Proteomes:UP000030748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA Schmutz J., Willis J.H., Rokhsar D.S.;
RT "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT population shotgun sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
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; KI630445; EYU39360.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A022RKE0; -.
DR STRING; 4155.A0A022RKE0; -.
DR eggNOG; KOG0186; Eukaryota.
DR PhylomeDB; A0A022RKE0; -.
DR Proteomes; UP000030748; Unassembled WGS sequence.
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:SF0; PROLINE DEHYDROGENASE 1, MITOCHONDRIAL; 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:UP000030748}.
FT DOMAIN 217..545
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT REGION 38..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 564 AA; 61652 MW; 32615E8787947F40 CRC64;
MASRIGHSKL LLNLPVFSRR LNTAASPSTT AAAATVPQAN FTGDPNPFDT KSTADDPTDL
FSSTVTIRLN TAAPPFITAA VPQPNFIKIP KTPVSLDDPE ELPPVKSIDP TTAGSGGGSG
GGAAVAGGEP PINLDDPREL FSSVPTSKLI KSTVTLHMAS MDSMVDMGSW VLKSGLMQNP
ISKGLVLGSI KHTFYEHFCG GKDLKEADNT VKRIWDDYGL RAMLDYGMEH ALDNGSCDSN
LDEFIQTIQS ATHSPTSPVS FVVVKITAIC PPSLLKRVSD LLRWEHKDKS MHLPWKRESF
PIFSDSTALY HTPQMPPPLT PKEENDLDLA YKRLVKICDK SLEANLPMLI DAEDTLIQPA
IDYFAYCAAI KYRRAHNIPL IFNTIQAYLK DARERLVIAK ISANKMGVPL GVKLVRGAYM
SSERKLAFFV GAESPIHETI QDTHACFNSC ASFMLEEIAK GSGSLVLATH NIESGKLAAA
KAVELGLEKD NENLEFAQLY GMAQALSFGL RNAGFKVSKY VPFGPVEQIM PYLLRRAEEN
RGLLSTSSLD RQLMRKELVR RIIS
//
