ID C1H7N6_PARBA Unreviewed; 530 AA.
AC C1H7N6;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 61.
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=PAAG_06777 {ECO:0000313|EMBL:EEH36359.1};
OS Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS brasiliensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502779 {ECO:0000313|EMBL:EEH36359.1, ECO:0000313|Proteomes:UP000002059};
RN [1] {ECO:0000313|EMBL:EEH36359.1, ECO:0000313|Proteomes:UP000002059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-826 / Pb01 {ECO:0000313|Proteomes:UP000002059};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN294011; EEH36359.1; -; Genomic_DNA.
DR RefSeq; XP_002791231.1; XM_002791185.2.
DR AlphaFoldDB; C1H7N6; -.
DR STRING; 502779.C1H7N6; -.
DR GeneID; 9094483; -.
DR KEGG; pbl:PAAG_06777; -.
DR VEuPathDB; FungiDB:PAAG_06777; -.
DR eggNOG; KOG0186; Eukaryota.
DR HOGENOM; CLU_018202_0_1_1; -.
DR OMA; QFCAGEK; -.
DR OrthoDB; 7218at2759; -.
DR Proteomes; UP000002059; Partially assembled WGS sequence.
DR GO; GO:0004657; F:proline dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0006562; P:proline catabolic process; IEA:InterPro.
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:SF30; 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:UP000002059}.
FT DOMAIN 157..512
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT REGION 36..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 530 AA; 58320 MW; BF72AF54798F5507 CRC64;
MRRQVAFKTT SACFGYAGPR TPARRAFSWN QYPVRHSHHE PGQLSDHSLP AAGGSSTSPP
GSTRPYATLN HTMPSSNTPK SSPLSILPLS TILRSLFVTT ISSSPLLFPP SLAFLTILAK
PESTFLNPDN NLLLKTLLGH TMYAQFCAGE TRAEVKGNIK ELKKIGFSGV ILGYAREVTM
DETEIQSLAQ ATVTKEREED MAQGIADLTA WKEGTLETVD LADDGDFVAL KFTGAGKGSV
RHLLHGLPPS SELEEAIVEI CERAKARNVR LLIDAEQQAV QPAIDKWALD FQRRYNKGPN
QRAIVYSTYQ AYLRSAPKTL SEHLAIAKAE GFVLGVKLVR GAYLGTEPRH LIWATKEDTD
KVYDGIAESL IKQQYGEILS PHHHPSTVAG SSNSSGQSNH HSNTFPKVNL VLASHNRASV
DRAQKIRNEQ LRLTGTEQIE MAYGQLSGMA DDISCELVQA GKAAREQQAE GVMAEVEAPK
AYKYLVWGTV GECTRYLLRR AQENRDAASR TEETRRAMAK ELRRRLVGGR
//
