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Database: UniProt
Entry: A0A1H8WJJ5_9EURY
LinkDB: A0A1H8WJJ5_9EURY
Original site: A0A1H8WJJ5_9EURY 
ID   A0A1H8WJJ5_9EURY        Unreviewed;       279 AA.
AC   A0A1H8WJJ5;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=proline dehydrogenase {ECO:0000256|ARBA:ARBA00012695};
DE            EC=1.5.5.2 {ECO:0000256|ARBA:ARBA00012695};
GN   ORFNames=SAMN04487948_13127 {ECO:0000313|EMBL:SEP27811.1};
OS   Halogranum amylolyticum.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae.
OX   NCBI_TaxID=660520 {ECO:0000313|EMBL:SEP27811.1, ECO:0000313|Proteomes:UP000199126};
RN   [1] {ECO:0000313|EMBL:SEP27811.1, ECO:0000313|Proteomes:UP000199126}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.10121 {ECO:0000313|EMBL:SEP27811.1,
RC   ECO:0000313|Proteomes:UP000199126};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00001974};
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; FODV01000031; SEP27811.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8WJJ5; -.
DR   OrthoDB; 8727at2157; -.
DR   UniPathway; UPA00261; UER00373.
DR   Proteomes; UP000199126; Unassembled WGS sequence.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0004657; F:proline dehydrogenase activity; IEA:InterPro.
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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          22..272
FT                   /note="Proline dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF01619"
SQ   SEQUENCE   279 AA;  31593 MW;  7C4C188BC3FB5D84 CRC64;
     MIPPIASRFV AAETATESLD YVAELNRDGI GGILNLLGEH YQTREAADED VSAYLDLVEQ
     VGRTELTACL SVKPSQIGLD AGDDVFRENL GRILERADEQ GVFVWVDMED HTTTDVTLDA
     YTEFATEYDG GVGLCVQANL KRTAEDLPRL ADVPGKVRLV KGAYDEPPEV AYQQKKHVNE
     AYRQYLEYMF EAFDGGIAVG SHDPEMIDYA RELHEEYGTD FEIQMLMGVR TDAQRELAQQ
     GYEVNQYIPY GDKWMSYFYR RIRERKENLV FAARAVLTS
//
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