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Database: UniProt
Entry: A0A1Q8AWI2_9CREN
LinkDB: A0A1Q8AWI2_9CREN
Original site: A0A1Q8AWI2_9CREN 
ID   A0A1Q8AWI2_9CREN        Unreviewed;       341 AA.
AC   A0A1Q8AWI2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Proline dehydrogenase domain-containing protein {ECO:0000259|Pfam:PF01619};
GN   ORFNames=AUF79_17940 {ECO:0000313|EMBL:OLE84106.1};
OS   Crenarchaeota archaeon 13_1_20CM_2_51_8.
OC   Archaea; Thermoproteota.
OX   NCBI_TaxID=1805093 {ECO:0000313|EMBL:OLE84106.1, ECO:0000313|Proteomes:UP000186073};
RN   [1] {ECO:0000313|EMBL:OLE84106.1, ECO:0000313|Proteomes:UP000186073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27843720;
RA   Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA   Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA   Banfield J.F.;
RT   "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT   heterotrophy are prevalent below the grass root zone.";
RL   PeerJ 4:E2687-E2687(2016).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OLE84106.1}.
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DR   EMBL; MNKD01000804; OLE84106.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q8AWI2; -.
DR   Proteomes; UP000186073; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004657; F:proline dehydrogenase activity; IEA:InterPro.
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: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   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        295..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        321..339
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          27..269
FT                   /note="Proline dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF01619"
SQ   SEQUENCE   341 AA;  38765 MW;  4AD5CEA9213B57A6 CRC64;
     MPGLTERLLY RVAKRWIAGY TLEDAIRVAH NANNRKLSVI LNRLGEHTPD EKLIQGYTEE
     YLKLLDQIQE GKIDGTISVK PSQLGLAANP SLYGTNLLRI IERAEAYDEF VWIDMENSPY
     TEGTLKTYRE ILPGHRQLGV CLQANMKRTE SDLKDLISRG GIIRLVKGAY PETGESVYKK
     RSDVDANYVR LMIMLFEGGG RFAIGTHDGK LIDKARELAK EQKRDFEFQM LKGIRDDIKP
     TLIEEGYRVS EYIPYGPEWY NYSKRRMRER KRNILREMKL RDGGLVVTDQ VDKNFIADLL
     VLLVILVVVV GGFAFLHSPS ILLGGGLALV VAVAAEFAWS R
//
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