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Database: UniProt
Entry: D2RY52_HALTV
LinkDB: D2RY52_HALTV
Original site: D2RY52_HALTV 
ID   D2RY52_HALTV            Unreviewed;       278 AA.
AC   D2RY52;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=proline dehydrogenase {ECO:0000256|ARBA:ARBA00012695};
DE            EC=1.5.5.2 {ECO:0000256|ARBA:ARBA00012695};
GN   OrderedLocusNames=Htur_2929 {ECO:0000313|EMBL:ADB61798.1};
OS   Haloterrigena turkmenica (strain ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB
OS   13204 / VKM B-1734 / 4k) (Halococcus turkmenicus).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Haloterrigena.
OX   NCBI_TaxID=543526 {ECO:0000313|EMBL:ADB61798.1, ECO:0000313|Proteomes:UP000001903};
RN   [1] {ECO:0000313|EMBL:ADB61798.1, ECO:0000313|Proteomes:UP000001903}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB 13204 / VKM B-1734 /
RC   4k {ECO:0000313|Proteomes:UP000001903};
RX   PubMed=21304683; DOI=10.4056/sigs.681272;
RA   Saunders E., Tindall B.J., Fahnrich R., Lapidus A., Copeland A.,
RA   Del Rio T.G., Lucas S., Chen F., Tice H., Cheng J.F., Han C., Detter J.C.,
RA   Bruce D., Goodwin L., Chain P., Pitluck S., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Rohde M., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Haloterrigena turkmenica type strain (4k).";
RL   Stand. Genomic Sci. 2:107-116(2010).
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; CP001860; ADB61798.1; -; Genomic_DNA.
DR   RefSeq; WP_012944063.1; NC_013743.1.
DR   AlphaFoldDB; D2RY52; -.
DR   STRING; 543526.Htur_2929; -.
DR   GeneID; 8743546; -.
DR   KEGG; htu:Htur_2929; -.
DR   eggNOG; arCOG06322; Archaea.
DR   HOGENOM; CLU_061158_0_0_2; -.
DR   OrthoDB; 8727at2157; -.
DR   UniPathway; UPA00261; UER00373.
DR   Proteomes; UP000001903; Chromosome.
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          18..270
FT                   /note="Proline dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF01619"
SQ   SEQUENCE   278 AA;  31366 MW;  7C89369F383B1654 CRC64;
     MIPPIANRFV AGESPARALE HVRRLNDRNI AGIVNLLGEH YTARPPVRSD AAEYRALVRD
     IANSHLEACI SVKPSQLGLD LGEDVFRETL ADVVEVAADH GVFVWIDMED HTTTDATLEA
     YEDLARAHAG GVGVCVQANL KRTREDVERL ADVPGKVRFV KGAYDEPADI AYRDTDRIDR
     EYEALLEYAF EHYGGGIAVG SHDPEMIEHA IDCHETHGTD FELQMLMGVR EDAQDDLAAE
     YPVYQYVPYG DRWKSYFYRR MTERTANVRF ALRAVLDR
//
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