ID W0JT26_9EURY Unreviewed; 323 AA.
AC W0JT26;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=proline dehydrogenase {ECO:0000256|ARBA:ARBA00012695};
DE EC=1.5.5.2 {ECO:0000256|ARBA:ARBA00012695};
GN ORFNames=HALLA_16600 {ECO:0000313|EMBL:AHG00178.1};
OS Halostagnicola larsenii XH-48.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Halostagnicola.
OX NCBI_TaxID=797299 {ECO:0000313|EMBL:AHG00178.1, ECO:0000313|Proteomes:UP000019024};
RN [1] {ECO:0000313|EMBL:AHG00178.1, ECO:0000313|Proteomes:UP000019024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XH-48 {ECO:0000313|EMBL:AHG00178.1,
RC ECO:0000313|Proteomes:UP000019024};
RG DOE Joint Genome Institute;
RA Anderson I., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (JAN-2014) 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; CP007055; AHG00178.1; -; Genomic_DNA.
DR RefSeq; WP_049953419.1; NZ_CP007055.1.
DR AlphaFoldDB; W0JT26; -.
DR STRING; 797299.HALLA_16600; -.
DR GeneID; 25146032; -.
DR KEGG; hlr:HALLA_16600; -.
DR PATRIC; fig|797299.3.peg.2327; -.
DR eggNOG; arCOG06322; Archaea.
DR HOGENOM; CLU_061158_0_0_2; -.
DR OrthoDB; 8727at2157; -.
DR UniPathway; UPA00261; UER00373.
DR Proteomes; UP000019024; 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; 2.
DR SUPFAM; SSF51730; FAD-linked oxidoreductase; 2.
PE 4: Predicted;
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000019024}.
FT DOMAIN 19..314
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT REGION 132..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 323 AA; 35708 MW; BDE81B55321ACBC3 CRC64;
MIPPIASRFV AGESPAKAIE HVQQLDDDEV GAILNLLGEH HTDPDVIAED VDAYRSLADS
IARTTFDACI SVKPSQIGLD IGPEEFESNL ERIVSHAADR DVFVWVDMED HTTTDATLEA
YERLAREYAP DRSARAEEVA GAGATEATEI GSTKTAESGS GTDGVMVEDG AVGEGVLGLC
LQANLKRTRE DLERLSDVPG KVRLVKGAYD EPKSIAYKEK ERVDEAYRTL LEDAFENRDG
GIAVGSHDPA MIEYARELHE EYGTPYEVQM LMGVRDDAQR DLAADGVTVY QYVPYGSRWL
SYFYRRVRER KENLLFAVRA VLS
//
