ID A0A0T5ZIL5_9CHLR Unreviewed; 315 AA.
AC A0A0T5ZIL5;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=proline dehydrogenase {ECO:0000256|ARBA:ARBA00012695};
DE EC=1.5.5.2 {ECO:0000256|ARBA:ARBA00012695};
GN ORFNames=XU10_C0023G0021 {ECO:0000313|EMBL:KRT62643.1};
OS Chloroflexi bacterium CSP1-4.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1640513 {ECO:0000313|EMBL:KRT62643.1, ECO:0000313|Proteomes:UP000051896};
RN [1] {ECO:0000313|EMBL:KRT62643.1, ECO:0000313|Proteomes:UP000051896}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSP1-4 {ECO:0000313|EMBL:KRT62643.1};
RA Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT "Critical biogeochemical functions in the subsurface are associated with
RT bacteria from new phyla and little studied lineages.";
RL Submitted (MAY-2015) 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|PIRSR:PIRSR000196-2};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000196-2};
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}.
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:KRT62643.1}.
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DR EMBL; LDXM01000023; KRT62643.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T5ZIL5; -.
DR STRING; 1640513.XU10_C0023G0021; -.
DR PATRIC; fig|1640513.3.peg.1879; -.
DR UniPathway; UPA00261; UER00373.
DR Proteomes; UP000051896; Unassembled WGS sequence.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0004657; F:proline dehydrogenase activity; IEA:UniProtKB-EC.
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 FAD {ECO:0000256|PIRSR:PIRSR000196-2};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000196-2};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000196-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:KRT62643.1}.
FT DOMAIN 52..305
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT BINDING 106
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000196-1"
FT BINDING 141
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000196-2"
FT BINDING 169
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000196-2"
FT BINDING 193..195
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000196-2"
FT BINDING 207
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000196-2"
FT BINDING 232..233
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000196-2"
FT BINDING 294
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000196-1"
FT BINDING 295
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000196-1"
SQ SEQUENCE 315 AA; 35130 MW; A05E33CE11CBFB99 CRC64;
MADLRRLPAH LLRGTFIWAS HRPSLGRLAT AVPLTRPMVR RFVAGETLAE ALEACDRLRG
AGMHTTLDIL GESVTSATAA REAATRYVDT LGALAQRGLD GNVSLKLTQM GLDVDPALCR
ENVGRVAAKA AEVGAFVRVD MEDSPKTEAT LTLVRELRAT TPDVGAVIQS YLRRSADDVE
RLIAEGTRVR LCKGAYDEPA EVAFPTKGEV DASYRRLMER LLRDGVYPAL ATHDDGLIAD
AEAFARREGI DPSRFEFQML YGIRRDLQAR LVREGWNVRV YVPYGREWYP YFMRRLAERP
ANVLFLLRSV VREGR
//
