ID A0A1H9XUH4_9MICO Unreviewed; 316 AA.
AC A0A1H9XUH4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-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=SAMN05216199_0336 {ECO:0000313|EMBL:SES49343.1};
OS Pedococcus cremeus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Pedococcus.
OX NCBI_TaxID=587636 {ECO:0000313|EMBL:SES49343.1, ECO:0000313|Proteomes:UP000199019};
RN [1] {ECO:0000313|Proteomes:UP000199019}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6963 {ECO:0000313|Proteomes:UP000199019};
RA Varghese N., Submissions S.;
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|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}.
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DR EMBL; FOHB01000012; SES49343.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9XUH4; -.
DR STRING; 587636.SAMN05216199_0336; -.
DR UniPathway; UPA00261; UER00373.
DR Proteomes; UP000199019; 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 Reference proteome {ECO:0000313|Proteomes:UP000199019}.
FT DOMAIN 49..307
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000196-1"
FT BINDING 143
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000196-2"
FT BINDING 171
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000196-2"
FT BINDING 195..197
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000196-2"
FT BINDING 234..235
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000196-2"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000196-1"
FT BINDING 297
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000196-1"
SQ SEQUENCE 316 AA; 35330 MW; F705A9717378CAD9 CRC64;
MDAGDLLRNA LLQLSKSDGV RRTIETAPVS RQVVRRFVPG STTEDAVAAT AELRMTNRLA
TIDYLGEDTT DLTQAIRTRD AYVHLLRELK RADLSQMGMG EVSLKLSALG QALPGDGAKI
ALEHAREICE AAADAGTTVT LDMEDHTTTD ATLEALRELR QDFPWVGAVI QSYLRRSEAD
CRDLAHEGSR VRLCKGAYKE PESVAFQSSE EVDTAYVRCL KVLMAGDGYP MVASHDPRLL
EIAGALAAHH RRDPQTFEYQ MLYGIRPEEQ KRIADRGDQM RVYIPYGEEW YGYLMRRMAE
RPANTMFFLR GLASRG
//
