ID A0A1U7PKZ6_9BACI Unreviewed; 326 AA.
AC A0A1U7PKZ6;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=proline dehydrogenase {ECO:0000256|ARBA:ARBA00012695};
DE EC=1.5.5.2 {ECO:0000256|ARBA:ARBA00012695};
GN ORFNames=SAMN05428946_0972 {ECO:0000313|EMBL:SIT73360.1};
OS Edaphobacillus lindanitolerans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Edaphobacillus.
OX NCBI_TaxID=550447 {ECO:0000313|EMBL:SIT73360.1, ECO:0000313|Proteomes:UP000187550};
RN [1] {ECO:0000313|EMBL:SIT73360.1, ECO:0000313|Proteomes:UP000187550}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MNA4 {ECO:0000313|EMBL:SIT73360.1,
RC ECO:0000313|Proteomes:UP000187550};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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; FTPL01000001; SIT73360.1; -; Genomic_DNA.
DR RefSeq; WP_076757194.1; NZ_FTPL01000001.1.
DR AlphaFoldDB; A0A1U7PKZ6; -.
DR STRING; 550447.SAMN05428946_0972; -.
DR OrthoDB; 9773461at2; -.
DR UniPathway; UPA00261; UER00373.
DR Proteomes; UP000187550; 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}.
FT DOMAIN 44..290
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000196-1"
FT BINDING 132
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000196-2"
FT BINDING 160
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000196-2"
FT BINDING 182..184
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000196-2"
FT BINDING 196
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000196-2"
FT BINDING 221..222
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000196-2"
FT BINDING 283
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000196-1"
FT BINDING 284
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000196-1"
SQ SEQUENCE 326 AA; 37541 MW; AD309452B44969C4 CRC64;
MSVAKDFFIM LSQNRMLNGA AKRWGLKLGA QSVVAGTTID EMVDSIRKLN ANGISATIDN
LGEFVFEKEE ALQAKEQILA VVEAIHQHKL DAHISLKPTQ LGLDVDVDFC RENLREIVAA
AHEYGIFVNF DMEDYSHLQP SFDLLEELHG DYDNVGTVIQ AYFFRAEEDI EKFKDYRLRI
VKGAYKEPEH LAYQTKEAID ANYIKLIEYH LLNGPFTSIA THDHHVINHV KKFVSEHGIP
NDKFEFQMLY GFRTDMQLEL TKEGYNFCTY VPFGIDWYGY FMRRLAERPQ NLNLIVKQTF
NKKTNTMIGL GVGAFLLGRI SKRTRR
//
