ID A0A1D8YAY6_9GAMM Unreviewed; 1079 AA.
AC A0A1D8YAY6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Bifunctional protein PutA {ECO:0000256|PIRNR:PIRNR000197};
DE Includes:
DE RecName: Full=Proline dehydrogenase {ECO:0000256|PIRNR:PIRNR000197};
DE EC=1.5.5.2 {ECO:0000256|PIRNR:PIRNR000197};
DE AltName: Full=Proline oxidase {ECO:0000256|PIRNR:PIRNR000197};
DE Includes:
DE RecName: Full=Delta-1-pyrroline-5-carboxylate dehydrogenase {ECO:0000256|PIRNR:PIRNR000197};
DE Short=P5C dehydrogenase {ECO:0000256|PIRNR:PIRNR000197};
DE EC=1.2.1.88 {ECO:0000256|PIRNR:PIRNR000197};
DE AltName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR000197};
GN ORFNames=BIZ42_11140 {ECO:0000313|EMBL:AOX62711.1};
OS Stenotrophomonas sp. LM091.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=1904944 {ECO:0000313|EMBL:AOX62711.1, ECO:0000313|Proteomes:UP000177427};
RN [1] {ECO:0000313|EMBL:AOX62711.1, ECO:0000313|Proteomes:UP000177427}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LM091 {ECO:0000313|EMBL:AOX62711.1,
RC ECO:0000313|Proteomes:UP000177427};
RA Lefeuvre P.;
RT "Complete genome sequence of a copper-resistant commensal bacteria:
RT Stenotrophomonas sp. strain LM091.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Oxidizes proline to glutamate for use as a carbon and
CC nitrogen source. {ECO:0000256|PIRNR:PIRNR000197}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamate 5-semialdehyde + NAD(+) = 2 H(+) + L-
CC glutamate + NADH; Xref=Rhea:RHEA:30235, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58066; EC=1.2.1.88;
CC Evidence={ECO:0000256|ARBA:ARBA00001468,
CC ECO:0000256|PIRNR:PIRNR000197};
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|PIRNR:PIRNR000197};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRNR:PIRNR000197};
CC -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC glutamate; L-glutamate from L-proline: step 1/2.
CC {ECO:0000256|PIRNR:PIRNR000197}.
CC -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC glutamate; L-glutamate from L-proline: step 2/2.
CC {ECO:0000256|ARBA:ARBA00004786, ECO:0000256|PIRNR:PIRNR000197}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the aldehyde
CC dehydrogenase family. {ECO:0000256|PIRNR:PIRNR000197}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the proline
CC dehydrogenase family. {ECO:0000256|PIRNR:PIRNR000197}.
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DR EMBL; CP017483; AOX62711.1; -; Genomic_DNA.
DR RefSeq; WP_070426472.1; NZ_CP017483.1.
DR AlphaFoldDB; A0A1D8YAY6; -.
DR STRING; 1904944.BIZ42_11140; -.
DR KEGG; slm:BIZ42_11140; -.
DR OrthoDB; 9812625at2; -.
DR UniPathway; UPA00261; UER00373.
DR Proteomes; UP000177427; Chromosome.
DR GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0004657; F:proline dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006561; P:proline biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0010133; P:proline catabolic process to glutamate; IEA:UniProtKB-UniRule.
DR CDD; cd07125; ALDH_PutA-P5CDH; 1.
DR Gene3D; 3.20.20.220; -; 1.
DR Gene3D; 1.20.5.460; Single helix bin; 1.
DR Gene3D; 1.20.5.550; Single Helix bin; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR025703; Bifunct_PutA.
DR InterPro; IPR029041; FAD-linked_oxidoreductase-like.
DR InterPro; IPR041349; PRODH.
DR InterPro; IPR024090; PRODH_PutA_dom_I.
DR InterPro; IPR024089; PRODH_PutA_dom_I/II.
DR InterPro; IPR024082; PRODH_PutA_dom_II.
DR InterPro; IPR002872; Proline_DH_dom.
DR InterPro; IPR005933; PutA_C.
DR NCBIfam; TIGR01238; D1pyr5carbox3; 1.
DR PANTHER; PTHR42862; DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE 1, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR42862:SF1; DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE 2, ISOFORM A-RELATED; 1.
DR Pfam; PF00171; Aldedh; 1.
DR Pfam; PF01619; Pro_dh; 1.
DR Pfam; PF14850; Pro_dh-DNA_bdg; 1.
DR Pfam; PF18327; PRODH; 1.
DR PIRSF; PIRSF000197; Bifunct_PutA; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR SUPFAM; SSF51730; FAD-linked oxidoreductase; 1.
DR SUPFAM; SSF81935; N-terminal domain of bifunctional PutA protein; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|PIRNR:PIRNR000197};
KW FAD {ECO:0000256|PIRNR:PIRNR000197};
KW Flavoprotein {ECO:0000256|PIRNR:PIRNR000197};
KW NAD {ECO:0000256|PIRNR:PIRNR000197};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000197};
KW Proline metabolism {ECO:0000256|PIRNR:PIRNR000197};
KW Repressor {ECO:0000256|PIRNR:PIRNR000197};
KW Transcription {ECO:0000256|PIRNR:PIRNR000197};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR000197}.
FT DOMAIN 32..78
FT /note="Proline utilization A proline dehydrogenase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18327"
FT DOMAIN 87..200
FT /note="Proline dehydrogenase PutA"
FT /evidence="ECO:0000259|Pfam:PF14850"
FT DOMAIN 210..509
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 602..1061
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 834
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
FT ACT_SITE 868
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 1079 AA; 115810 MW; 9E8E2D9FEA711336 CRC64;
MTASSVLPPA PASSGAARPP LLSAELPAVP NAFRQAITDA WLKDEATHVR ELLEQARLPA
AEQARVQATA ADLVKRVRVR AQDQGAIEAF MRQYDLGSEE GVLLMCVAEA LLRIPDQETA
DKLIRDKLGD ADWKKHMGGS DSVLVNASTW GLMLTGRLVQ INDATRADVP GAFKRLIGRV
GEPVIRLAVR QAMKIMGHQF VMGRTIDEAL SRSHKGDNAS YRYSFDMLGE GALTMKDAKR
YLEDYRRAIH SIGGDHKARG GRPDGDVNSA PGISIKLSAL YPRYEHAKRA RVMADLVPGV
LELAQLAKSY GIGCTVDAEE TDRLELSLDI IETVVSDASL AGWEGFGVVV QSYQKRTPYT
IDYLADLARR IGRRLQVRLV KGAYWDAEIK RAQIEGLPAY PVFTRKQNTD VSYLACAKRL
FTHSDAIYPM FATHNAHTIA AVQAIAKGGQ YEHQKLHGMG DDLYAEVVPA DRLNVPCRVY
APVGSHEDLL PYLVRRLLEN GANSSFVNRI TDENVAIDDL IRDPVEVVSS FASIPHPKIP
LPVDLLRSQN HDRKNSMGVN LANDNDLRAL AEQLNAAVPA PGKSGWHAAP LVPGANPTAA
LLNVTNPADT RQVVGQWQPA DSATVEKALA NAVAAQPAWN RTPAASRAAI LEHAADQLEA
RLPEFMALCV KEAGKSLPDG IAEVREAVDF LRYYAKQARE QFGHAEKLPS PTGESNELQL
HGRGVFVCIS PWNFPLAIFL GQVSAALAAG NSVIAKPAEQ TNLIGYYAVK LLLDAGVPEG
VVQFLPGDGA TVGAALTADP RVAGVAFTGS TDTARAINRA MAARDAAIGV LIAETGGQNA
FIADSSALPE QLVKDAIGSA FTSAGQRCSA ARVLFVQDDI ADKVMTMLSG AMAELKVGDP
GLLSTDVGPV IDADALQILK DHAVRMEKET RLIAAATLSD EAAHGTFFAP RAYELKNLDQ
LHKEIFGPVL HVIRWKGDQL DAVIDQINAT GYGLTLGVHS RIDETVDRIS SRINVGNVYV
NRNQIGAVVG VQPFGGQGLS GTGPKAGGPH YLLRFATEKT VTVNTTAAGG NASLLTLGD
//
