ID A0A023Y838_9GAMM Unreviewed; 1074 AA.
AC A0A023Y838;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 49.
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=DX03_18265 {ECO:0000313|EMBL:AHY60586.1};
OS Stenotrophomonas rhizophila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=216778 {ECO:0000313|EMBL:AHY60586.1, ECO:0000313|Proteomes:UP000025222};
RN [1] {ECO:0000313|EMBL:AHY60586.1, ECO:0000313|Proteomes:UP000025222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14405 {ECO:0000313|Proteomes:UP000025222};
RA Alavi P., Starcher M.R., Thallinger G., Zachow C., Mueller H., Berg G.;
RT "Is there a border between beneficial and pathogenic bacteria?";
RL Submitted (APR-2014) 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; CP007597; AHY60586.1; -; Genomic_DNA.
DR RefSeq; WP_038690933.1; NZ_CP007597.1.
DR AlphaFoldDB; A0A023Y838; -.
DR STRING; 216778.DX03_18265; -.
DR GeneID; 61477857; -.
DR HOGENOM; CLU_005682_1_0_6; -.
DR UniPathway; UPA00261; UER00373.
DR Proteomes; UP000025222; 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 33..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 597..1056
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 829
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
FT ACT_SITE 863
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 1074 AA; 115292 MW; 94BB53364E749159 CRC64;
MTAPSAPIPA PAPSGALRPP LLSPELRTPP PAFRQAITDA WMKDEASHVR ELLAQARLPA
DEQAQVQATA ADLVKRVRVR AQDQGAIEAF MRQYDLGSEE GVLLMCVAEA LLRIPDQDTA
DKLIRDKLGD ADWKKHMGGS DSVLVNASTW GLMLTGRLVQ INDATRADVP GAFARLIGRV
GEPVIRLAVR QAMKIMGHQF VMGRTIDEAL SRSHKGDNAS YRYSFDMLGE GALTMKDAKR
YLEDYRRAIH SIGGDHKARG GRPDGDVNAA PGISIKLSAL YPRYEHAKRA RVMADLVPGV
LELAQLAKSY GIGCTVDAEE TDRLELSLDI IEAVVSDASL SGWEGFGVVV QAYQKRTPYT
IDYLADLARR IGRRLQVRLV KGAYWDAEIK RAQIDGLPAY PVFTRKQNTD VSYLACTKRL
FSHADALYPM FATHNAHTIA AVKAIAKGGQ YEHQKLHGMG DDLYAEVVPA NRLNVPCRVY
APVGSHEDLL PYLVRRLLEN GANSSFVNRI TDDAVAIDDL IRDPVEAVSS FASIPHPKIP
LPVDLLRSQN HDRTNSMGVN LANDNDLRAL AEQLNAAVKP WKAAPLVPGA TPTGVLLNVT
NPADTRQVVG QWQPADSATV EKALANAVAA QPAWNRTPAA SRAAILEHAA EQLEARMPEF
MALCVKEAGK SLPDGIAEVR EAVDFLRYYA KQAREQFGHA EKLPSPTGES NELQLHGRGV
FVCISPWNFP LAIFLGQVAA ALAAGNSVIA KPAEQTNLIG YYAVKLLLDA GVPEGVVQFL
PGDGATVGAA LTADPRVAGV AFTGSTDTAR AINRAMAARD AAIGVLIAET GGQNAFIADS
SALPEQLVKD AIGSAFTSAG QRCSAARVLF VQDDIADKVM TMLSGAMAEL KVGDPGLLST
DVGPVIDADA LQILQDHAVR MEREARLIAA AELDEAAAHG TFFAPRAYEL KNLDQLHKEV
FGPVLHVIRW KGDQLDAVID QINATGYGLT LGVHSRIDET VDRISSRINV GNVYVNRNQI
GAVVGVQPFG GQGLSGTGPK AGGPHYLLRF ATEKTVTVNT TAAGGNASLL TLGD
//
