ID   F5Y611_RAMTT            Unreviewed;      1019 AA.
AC   F5Y611;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 61.
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   Name=putA {ECO:0000313|EMBL:AEG91515.1};
GN   OrderedLocusNames=Rta_04440 {ECO:0000313|EMBL:AEG91515.1};
OS   Ramlibacter tataouinensis (strain ATCC BAA-407 / DSM 14655 / LMG 21543 /
OS   TTB310).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Ramlibacter.
OX   NCBI_TaxID=365046 {ECO:0000313|EMBL:AEG91515.1, ECO:0000313|Proteomes:UP000008385};
RN   [1] {ECO:0000313|Proteomes:UP000008385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-407 / DSM 14655 / LMG 21543 / TTB310
RC   {ECO:0000313|Proteomes:UP000008385};
RA   Barakat M., Ortet P., De Luca G., Jourlin-Castelli C., Ansaldi M., Py B.,
RA   Fichant G., Coutinho P., Voulhoux R., Bastien O., Roy S., Marechal E.,
RA   Henrissat B., Quentin Y., Noirot P., Filloux A., Mejean V., DuBow M.,
RA   Barras F., Heulin T.;
RT   "Genome of the cyst-dividing bacterium Ramlibacter tataouinensis.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEG91515.1, ECO:0000313|Proteomes:UP000008385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-407 / DSM 14655 / LMG 21543 / TTB310
RC   {ECO:0000313|Proteomes:UP000008385};
RX   PubMed=21912644; DOI=10.1371/journal.pone.0023784;
RA   De Luca G., Barakat M., Ortet P., Fochesato S., Jourlin-Castelli C.,
RA   Ansaldi M., Py B., Fichant G., Coutinho P.M., Voulhoux R., Bastien O.,
RA   Marechal E., Henrissat B., Quentin Y., Noirot P., Filloux A., Mejean V.,
RA   Dubow M.S., Barras F., Barbe V., Weissenbach J., Mihalcescu I.,
RA   Vermeglio A., Achouak W., Heulin T.;
RT   "The Cyst-Dividing Bacterium Ramlibacter tataouinensis TTB310 Genome
RT   Reveals a Well-Stocked Toolbox for Adaptation to a Desert Environment.";
RL   PLoS ONE 6:E23784-E23784(2011).
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; CP000245; AEG91515.1; -; Genomic_DNA.
DR   RefSeq; WP_013899748.1; NC_015677.1.
DR   AlphaFoldDB; F5Y611; -.
DR   STRING; 365046.Rta_04440; -.
DR   KEGG; rta:Rta_04440; -.
DR   PATRIC; fig|365046.3.peg.459; -.
DR   eggNOG; COG0506; Bacteria.
DR   eggNOG; COG4230; Bacteria.
DR   HOGENOM; CLU_005682_1_0_4; -.
DR   OrthoDB; 6187633at2; -.
DR   UniPathway; UPA00261; UER00373.
DR   Proteomes; UP000008385; 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   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; 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   PIRSF; PIRSF000197; Bifunct_PutA; 2.
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   Reference proteome {ECO:0000313|Proteomes:UP000008385};
KW   Repressor {ECO:0000256|PIRNR:PIRNR000197};
KW   Transcription {ECO:0000256|PIRNR:PIRNR000197};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR000197}.
FT   DOMAIN          57..162
FT                   /note="Proline dehydrogenase PutA"
FT                   /evidence="ECO:0000259|Pfam:PF14850"
FT   DOMAIN          178..490
FT                   /note="Proline dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF01619"
FT   DOMAIN          562..1000
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        778
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
FT   ACT_SITE        812
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ   SEQUENCE   1019 AA;  107556 MW;  7F8D30BDE50E5C65 CRC64;
     MDTPAADRLP SPYRPEAAVL ADRLRRLEGA LDWAAAAAAA APWVQAVRRH PPPFWAMESL
     LKEYPISSAE GLALMRLAEA LLRVPDAETA VALTADQLGR ADFSGAADGA LARLSNAAIA
     LSKKLLPEQA DAPDGGGLLA RLGARTVVAA TLRAVQLLGR QFVLGQDIGA ALDEADAARR
     AQPALLFSYD MLGEGARTAH DAERYLASYR AAIAAIAARG DAARAPAESD GISIKLSALH
     PRYEEAQRER VLRELVPRVW QLCEQAARSN LNLTIDAEEV DRLELSLAVF EALAESVAQR
     HPRWSGFGLA LQSYQTRALE LIEHVADLAR RLGLRFMCRL VKGAYWDAEI KRAQELGLPH
     YPVFTHKQHT DVSYLACARA LLQAADAIYP QFATHNAGTI AAIRQMAERE GAAFELQRLH
     GMGEGVYREI LSRYTPSGQA GLAPTQPPPS GGGFEPRVRV YAPVGKHRDL LAYLVRRLLE
     NGANSSFVHQ LADESVGLDQ LLASPLAQAR ASLARLAQQP ALPLPAGLYG PGRRNSAGLD
     LAVAAMRAPL LAAHAQLRVP PVAQAQAGEA PAAVARAAAA FPAWDARPVA ERAQALRRAA
     DAMEARMAPL CALLVAEGRK TWGDAVAEVR EAVDFLRYYA GEAERVMQPA LLPGPTGERN
     ELRLAGRGPW VCISPWNFPL AIFTGQVAAA LAAGNTVLAK PAEQTPAVAR EAVRLLHEAG
     VPPDALQLLH GPGETVGAAL VAAPGVAGVV FTGSTQVARL IQRALAAKDG AIVPLIAETG
     GINAMLVDST ALPEQVADAV VQSAFRSAGQ RCSALRLLCV HEGIADAVIE MVAGAARELT
     VGDPALLSTD VGPVIDAQAF AGLQGELQRL RQTARAVLAP AEAPAAPPHC IAPQAFEVER
     VTDVQREIFG PVLHIARWSG DPQAVVEQVN ALGYGLTLGI QTRIDSRAQA LAARARVGNV
     YVNRNMIGAV VGVQPFGGEG LSGTGPKAGG PHYLPRFCAE RTLTVNTAAA GGNVALLAG
//