ID A0A3M6R0K9_9BURK Unreviewed; 1299 AA.
AC A0A3M6R0K9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=D8I35_06760 {ECO:0000313|EMBL:RMX08741.1};
OS Corticibacter populi.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Corticibacter.
OX NCBI_TaxID=1550736 {ECO:0000313|EMBL:RMX08741.1, ECO:0000313|Proteomes:UP000278006};
RN [1] {ECO:0000313|EMBL:RMX08741.1, ECO:0000313|Proteomes:UP000278006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 105136 {ECO:0000313|EMBL:RMX08741.1,
RC ECO:0000313|Proteomes:UP000278006};
RA Bernier A.-M., Bernard K.;
RT "Draft genome of Cortibacter populi DSM10536.";
RL Submitted (OCT-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RMX08741.1}.
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DR EMBL; RDQO01000001; RMX08741.1; -; Genomic_DNA.
DR OrthoDB; 6187633at2; -.
DR UniPathway; UPA00261; UER00373.
DR Proteomes; UP000278006; Unassembled WGS sequence.
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; 1.10.1220.10; Met repressor-like; 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; IPR013321; Arc_rbn_hlx_hlx.
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 InterPro; IPR048798; PutA_RHH.
DR InterPro; IPR010985; Ribbon_hlx_hlx.
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 Pfam; PF21775; PutA_1st; 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 SUPFAM; SSF47598; Ribbon-helix-helix; 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:UP000278006};
KW Repressor {ECO:0000256|PIRNR:PIRNR000197};
KW Transcription {ECO:0000256|PIRNR:PIRNR000197};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR000197}.
FT DOMAIN 11..42
FT /note="PutA RHH"
FT /evidence="ECO:0000259|Pfam:PF21775"
FT DOMAIN 89..134
FT /note="Proline utilization A proline dehydrogenase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18327"
FT DOMAIN 144..254
FT /note="Proline dehydrogenase PutA"
FT /evidence="ECO:0000259|Pfam:PF14850"
FT DOMAIN 264..564
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 656..1097
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 878
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
FT ACT_SITE 912
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 1299 AA; 139549 MW; D8AD9AFB245D6554 CRC64;
MATTTIGIKV DEQIRDRLRD AAQQLGCSPH WLHKQAVLGY IESIEKGLLP ADLGHWGGAL
AATEDGGGAA LVESSAPFYA FAQEVQPQSV LRAAITAAYR RPETECLPML VGLARNPQPE
AVKVLASRLV EALRERRQKK SGGVEALVQE YSLSSQEGVA LMCLAEALLR IPDRATRDAL
IRDKVSRGDW RAHADSPSMF VNAATWGLML TGKLVAVHSE KTLGAALTRL IARGGEPLIR
QGVNTAMRMM GEQFVTGQTI AAALANSRKL EEKGFRYSYD MLGEAATTEE DALRYMQAYE
QAIHAIGKAS QGRGIYEGPG ISIKLSALHA RYARAQRERV MAELYPRLLA LAQLARQYDI
GLNIDAEEAD RLELSLDLLE HLCLEPALAG WNGIGFVVQA YQKRAPFVLD WIIDLARRSR
HRLMVRLVKG AYWDSEIKRA QIDGLEGYPV HTRKVHTDVS YLACARKLLA VPDAVFPQFA
THNAQTLASI YQMAGQNYYA GQYEFQCLHG MGEPLYDAVV GPVAEGRLGR PCRIYAPVGS
HETLLAYLVR RLLENGANTS FVHQIGDASM PIERLVADPV EVALALQPLG RPHDRIPLPR
ALYEAQGRLN SAGLDLSNEQ RLASLSAALL GSVDVRWTAQ PTVPGQASSA APLTWQEVRN
PADRYDVIGQ VCLADEGQLR QAIAEAGRAA PIWQATPVAE RAEALLRAAQ LLQDQMQPLM
GLLVREAGKT YANAIAEVRE AIDFLRYYAQ QARATLANDS HRPLGLVACI SPWNFPLAIF
TGQVAAALAA GNAVIAKPAE QTNLIAAQAV ALLHQAGIPA GVLQLLPGAG ETVGAALVAD
PAVKGVVFTG STEVARLINR TLAARLDDAG KPIPLIAETG GINAMIVDSS ALAEQVVADV
LSSAFDSAGQ RCSALRLLCV QDDCADRLLG MLEGAMRQLR VGNPDQLATD VGPVIDAQAQ
AGIEAYVEQM RAAGHRVQRL TLEPACRQGI FVAPTLIEVA RVEDVTREVF GPVLHVLRYR
RSGIDALVDA INALGYGLTF GVHTRLDETV AHLTGRIQAG NHYVNRNIVG AVVGVQPFGG
EGLSGTGPKA GGPLYLHRLL ADAPALAQLP APSRADADGV LRVAAGASLV LDGPTGELNS
YALLPRGRIW CLPQSVEGLL RQWQTCALGG NRMVLADTPE NRRLAQEAAV QDAALPERLD
WRPVDGLLTN APAAAAGGVD ETMQDDVQAV LFEGDADALL ALQQQLAARR EGALLGVQGL
THEEIRQGRP YRHERLLREV ATSVNTAAAG GNASLMMVG
//
