ID F4QLJ6_9CAUL Unreviewed; 1042 AA.
AC F4QLJ6;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, 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=ABI_19340 {ECO:0000313|EMBL:EGF93494.1};
OS Asticcacaulis biprosthecium C19.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=715226 {ECO:0000313|EMBL:EGF93494.1, ECO:0000313|Proteomes:UP000006512};
RN [1] {ECO:0000313|Proteomes:UP000006512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C19 {ECO:0000313|Proteomes:UP000006512};
RA Brown P.J.B., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Draft genome sequence of Brevundimonas diminuta.";
RL Submitted (MAR-2011) 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; GL883077; EGF93494.1; -; Genomic_DNA.
DR RefSeq; WP_006272692.1; NZ_GL883077.1.
DR AlphaFoldDB; F4QLJ6; -.
DR STRING; 715226.ABI_19340; -.
DR eggNOG; COG0506; Bacteria.
DR eggNOG; COG4230; Bacteria.
DR HOGENOM; CLU_005682_1_0_5; -.
DR OrthoDB; 9812625at2; -.
DR UniPathway; UPA00261; UER00373.
DR Proteomes; UP000006512; 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; 1.20.5.460; 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; 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 71..184
FT /note="Proline dehydrogenase PutA"
FT /evidence="ECO:0000259|Pfam:PF14850"
FT DOMAIN 193..483
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 568..1023
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 800
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
FT ACT_SITE 834
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 1042 AA; 112015 MW; 8AE4CE36C6E63E7E CRC64;
MPDASPARTS APVQVFDWDS LDDHKYLSDA DICARLLRDN PLDDETRAVV RAEAESLVRA
TRKAAQRQGV VESFLKEFSL GTREGLALMC LAEALLRVPD EATRDQLIAE KISAADWASH
LGHSDNWFVN ASTWGLMLTG KIIDVEDKAK TDLGGYLAGL TQRMGEPVIR AAVAQAIRIM
GEQFVLGRTI EDALKRSKKE GYLCSFDMLG EGARTEHDAV RYAQAYADAI TALSKVAKGG
PEADHGISVK LSALYSRYEA AKAADVFEHL YPRVKALAIQ AAKADINFTL DAEETDRLAL
SLKVLDRLAH EPELGEWKGL GLAVQAYQKR CPEVITALRH LAEVSGRRLM VRLVKGAYWD
TEIKRAQVYG REDYPVHTTK AATDLSYLVC AKALIDAAPY IYSQFATHNA HSLAAVRRMA
NAKGVKVEFQ RLHGMGEQLY AEALDQFEPF PLRAYAPVGG HEDLLPYLVR RLLENGANSS
FVNALLDERI RPADVISDPV VKVMAHPNRH ARLPSPRDMY GDRLNSHGPD ISIAKVRQRL
TAAVTALDKD PKDANALIGG KPHSTYAAHV YAPADLTRIV GEVHDADPAM ITEAFDRATA
AQPAWNALGG DGRAKVLEAM ADALEDRHDK LCAILVREAG KTWGDAISEV REAADFCRFY
AKLAREQFAG PQILTGPVGE RNSHELHGRG VFVCISPWNF PLAIFTGQIA AALAAGNAVL
AKPAEQTPLI AQKAVKLFYG AGLKPDLLAL LPGGGASVGA ALVAHPGIAG VAFTGGTDTA
RMINKTLAGK EGPIVPFIAE TGGLNGMFVD TTALREQVVD DVIASAFGSA GQRCSALRLL
FLPSELADDY IATLKGAMDQ LHLGDPAQFD VDVGPVIDAD ALEMLNLHLD ALTERGQVLH
RAPLPDGLNG HFFAPVLAEI SGPQELAREV FGPILHIVRY DSQNPEAMTN ALKSSGYGLT
LGVHSRLEAF AERIMQAVPA GNVYVNRTVI GAVVGVQPFG GEGLSGTGPK AGGPLSLSRF
ASERAVSVNI TAQGGDPALL NL
//
