ID A0A1H0RDV6_9BRAD Unreviewed; 1202 AA.
AC A0A1H0RDV6;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=SAMN05444050_6332 {ECO:0000313|EMBL:SDP27550.1};
OS Afipia sp. GAS231.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Afipia.
OX NCBI_TaxID=1882747 {ECO:0000313|EMBL:SDP27550.1, ECO:0000313|Proteomes:UP000198617};
RN [1] {ECO:0000313|EMBL:SDP27550.1, ECO:0000313|Proteomes:UP000198617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GAS231 {ECO:0000313|EMBL:SDP27550.1,
RC ECO:0000313|Proteomes:UP000198617};
RA de Groot N.N.;
RL Submitted (OCT-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; LT629703; SDP27550.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0RDV6; -.
DR STRING; 1882747.SAMN05444050_6332; -.
DR OrthoDB; 9812625at2; -.
DR UniPathway; UPA00261; UER00373.
DR Proteomes; UP000198617; Chromosome i.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000198617};
KW Repressor {ECO:0000256|PIRNR:PIRNR000197};
KW Transcription {ECO:0000256|PIRNR:PIRNR000197};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR000197}.
FT DOMAIN 17..64
FT /note="Proline utilization A proline dehydrogenase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18327"
FT DOMAIN 72..183
FT /note="Proline dehydrogenase PutA"
FT /evidence="ECO:0000259|Pfam:PF14850"
FT DOMAIN 193..490
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 571..1005
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 790
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
FT ACT_SITE 824
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 1202 AA; 128674 MW; 0679EADB7863F9B6 CRC64;
MANTFSFEGF APPLTSTPLR QRITRAYRLP EIECVPPLIE AAALPAEVRD AAAATARSLI
EALRSTSQPR GVAALVHEFS LSSREGVALM CLAEALLRIP DADTRDAIIR DKVAPGNWKA
HIGGERSLFV NAAVWGLVVT GKLTSPVEPN SLAGALTRVV QRCGEPVIRK SVEIAMRTMG
EQFVLGQTID EALANARQRE LEGFTYSYDM LGEAAMTSAD ADRYFYDYER AIHAIGKAAA
GRSVLASPGI SIKLSALHPR YVRSQAQRVM KELLPRVRQL TVLARSYGIG LNIDAEEADR
LELSLDLLEA LALDPELRDW DGLGFVVQAY GKRCPFVIDW IVDLARRAGR RIMVRLVKGA
YWDAEIKRAQ VEGLADFPVY TRKIHTDVAY IACARKLLAA REHVYPQFAT HNAQTVATLY
HMAGQGYAAG DYEFQCLHGM GEPLYSAVVP DNALARPCRI YAPVGTHATL LAYLVRRLLE
NGANSSFVNQ VADPAISVDQ LIADPVKVAS SMPIIGAMHD AIALPERLYP GRKNSRGLDL
TDEATLAAVS KVLAHSATRK WIAGSATGQS RIILNPADHR DEVGIVFEAS EADAEAAVAR
AVKSRWSGVP VAERADVLGR AADLLESRME ELLGLIMREA GKSLANAVGE VREAVDFLRY
YAGQGRVTLN TSQHRPVGPV AAISPWNFPL AIFTGQVAAA LMAGNPVIAK PAEETPLIAA
QAVAILHEAG VHPDALQLVP GDGTIGAALV AASEIAAVIF TGSTEVARII QLTLAGRLSK
DGAPIPLIAE TGGQNVMIVD SSALTEQVVV DVLASAFDNA GQRCSALRIL CVQEEVAERT
LEMLMGAVAE LSIRPTNRLS ADVGPIISAE ARDTIERHVE RMRALGCRIE RATVASEAGN
GTFVPPTIIE IKGLDVLERE VFGPVLHILR YRRDDLDTLL DQINATGYAL TFGLHTRLDE
TIEAVTGRID AGNIYVNRNM VGAVVGVQPF GGHGLSGTGP KAGGPLYLGR LVNGRSLDIG
QGTEDAALAD FRAWLLDRGE IATSEIAANH AQRTPFGLKL LLAGPVGEEN AYRICGRGAI
LLKPCTRTGL LRQLSAVLAT GNTAVVEASW LKDLHGLPSS VASRICTEGP AIAAVLVESD
RPSLMHTMKQ IASRPGPLVP VQSRSVDGEG ADDYRLDWLV HEVSVSTNTA ASGGNASLMA
IA
//
