ID A0A1I1X486_9PROT Unreviewed; 1038 AA.
AC A0A1I1X486;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=SAMN05428977_10056 {ECO:0000313|EMBL:SFE02169.1};
OS Nitrosomonas sp. Nm166.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=1881054 {ECO:0000313|EMBL:SFE02169.1, ECO:0000313|Proteomes:UP000199102};
RN [1] {ECO:0000313|EMBL:SFE02169.1, ECO:0000313|Proteomes:UP000199102}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nm166 {ECO:0000313|EMBL:SFE02169.1,
RC ECO:0000313|Proteomes:UP000199102};
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; FONE01000005; SFE02169.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1X486; -.
DR STRING; 1881054.SAMN05428977_10056; -.
DR OrthoDB; 6187633at2; -.
DR UniPathway; UPA00261; UER00373.
DR Proteomes; UP000199102; 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 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000199102};
KW Repressor {ECO:0000256|PIRNR:PIRNR000197};
KW Transcription {ECO:0000256|PIRNR:PIRNR000197};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR000197}.
FT DOMAIN 11..58
FT /note="Proline utilization A proline dehydrogenase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18327"
FT DOMAIN 67..175
FT /note="Proline dehydrogenase PutA"
FT /evidence="ECO:0000259|Pfam:PF14850"
FT DOMAIN 185..477
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 559..1015
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT COILED 43..80
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 790
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
FT ACT_SITE 824
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 1038 AA; 114656 MW; 0330FFCE40767C6C CRC64;
MIHDTPFPSL TPSRAAINRS YLRDEAEHLD ALLPLIKLNE NEQVQVEELA RRLVNRVRSL
EQARNGIEAL LHEYDLSTEE GVLLMCLAEA LLRIPDAETA DRLIRDKLSS AEWSQHLGHS
ASWLVNASTW GLLLTGKFVK LETSSSHLDR LISRSGEPVI RVAIKQAMRL IGHQFVMGNT
IDEALTRSHD DENRRYRYSF DMLGEAALTR ADVVHYWDAY HHAIVTLGKQ VGEGELLAHP
GISVKLSALH PRYEYTQRQR VLEELSPRLL DLALAAKAAN ISMTIDAEEV ERLDLSLDLF
ETVYRNDKLS GWNGFGLAIQ AYQKRAVPII DWLAQLASEC NRQIPVRLVK GAYWDTEIKQ
AQERGLDGYP VFTRKAATDV SFLACARRLL ESNDLLYPQF ATHNARTVAT LIAMAGARSF
EFQRLHGMGE VLYNTVLDEY PQFNCRVYAP VGSYQELLPY LVRRLLENGA NSSFVNQIVN
ERHSVEEIIA DPVSQLEHQQ SHIPIPRHLY GEARLNSSGI NLADREAQRH LDQALEEASR
QSWHAAPIVD GKVLTGNAQA ILNPADHTDV IGEVSLADTS AADRALSVAH DAAPEWANSS
ANERAALLEQ AAALFEAERA EVMARIIREG GRTIHDAQNE VREAIDFCRY YAAQARHHFE
RPIALPGITG ETSQLQLAGR GVFICISPWN FPVSIFTGQI TAALAAGNSV IVKPAAFTPL
CAAYVIHLLH RAGIPQAVLH FVPGSGGEIG MKLVSDPRIA GVAFTGSTST ARQINQALAQ
NECILPFIAE TGGQNCMIVD SSALPEQVVK DVTASAFNSA GQRCSALRVL FLQQEIAPQI
LEMLSGAMDE LHIGNPMRLS TDIGPLISLS ARDDLQRHSE RMNNEARLIK IMQLPQGNEQ
GSYFSPRVYE IEKLSQLQHE VFGPILHVIR YQASRLNAVV EAINNSGYGL TLGIHSRIDT
TIDYITRHVR CGNTYVNRNI IGAVVGSQPF GGEGLSGTGP KAGGPHYLQR FATERVVTVN
TAAVGGNTDL LSFREMKS
//
