ID A0A2A3LM58_9GAMM Unreviewed; 1070 AA.
AC A0A2A3LM58;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=CMZ84_06230 {ECO:0000313|EMBL:PBJ84050.1};
OS Xanthomonadaceae bacterium NML93-0399.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae.
OX NCBI_TaxID=2032565 {ECO:0000313|EMBL:PBJ84050.1, ECO:0000313|Proteomes:UP000218035};
RN [1] {ECO:0000313|EMBL:PBJ84050.1, ECO:0000313|Proteomes:UP000218035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML93-0399 {ECO:0000313|EMBL:PBJ84050.1,
RC ECO:0000313|Proteomes:UP000218035};
RA Bernier A.-M., Bernard K.;
RT "Clinical and environmental strains of Xanthomonadaceae.";
RL Submitted (SEP-2017) 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:PBJ84050.1}.
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DR EMBL; NTJI01000001; PBJ84050.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A3LM58; -.
DR OrthoDB; 9812625at2; -.
DR UniPathway; UPA00261; UER00373.
DR Proteomes; UP000218035; 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 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 27..73
FT /note="Proline utilization A proline dehydrogenase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18327"
FT DOMAIN 82..195
FT /note="Proline dehydrogenase PutA"
FT /evidence="ECO:0000259|Pfam:PF14850"
FT DOMAIN 205..506
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 591..1052
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 825
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
FT ACT_SITE 859
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 1070 AA; 114551 MW; E02A6BF3C9F0B7C5 CRC64;
MPLLSPAGRP ALNASPSHAV PAASLQPLRA AITAAWTGDE TSRVQALLAE ARQPDADRAA
IQAAAADLVR RVRLRARDRG AIEAFMQQYD LGSEEGALLM CVAEALLRIP DEGTADALIR
DKLGEANWRK HMGQSDSVLV NASTWGLMLT GHLVDLADET KRNVHGAFKR LVGRVGEPVI
RLAVRQAMRI MGHQFVMGRT ISEALARSRK GDNAAYRYSF DMLGEAALTQ RDADRYLKAY
QDAIDAIGRS GTFDDEIGAP SISVKLSALH PRYEHAKHAR VIAELAPRLL DLAQRAKAHR
IGLTVDAEES DRLELSLDVI EAALTDASLA GWNGFGIVVQ AYQKRAPFVI DWIAALARMH
GRRIPVRLVK GAYWDSEVKR AQVEGHPGYP VFTRKPNTDV SYLANARRLL SASDAIYPMF
ATHNAHTIAA VHRLAQTVLP GRVARTAYEF QKLHGMGDDL YAEVIPADRL DVACRVYAPV
GSHEDLLPYL VRRLLENGAN SSFVNRISDE DVAIDDLIRD PVDVVSGFES IPHPRIPLPV
DLYRSQSHDR SNSMGVNLAN DAQLEALAEQ IRSATTTWSA TPLVPGAQPT GEKVVVNSPA
DRRVHVGDWL PADSATVERA LDNATAAHAD WNATPAASRA AILEHAADVL ESRTAQFIAM
CTREAGKTIP DGVAEVREAV DFLRYYAGEA RRLFVDEALP GPTGESNTLQ LSGRGVFVCI
SPWNFPLAIF AGQIAASLAA GNTVIAKAAE QTTLVGFEAV KLLHEAGIPK NVLQYVPGDG
ASVGAALTGD ARVAGVVFTG SNATALAINR ALAARDGAIG TLIAETGGQN ALIADSSALP
EQLVKDALGS AFTSAGQRCS AARVLFVQDD IADKVLDMLA GAMAELKVGD PALLSTDVGP
VIDADALRML DAHAERMANE ARLIATTPVG EDAAHGTFFA PRAWELQSLS QLQRENFGPA
LHVIRWKAEQ LDAVLDAINS TGYGLTLGIH SRIDETVEKI TARARVGNVY VNRNQIGAVV
GVQPFGGQRL SGTGPKAGGP HYLPRFTTEK TVTINTTAAG GNASLLTLGE
//
