ID A0A1S6EZX8_9CAUL Unreviewed; 1042 AA.
AC A0A1S6EZX8;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=BZG35_16050 {ECO:0000313|EMBL:AQR63587.1};
OS Brevundimonas sp. LM2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=1938605 {ECO:0000313|EMBL:AQR63587.1, ECO:0000313|Proteomes:UP000189107};
RN [1] {ECO:0000313|EMBL:AQR63587.1, ECO:0000313|Proteomes:UP000189107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LM2 {ECO:0000313|EMBL:AQR63587.1,
RC ECO:0000313|Proteomes:UP000189107};
RA Hentchel K., Vargas G., Fiebig A., Chen S.L., Coleman M., Crosson S.;
RT "Genome sequences of bacteria isolated from the littoral zone of southern
RT Lake Michigan.";
RL Submitted (JAN-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}.
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DR EMBL; CP019508; AQR63587.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S6EZX8; -.
DR STRING; 1938605.BZG35_16050; -.
DR KEGG; brl:BZG35_16050; -.
DR UniPathway; UPA00261; UER00373.
DR Proteomes; UP000189107; Chromosome.
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 68..181
FT /note="Proline dehydrogenase PutA"
FT /evidence="ECO:0000259|Pfam:PF14850"
FT DOMAIN 190..481
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 567..1025
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 799
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
FT ACT_SITE 833
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 1042 AA; 110924 MW; 9D6A2C8BAE22D130 CRC64;
MPPVAGLRPA LSQDWDTLDH GKFADEPTRL AGLLAAATLD GPTRAAVVAD AVALVEHARL
SQKKQGVVES FLQEFSLGTR EGLALMCLAE ALLRTPDEDT RDRLIAEKIG SADWASHLGQ
SDSLFVNAST WGLMLTGRLV DADEQAKRDL PGFLTRVAGR LGEPVIRQAV AAAVRIMGEQ
FVVGRTIEAA LKRSNKEGWL CSFDMLGEGA RTAADAERYE KIYADAITAV GKTAKGQGPE
VGHGVSVKLS ALSPRYEATH EDRVWTELYP RVLRLARIAA AADINFTMDA EEADRLALSL
KLLDRLAHEP SLGDWTGLGL AVQAYQKRGP EVIARVADLA RASGRRLMVR LVKGAYWDTE
IKRAQVMGRT DYPVFTTKAA TDLNYLVCAR AMIDAAPHLY SQFATHNAHS LAAVHRMAKD
AGVKIEFQRL HGMGEALYEA AAETFGPMIV RAYAPVGGHE DLLPYLVRRL LENGANSSFV
HALLDERVPA SAVAADPIAV VELAPDRHAR IPPPKDMYMD RQNSLGRDYS QKADRERHAA
ALSRVDAERF LSGPLIEGGL AAGENPRDVT NPWDRTQVIG RVSEATTEDV DHAVDRAQRA
QVAWDRAGGS RRAPVLRAMA DALEADMDRL VALLCREAGK TLNDGVAEVR EAADFCRYYA
MLAEKDFGGP VSLAGPVGET NRLVLHGRGV FACISPWNFP LAIFTGQIAA ALAAGNAVLA
KPAEQTPLIA AEAVRLFHAA GLDADLLALV PGRGETVGAA LVSHPGIDGV AFTGGTDTAA
AINRAIAARP GPILPFIAET GGLNGMFVDT TALREQVIDD VIGSAFGSAG QRCSALRILY
VPRDSADSVI EGLKGALAAQ VVGDPADPST DIGPVIDTES RQALEAHIGR LTRDARILAR
AAMPTGAERG DLFAPTIAEI PTPDYLEREV FGPILHIYRY DPADLKSVAG KLAARGYGLT
LGVHSRIEAF AEEVVSLVPA GNVYINRGVT GAVVGVQPFG GEGLSGTGPK AGGPNSLIRY
ASEKAISNNI SAQGGDPALL NL
//
