ID A0A1S8D8B6_9PROT Unreviewed; 1228 AA.
AC A0A1S8D8B6;
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 Name=putA {ECO:0000313|EMBL:ONH83595.1};
GN ORFNames=APZ41_008690 {ECO:0000313|EMBL:ONH83595.1};
OS Roseomonas mucosa.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Roseomonas.
OX NCBI_TaxID=207340 {ECO:0000313|EMBL:ONH83595.1, ECO:0000313|Proteomes:UP000054844};
RN [1] {ECO:0000313|EMBL:ONH83595.1, ECO:0000313|Proteomes:UP000054844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAVE376 {ECO:0000313|EMBL:ONH83595.1,
RC ECO:0000313|Proteomes:UP000054844};
RA Choudhury M.A., Sidjabat H.E., Wailan A.M., Zhang L., Marsh N.M.,
RA Rickard C.M., Davies M., Mcmillan D.J.;
RT "Draft genome sequence of Roseomonas mucosa strain AU37, isolated from a
RT peripheral intravenous catheter.";
RL Submitted (DEC-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}.
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:ONH83595.1}.
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DR EMBL; LLWF02000021; ONH83595.1; -; Genomic_DNA.
DR RefSeq; WP_076970216.1; NZ_LLWF02000021.1.
DR AlphaFoldDB; A0A1S8D8B6; -.
DR STRING; 207340.APZ41_008690; -.
DR OrthoDB; 9812625at2; -.
DR UniPathway; UPA00261; UER00373.
DR Proteomes; UP000054844; 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 Reference proteome {ECO:0000313|Proteomes:UP000054844};
KW Repressor {ECO:0000256|PIRNR:PIRNR000197};
KW Transcription {ECO:0000256|PIRNR:PIRNR000197};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR000197}.
FT DOMAIN 29..75
FT /note="Proline utilization A proline dehydrogenase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18327"
FT DOMAIN 83..194
FT /note="Proline dehydrogenase PutA"
FT /evidence="ECO:0000259|Pfam:PF14850"
FT DOMAIN 204..501
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 590..1029
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 810
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
FT ACT_SITE 844
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 1228 AA; 129032 MW; B896F719DAA691A1 CRC64;
MSLAARLDMP SAAPIPFDAF AASVQAQGPL RAAITRHERA AEPGCIARLL PDATLPAPLA
ARAAATATRL VEALRRKGTR GAVEGLVQEF SLSSQEGVAL MCLAEALLRI PDTATRDALI
RDKIGGGDWR SHLGHSPSLF VNAATWGLVV TGRLATTSSE TGLSHALTRL IARGGEPVIR
KGVDLAMRMM GEQFVTGQTI AEALVRARKM EAKGFRYSYD MLGEAATTAA DAERYHRDYE
TAIHAIGQAA AGRGIYEGPG ISIKLSALHP RYARAQRDRV MAELLPRVAL LAGLAKRYDI
GLNIDAEEAD RLDLSLDILE ALCLDPALAG WDGLGFVVQA YQKRAPFVLD FVIDLARRSG
HRLMVRLVKG AYWDSEIKRA QIDGLEDFPV FTRKRHTDVS YLACARKLLE ARDAVFPQFA
THNAQTLASI HALAGEGFRI GDHEFQCLHG MGEPLYEEVV GPGKLDRPCR IYAPVGTHET
LLAYLVRRLL ENGANSSFVN RIQDPAVTVE ALAADPAAQV AAEQPPGAPN PHIALPCGLF
GAERANSLGL NLSNEAELAR LATALRDSAA QDWRAAPLLA GMKGQGLPRP VLNPANHRDR
VGMVVEASAE AVGSALHIAA EAAAAWAAEP PEARAACLSR AADLLEQRMP LLLGLLVREA
GKSFANAVAE VREAVDFLRY YGAQVRRDFR NGTHRPLGPV LCISPWNFPL AIFTGQVAAA
LAAGNPVIAK PAEETPLIAA QSVAILHEAG VPAGVLQLLP GDGQVGAALV ADARIHGVMF
TGSTEVARRI QAELAKRLNP GGAPVPLIAE TGGQNALVVD SSALAEQVVG DVLVSAFDSA
GQRCSALRVL CLQEDVADRV LAMLRGALAE LSTGNPERLS TDIGPVITGE ARDGILAHIE
AMRAAGYPVH QSALPEECRH GTFVPPTIIE IDSLEALTRE VFGPVLHVLR FRRDGIEALM
RAVNATGYGL TFGVHSRIDE TIQHVTALAR AGNVYVNRNL VGAVVGVQPF GGHGLSGTGP
KAGGPLYLRR LLAARPASTG LPAGTAPAPL RAPLRAWAAW LAGRGEAGAA AEAEALAAIT
PAGLALELPG PVGERNAYAT EPRGSVLCHA ADAATLHRAV SAALAAGNRA LIAAGGTRLG
APLPPALAAW VREAGPAALP EVQAVLFGGT EEALKALAQQ LASLDGPIVP VHVADAQTGF
PAEFLLLERS VSTNTAAAGG NAKLMMLG
//
