ID A0A1Y5SFE9_9RHOB Unreviewed; 1157 AA.
AC A0A1Y5SFE9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-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:SLN36727.1};
GN ORFNames=PSA7680_01776 {ECO:0000313|EMBL:SLN36727.1};
OS Pseudoruegeria aquimaris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Pseudoruegeria.
OX NCBI_TaxID=393663 {ECO:0000313|EMBL:SLN36727.1, ECO:0000313|Proteomes:UP000193409};
RN [1] {ECO:0000313|EMBL:SLN36727.1, ECO:0000313|Proteomes:UP000193409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7680 {ECO:0000313|EMBL:SLN36727.1,
RC ECO:0000313|Proteomes:UP000193409};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-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; FWFQ01000010; SLN36727.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5SFE9; -.
DR OrthoDB; 9812625at2; -.
DR UniPathway; UPA00261; UER00373.
DR Proteomes; UP000193409; 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 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; 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:UP000193409};
KW Repressor {ECO:0000256|PIRNR:PIRNR000197};
KW Transcription {ECO:0000256|PIRNR:PIRNR000197};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR000197}.
FT DOMAIN 4..51
FT /note="Proline utilization A proline dehydrogenase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18327"
FT DOMAIN 59..168
FT /note="Proline dehydrogenase PutA"
FT /evidence="ECO:0000259|Pfam:PF14850"
FT DOMAIN 177..470
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 554..987
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 766
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
FT ACT_SITE 800
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 1157 AA; 122636 MW; 005CCBB54FDF9021 CRC64;
MPLSPLRDRI RALHFAEEDG LLARLQQEAQ IGESLRAKAH ARAVSLVEDI RGRADPGLME
VFLAEYGLST KEGIALMCLA EALLRVPDSE TVDALIEDKI APSAWGEHLG HSSSHLVNAS
TWALMLTGKV LSDGQGLASV LRGAIRRLGE PVIRVAVGRA MREMGHQFVL GETIESALKR
GAARVAQGFT YSYDMLGEAA LTARDADAFF TAYAEAITAL APHCASEDIR ENPGISVKLS
ALYPRYEFTQ HERVMADLVP RLRELAKMAA NAGMGFNIDA EEADRLDLSL DVIEAVLKEP
ALEGWEGFGV VVQAYGKRAG AVLDWLHALA ETLDRRIMVR LVKGAYWDTE IKRAQAEGLP
GFPVFTRKVA TDVAYLCNAR KLLGMTDRIY PQFATHNAHT VAAILEMAED LQAFEFQRLH
GMGEALHDIV KAQAGTRCRI YAPVGAHRDL LAYLVRRLLE NGANSSFVNQ IVDESVPAAA
VAADPFEALA AAGRNAAVVP PADLFRPERR NSRGWDVNDP LHAGQIEAAR APYAQKAYAV
TPLLADGLAQ EGGETLEIRN PARPEDRLGT ALCVTPALAA QAVEAARPWA APVAERRAVL
ERAADLYEAR HGEIFALLAR EAGKTWRDAI AELREAVDFL RYYAARAEQE PNGPLGTVTC
ISPWNFPLAI FTGQIAAALA TGNAVLAKPA ETTNAIAFLA MRLLHEAGVP RAALQLLPGT
GREIGPVLTG TPGVGGVCFT GSTATAQGIN RVMAARLAPC APLIAETGGL NAMIVDSTAL
PEQAVRDIVA SAFQSAGQRC SALRLLYVQE DVAPAIRKML FGAMDALRIG DPWQAATDVG
PVISAEAKAG IEAHVAAAKA EGRLLKQLRP PQQGTFVGPA VIEVSGMADL TREIFGPVLH
IATFRAEELD RVVEEINASG YGLTFGVHSR IDSRVDALVR KIRVGNIYVN RNQIGAVVGS
QPFGGEGLSG TGPKAGGPAY LARFTRPESA PAAEAGPAGG TVEVGAVQAA IDDAGRQGGL
LLRTESLPGP TGESNRLSVF GRGTVLCLGP GLAAAQEQAR IARAEGCAAV VVAPGAALDG
HLAPEALEHL AGVSVVAFWG DEQEARAYRQ ALARRDGPMI PLVTATDLPA RCRLERHVCV
DTTAAGGNAA LLASAGA
//
