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Bifunctional protein PutA [Includes: Proline dehydrogenase (EC 1.5.5.2) (Proline oxidase); Delta-1-pyrroline-5-carboxylate dehydrogenase (P5C dehydrogenase) (EC 1.2.1.88) (L-glutamate gamma-semialdehyde dehydrogenase)]

 B9NWB1_9RHOB            Unreviewed;      1158 AA.
B9NWB1;
24-MAR-2009, integrated into UniProtKB/TrEMBL.
24-MAR-2009, sequence version 1.
12-SEP-2018, entry version 51.
RecName: Full=Bifunctional protein PutA {ECO:0000256|PIRNR:PIRNR000197};
Includes:
RecName: Full=Proline dehydrogenase {ECO:0000256|PIRNR:PIRNR000197};
EC=1.5.5.2 {ECO:0000256|PIRNR:PIRNR000197};
AltName: Full=Proline oxidase {ECO:0000256|PIRNR:PIRNR000197};
Includes:
RecName: Full=Delta-1-pyrroline-5-carboxylate dehydrogenase {ECO:0000256|PIRNR:PIRNR000197};
Short=P5C dehydrogenase {ECO:0000256|PIRNR:PIRNR000197};
EC=1.2.1.88 {ECO:0000256|PIRNR:PIRNR000197};
AltName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR000197};
ORFNames=RKLH11_3687 {ECO:0000313|EMBL:EEE36085.1};
Rhodobacteraceae bacterium KLH11.
Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
Rhodobacteraceae.
NCBI_TaxID=467661 {ECO:0000313|EMBL:EEE36085.1, ECO:0000313|Proteomes:UP000005135};
[1] {ECO:0000313|Proteomes:UP000005135}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=KLH11 {ECO:0000313|Proteomes:UP000005135};
PubMed=21742885; DOI=10.1128/JB.05556-11;
Zan J., Fricke W.F., Fuqua C., Ravel J., Hill R.T.;
"Genome Sequence of Ruegeria sp. Strain KLH11, an N-Acylhomoserine
Lactone-Producing Bacterium Isolated from the Marine Sponge Mycale
laxissima.";
J. Bacteriol. 193:5011-5012(2011).
-!- FUNCTION: Oxidizes proline to glutamate for use as a carbon and
nitrogen source. {ECO:0000256|PIRNR:PIRNR000197}.
-!- CATALYTIC ACTIVITY: L-glutamate 5-semialdehyde + NAD(+) + H(2)O =
L-glutamate + NADH. {ECO:0000256|PIRNR:PIRNR000197}.
-!- CATALYTIC ACTIVITY: L-proline + a quinone = (S)-1-pyrroline-5-
carboxylate + a quinol. {ECO:0000256|PIRNR:PIRNR000197}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000256|PIRNR:PIRNR000197};
-!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
glutamate; L-glutamate from L-proline: step 1/2.
{ECO:0000256|PIRNR:PIRNR000197}.
-!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
glutamate; L-glutamate from L-proline: step 2/2.
{ECO:0000256|PIRNR:PIRNR000197}.
-!- SIMILARITY: In the C-terminal section; belongs to the aldehyde
dehydrogenase family. {ECO:0000256|PIRNR:PIRNR000197}.
-!- SIMILARITY: In the N-terminal section; belongs to the proline
dehydrogenase family. {ECO:0000256|PIRNR:PIRNR000197}.
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EMBL; DS999532; EEE36085.1; -; Genomic_DNA.
RefSeq; WP_008758943.1; NZ_DS999532.1.
ProteinModelPortal; B9NWB1; -.
STRING; 467661.RKLH11_3687; -.
EnsemblBacteria; EEE36085; EEE36085; RKLH11_3687.
eggNOG; ENOG4105C26; Bacteria.
eggNOG; COG0506; LUCA.
eggNOG; COG4230; LUCA.
OrthoDB; POG091H043M; -.
UniPathway; UPA00261; UER00373.
UniPathway; UPA00261; UER00374.
Proteomes; UP000005135; Unassembled WGS sequence.
GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IEA:UniProtKB-UniRule.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
GO; GO:0004657; F:proline dehydrogenase activity; IEA:UniProtKB-UniRule.
GO; GO:0006561; P:proline biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0010133; P:proline catabolic process to glutamate; IEA:UniProtKB-UniRule.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.40.309.10; -; 1.
Gene3D; 3.40.605.10; -; 2.
InterPro; IPR016161; Ald_DH/histidinol_DH.
InterPro; IPR016163; Ald_DH_C.
InterPro; IPR016160; Ald_DH_CS_CYS.
InterPro; IPR016162; Ald_DH_N.
InterPro; IPR015590; Aldehyde_DH_dom.
InterPro; IPR025703; Bifunct_PutA.
InterPro; IPR005933; Delta1-pyrroline-5-COlate_DH-3.
InterPro; IPR029041; FAD-linked_oxidoreductase-like.
InterPro; IPR024089; PRODH_PutA_dom_I/II.
InterPro; IPR024082; PRODH_PutA_dom_II.
InterPro; IPR002872; Proline_DH_dom.
Pfam; PF00171; Aldedh; 1.
Pfam; PF01619; Pro_dh; 1.
Pfam; PF14850; Pro_dh-DNA_bdg; 1.
PIRSF; PIRSF000197; Bifunct_PutA; 1.
SUPFAM; SSF51730; SSF51730; 1.
SUPFAM; SSF53720; SSF53720; 1.
SUPFAM; SSF81935; SSF81935; 1.
TIGRFAMs; TIGR01238; D1pyr5carbox3; 1.
PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000005135};
DNA-binding {ECO:0000256|PIRNR:PIRNR000197};
FAD {ECO:0000256|PIRNR:PIRNR000197};
Flavoprotein {ECO:0000256|PIRNR:PIRNR000197};
NAD {ECO:0000256|PIRNR:PIRNR000197};
Oxidoreductase {ECO:0000256|PIRNR:PIRNR000197,
ECO:0000313|EMBL:EEE36085.1};
Proline metabolism {ECO:0000256|PIRNR:PIRNR000197};
Reference proteome {ECO:0000313|Proteomes:UP000005135};
Repressor {ECO:0000256|PIRNR:PIRNR000197};
Transcription {ECO:0000256|PIRNR:PIRNR000197};
Transcription regulation {ECO:0000256|PIRNR:PIRNR000197}.
DOMAIN 60 169 Pro_dh-DNA_bdg.
{ECO:0000259|Pfam:PF14850}.
DOMAIN 183 472 Pro_dh. {ECO:0000259|Pfam:PF01619}.
DOMAIN 555 986 Aldedh. {ECO:0000259|Pfam:PF00171}.
ACT_SITE 766 766 {ECO:0000256|PIRSR:PIRSR000197-1}.
ACT_SITE 800 800 {ECO:0000256|PIRSR:PIRSR000197-1,
ECO:0000256|PROSITE-ProRule:PRU10008}.
SEQUENCE 1158 AA; 123496 MW; 342B20EEB4D5FD32 CRC64;
MTGLSTLRHD IRDNHLRDEG TILRELMARA AISAPVRASA HNRAVSLIQA IRSDDTPGLM
EVFLAEYGLS TSEGVALMCL AEALLRVPDE DTIDALIEDK IAPSAWGQHL GNSSSSLVNA
STWALMLTGK VLQEGSGVAA TLKSAVKRLG EPVIRAAVGR AMKEMGAQFV LGQTIAEAIQ
QGRTKEEQGY TYSYDMLGEA ALTAADAAGF FVAYQDAISA LAKECRSTDI RENPGISIKL
SALHPRYEVG QKDRVMDELV PLTLKLAQQA KDAGMGLNID AEEADRLDLS LDVIEAVLRD
PSLAGWDGFG VVVQAYGKRA SQVLDWLHAL TTQLDRKIMV RLVKGAYWDT EIKRAQVEGL
GGFPVFTRKA ATDVSYICAA KQLLGMSDRI YPQFATHNAH TVAAILEMAG DTKRSFEFQR
LHGMGESLHD LVLESEGTRC RIYAPVGAHR DLLAYLVRRL LENGANSSFV NQIVDESVPP
ETIAYDPFES IATPEPHMAV RMPADLYGAE RPNARGWDLH DVTDLDQIKQ ARHPFQAETW
EIGPVIAGEV VGDRVLDVIN PANHSDQLGT ALQASAEDME TALNVAARWD ATAATRGDIL
RKAADLYEEN FGEIFAALTR EAGKTPMDAI SELREAVDFL RYYAARAAGL IHPARGVVAC
ISPWNFPLAI FTGQIAAALA AGNGVIAKPA QPTAIIASIG VRLLHAAGVP RTALQLIPGR
GSVVGAKMTS DPRINGVCFT GSTLTAQTIN RAMSHEIDPG APLIAETGGL NAMIVDSTAL
PEQAIKDIVA SAFQSAGQRC SALRILYVQE DVAETLLTML YGAMDELVVG DPWDLRTDVG
PVIDRGAQQE ILEYIEVARS EGRVLKQLAA PDAGTFVPPT VLRVSSISDM EKEVFGPVMH
VATYKASELD QVVDAINATG FGLTFGMHSR IDDRIEQVTS RIAVGNMYIN RNQIGAIVGS
QPFGGEGLSG TGPKAGGPSY VRRFTQGVSR NLASEAAPVV SSARIRSAIR ETEAPGRLAL
SRSELPGPTG ESNVLSTYGR GTFLCLGPTL AAAQQQASIV RAHGCGAVIV APGATGSGTA
DGAVDPAVLG VLEGIDAVVH WGAEADQRAV RKALAERDGA LVPLITEEDF GDRCLLERHI
CVDTTAAGGN ATLLAEVS


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