ID A0A077DDU7_9BURK Unreviewed; 1198 AA.
AC A0A077DDU7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=IX83_02300 {ECO:0000313|EMBL:AIL32301.1};
OS Basilea psittacipulmonis DSM 24701.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Basilea.
OX NCBI_TaxID=1072685 {ECO:0000313|EMBL:AIL32301.1, ECO:0000313|Proteomes:UP000028945};
RN [1] {ECO:0000313|EMBL:AIL32301.1, ECO:0000313|Proteomes:UP000028945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24701 {ECO:0000313|EMBL:AIL32301.1,
RC ECO:0000313|Proteomes:UP000028945};
RX PubMed=24581117; DOI=10.1186/1471-2164-15-169;
RA Whiteson K.L., Hernandez D., Lazarevic V., Gaia N., Farinelli L.,
RA Francois P., Pilo P., Frey J., Schrenzel J.;
RT "A genomic perspective on a new bacterial genus and species from the
RT Alcaligenaceae family, Basilea psittacipulmonis.";
RL BMC Genomics 15:169-169(2014).
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; CP009238; AIL32301.1; -; Genomic_DNA.
DR RefSeq; WP_038498707.1; NZ_CP009238.1.
DR AlphaFoldDB; A0A077DDU7; -.
DR STRING; 1072685.IX83_02300; -.
DR KEGG; bpsi:IX83_02300; -.
DR eggNOG; COG0506; Bacteria.
DR eggNOG; COG4230; Bacteria.
DR HOGENOM; CLU_005682_1_0_4; -.
DR OrthoDB; 6187633at2; -.
DR UniPathway; UPA00261; UER00373.
DR Proteomes; UP000028945; 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 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:UP000028945};
KW Repressor {ECO:0000256|PIRNR:PIRNR000197};
KW Transcription {ECO:0000256|PIRNR:PIRNR000197};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR000197}.
FT DOMAIN 10..56
FT /note="Proline utilization A proline dehydrogenase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18327"
FT DOMAIN 65..176
FT /note="Proline dehydrogenase PutA"
FT /evidence="ECO:0000259|Pfam:PF14850"
FT DOMAIN 185..479
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 559..1007
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 780
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
FT ACT_SITE 814
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 1198 AA; 131368 MW; C9DD7061A3E0B3CA CRC64;
MFKFSHAQEA LRNRITEAYR ADEAKAVQWL LAQQPLNEDE KVTIAKQAKE LILKVRENRK
KASGVDALMH EFTLSTEEGI ALMCLAEALL RIPDVETRNK LIQDKISGGD WKKHLGHSPS
LFVNSTAWGL FITGKLTSSL SENSLSSALT RVVAKGGQPL IRLAVNHAMR LLGKQFVTGE
TIEEALKNGA AREKMGYRFS FDMLGEAAMT SEDAQRYYQD YVKAIHAIGK QSAGKGVYDG
NGISVKLSAI HPRYSRAKHE RVMTELLPRL KELFLLAKQY DIGLNIDAEE ANRLELSLDL
IESLIKDPDL KGFKGIGIVV QAYQKRCPYV IDYLVDVARR HGQKLMIRLV KGAYWDSEIK
WSQLEGLEGY PVYTRKAHTD VSYLVCARKL LAAQDAVFPQ FATHNAYTAC AIYHMGKGLD
FEFQCLHGMG ETLYDQVVGE KNLGRRVRVY APVGTHETLL AYLVRRLLEN GANSSFVNQL
VDEKVSIDDL VKCPLDVAET YQGKMHQALP LPRKLYGSAR DNSLGIDLSN ELALAQLEQA
MNAFEPHYVA SSLLAVADEQ AKTVEVLNPA NHDDKVGQAT FSDVKVVSKV IEAAIAGQTA
WASKPVKERA DCLRRFADLM EEHMPSLMAL AIREAGKTLT NAIAEIREAV DFCRYYADEA
EHHLPADAQA VGAVVTISPW NFPLAIFIGQ TVAALVVGNS VVAKPAEQTS LIAHRAVTLL
HQAGVPTTAL QLILGAGDVG AALTSDARIA GVIFTGSTEV AKLINKNLKA RDDQPLLIAE
TGGQNAMIVD STALPEQVCV DVLNSAFDSA GQRCSALRIL CVQEEVADRT LKMIKDAMNE
LKVGNPVDMD TDIGPVIDAE AQKNLNDHIQ HISKVAKNVH QIKMQDTLES KGTYVLPTLI
ELNNLNELKK EVFGPVLHVI RYRSEDLLNL IDQINAKGYA LTHGVHSRID ATVAQIIDRV
NAGNIYVNRN IVGAVVGVQP FGGHGLSGTG PKAGGPFYLQ RLINTKQWRK PLVTTEAVFD
QKAADALIHS LNQNANIQNK AYLQEAVNQA KAYHLHGAVA TLKGPTGEEN TLHWELPKGI
WLYGGDLEQA LKVAVQLQVL GFKFFVLPDH PVAQYSSVFS GLTVTEHSLI LSNVSHVLSL
GSFPSAERLR LADSQGAIVH LIETQQEVDY LRLYQEVSVS INTTAAGGNA SLMAMSEA
//
