ID A0A0X1T5T1_PSEAA Unreviewed; 1317 AA.
AC A0A0X1T5T1;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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:AMB87445.1};
GN ORFNames=AWM79_19945 {ECO:0000313|EMBL:AMB87445.1};
OS Pseudomonas agarici.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=46677 {ECO:0000313|EMBL:AMB87445.1, ECO:0000313|Proteomes:UP000063229};
RN [1] {ECO:0000313|EMBL:AMB87445.1, ECO:0000313|Proteomes:UP000063229}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 2472 {ECO:0000313|EMBL:AMB87445.1,
RC ECO:0000313|Proteomes:UP000063229};
RA McClelland M., Jain A., Saraogi P., Mendelson R., Westerman R.,
RA SanMiguel P., Csonka L.;
RL Submitted (JAN-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}.
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DR EMBL; CP014135; AMB87445.1; -; Genomic_DNA.
DR RefSeq; WP_017130104.1; NZ_JACAQG010000057.1.
DR STRING; 46677.AWM79_19945; -.
DR OrthoDB; 9812625at2; -.
DR UniPathway; UPA00261; UER00373.
DR Proteomes; UP000063229; 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 CDD; cd22233; RHH_CopAso-like; 1.
DR Gene3D; 3.20.20.220; -; 1.
DR Gene3D; 1.10.1220.10; Met repressor-like; 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; IPR013321; Arc_rbn_hlx_hlx.
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 InterPro; IPR048798; PutA_RHH.
DR InterPro; IPR010985; Ribbon_hlx_hlx.
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 Pfam; PF21775; PutA_1st; 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 SUPFAM; SSF47598; Ribbon-helix-helix; 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:UP000063229};
KW Repressor {ECO:0000256|PIRNR:PIRNR000197};
KW Transcription {ECO:0000256|PIRNR:PIRNR000197};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR000197}.
FT DOMAIN 11..43
FT /note="PutA RHH"
FT /evidence="ECO:0000259|Pfam:PF21775"
FT DOMAIN 87..134
FT /note="Proline utilization A proline dehydrogenase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18327"
FT DOMAIN 146..257
FT /note="Proline dehydrogenase PutA"
FT /evidence="ECO:0000259|Pfam:PF14850"
FT DOMAIN 267..567
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 654..1101
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
SQ SEQUENCE 1317 AA; 142983 MW; 958ED24F032F986B CRC64;
MATTTLGVKL DDPTRERLKA AAHSIDRTPH WLIKQAIFNY LEKLESGATL SELSGTVRGE
TDDAGELQAD HAHQCFLEFA ESILPQSVLR SAITAAYRRP ESEVVPMLLE QARLPVAMAE
ATHKLASNIA QKLRNQKSVG GRAGIVQGLL QEFSLSSQEG VALMCLAEAL LRIPDKGTRD
ALIRDKISTG NWHPHLGNSP SLFVNAATWG LLLTGKLVAT HNEAGLTSSL SRIIGKSGEP
MIRKGVDMAM RLMGEQFVTG ETIAEALANA SRFEAKGFRY SYDMLGEAAL TERDAQKYLA
SYEQAIHAIG KASHGRGIYE GPGISIKLSA LHPRYSRAQY ERVMDELYPR LLSLTLLAKQ
YDIGLNIDAE EADRLELSLD LLERLCFEPQ LTGWNGIGFV IQAYQKRCPY VIDYVIDLAR
RSRHRLMIRL VKGAYWDSEI KRAQVEGLEG YPVYTRKVYT DVSYIACARK LLSVPEVIYP
QFATHNAHTL SAIYHIAGQN YYPGQYEFQC LHGMGEPLYE QVVGKVAEGK LNRPCRVYAP
VGTHETLLAY LVRRLLENGA NTSFVNRIAD QSISIQELVA DPVSSIEQMA LQEGGFGLPH
PRIPLPRELY GPERANSAGI DMANEHRLAS LSCALLASAH NNWKAAPMLG CDASNETATA
VLNPSDQRDL VGYVQEATVE DVDNAVQCAL SAAPIWQATP PAERAAILER AADLMEGEIQ
PLMGLLAREA GKTFANAIAE VREAVDFLRY YAVQARNDFS NDAHRPLGPV VCISPWNFPL
AIFSGQVAAA LAAGNPVLAK PAEQTPLIAA QAVRLLLEAG IPQGVVQLLP GRGETVGARL
VGDERVKGVM FTGSTEVARL LQRNVAGRLD NQGRPIPLIA ETGGQNAMIV DSSALTEQVV
IDVVSSAFDS AGQRCSALRV LCLQEDCAER VIEMLKGAMA ECRLGNPERL SVDIGPVIDA
EAKAGIEKHI QAMRDKGRSV YQVAIADSEE CKRGTFVMPT LIELESFDEL QREIFGPVLH
VVRYKRKEID SLIAQINASG YGLTLGVHTR IDETIAKVID TVNAGNVYVN RNIVGAVVGV
QPFGGEGLSG TGPKAGGPLY LYRLLATRPS DAIEQSFVRV DALNAPDMRL RDAMSKPLIA
LQTWARANQQ PELAELCTQF AAQSQSGITR PLVGPTGERN TYAILPREHV LCLAAVEADL
LSQLAAVLAV GSSAVWPEGE LGKALHARLP KEVQARIQQV ADWQKDEAIF DAVLHHGHSD
QLRAVCQQVA KRAGAIVGVQ GLSQGETGIA LERLVIERAL SVNTAAAGGN ASLMTIG
//
