ID   A1U2B1_MARN8            Unreviewed;      1209 AA.
AC   A1U2B1;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 105.
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   OrderedLocusNames=Maqu_2049 {ECO:0000313|EMBL:ABM19130.1};
OS   Marinobacter nauticus (strain ATCC 700491 / DSM 11845 / VT8) (Marinobacter
OS   aquaeolei).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Marinobacteraceae; Marinobacter.
OX   NCBI_TaxID=351348 {ECO:0000313|EMBL:ABM19130.1, ECO:0000313|Proteomes:UP000000998};
RN   [1] {ECO:0000313|Proteomes:UP000000998}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700491 / DSM 11845 / VT8
RC   {ECO:0000313|Proteomes:UP000000998};
RX   PubMed=21335390; DOI=10.1128/aem.01866-10;
RA   Singer E., Webb E.A., Nelson W.C., Heidelberg J.F., Ivanova N., Pati A.,
RA   Edwards K.J.;
RT   "Genomic potential of Marinobacter aquaeolei, a biogeochemical
RT   'opportunitroph'.";
RL   Appl. Environ. Microbiol. 77:2763-2771(2011).
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; CP000514; ABM19130.1; -; Genomic_DNA.
DR   RefSeq; WP_011785523.1; NC_008740.1.
DR   AlphaFoldDB; A1U2B1; -.
DR   STRING; 351348.Maqu_2049; -.
DR   KEGG; maq:Maqu_2049; -.
DR   eggNOG; COG0506; Bacteria.
DR   eggNOG; COG4230; Bacteria.
DR   HOGENOM; CLU_005682_1_0_6; -.
DR   OrthoDB; 9812625at2; -.
DR   UniPathway; UPA00261; UER00373.
DR   Proteomes; UP000000998; 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   Repressor {ECO:0000256|PIRNR:PIRNR000197};
KW   Transcription {ECO:0000256|PIRNR:PIRNR000197};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR000197}.
FT   DOMAIN          13..59
FT                   /note="Proline utilization A proline dehydrogenase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18327"
FT   DOMAIN          67..178
FT                   /note="Proline dehydrogenase PutA"
FT                   /evidence="ECO:0000259|Pfam:PF14850"
FT   DOMAIN          188..481
FT                   /note="Proline dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF01619"
FT   DOMAIN          562..1005
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        785
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
FT   ACT_SITE        819
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ   SEQUENCE   1209 AA;  131510 MW;  03C0386A35B68B11 CRC64;
     MSLQQSVAPE LNDIRQAIRA NYLADEHEVI HRLIAEAQLS DETRKAISAR AAELVRDVRN
     SARPTIMEKF LAEYGLTTKE GVALMCLAEA LLRVPDNLTI QDLIEDKITS GNWGAHVGKA
     KSGMINSATL ALLMTSNLLK DSERQSVGDT LRKLVKRLGE PVVRTVAGQA MKEMGRQFVL
     GRTIEEAQDR GKSQEERGYT YSYDMLGEAA RTDADAQRYY QAYSDAIDSI SKRCKGDVRT
     NPGISVKLSA LLARYEYGHK ERVMNELMPR ALKLARKAAA ANMGFNIDAE EQDRLDLSLD
     VIEAILSDPE LKDWQGFGVV VQAFGKRASQ TLDWLYALSE KLDRRIMVRL VKGAYWDAEI
     KRAQVMGLSD FPVFTRKACS DVAYLAGARK LLGMTDRIYP QFATHNAHSV SAVLELAKDL
     SRDKFEFQRL HGMGESLHDQ VLEDSGVPCR IYAPVGAHKD LLAYLVRRLL ENGANSSFVN
     QIVDTSITPE EIAKDPIDVV VGLGHNLSSK AIVHPSKIFG EQRRNSKGWD ITDPVTVAEI
     DEGRNRYKSH QWKGGPILAV DSVSDEVVEV RNPANPDDLV GHITYTSEAD ISSALGAAQE
     GFKQWSAVPA EERAAMIRRV GDLYEENVHE LFALTTREAG KSLLDAVAEI REAVDFAMFY
     ANEGIRYKND GEARGVMCCI SPWNFPLAIF TGQILANLAA GNAVVAKPAE QTSLLAFRAV
     ELMHQAGIPR AAIQLLPGTG ATVGSGLTSD ARVTGVCFTG STATAQRINK AMTEHMEPDA
     PLVAETGGLN AMIVDSTALP EQVVRDVLAS SFQSAGQRCS ALRMLYVQKD IADNLLEMLY
     GAMEELGIGD PWQLSTDVGP VIDENARKKI TDHCQKFEQQ GKLLKKLNVP EKGLFVSPAV
     LQVSGIEELE EEIFGPVLHV ATFEAKDIDK VIDAVNAKGY GLTFGIHSRV DRRIEHIASR
     IKVGNTYVNR NQIGAIVGSQ PFGGEGLSGT GPKAGGPQYV RRFLRGEVVE KPAQSSDKVL
     SADKAQKLID KLAKVEVPEA EGRQALLVPF FGKVPAPLDE GYEDMPGPTG EQNHLSCHGR
     GLVLCLGPDA ESAVEQAGTA LSQGNKVVVI APGAEKALAD AIKAGLPVVA SDGMLDPDAL
     SHLTGFEAVV SVAEKPLLKQ YRMALSKRDG ALLPVITEHK LDQRYVIERH LCIDTTAAGG
     NASLIASAE
//