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Database: UniProt
Entry: A0A0P8YAM5_9RHOB
LinkDB: A0A0P8YAM5_9RHOB
Original site: A0A0P8YAM5_9RHOB 
ID   A0A0P8YAM5_9RHOB        Unreviewed;      1144 AA.
AC   A0A0P8YAM5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
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=JI58_06295 {ECO:0000313|EMBL:KPU84026.1};
OS   Marinosulfonomonas sp. PRT-SC04.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Marinosulfonomonas.
OX   NCBI_TaxID=1527300 {ECO:0000313|EMBL:KPU84026.1, ECO:0000313|Proteomes:UP000054415};
RN   [1] {ECO:0000313|EMBL:KPU84026.1, ECO:0000313|Proteomes:UP000054415}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PRT-SC04 {ECO:0000313|EMBL:KPU84026.1};
RA   Leon Zayas R.I., Novotny M., Podell S., Shepard C.M., Berkenpas E.,
RA   Nikolenko S., Pevzner P., Lasken R.S., Bartlett D.H.;
RT   "Microbial Metabolic Properties Below 8,000 Meters Depth Within the Puerto
RT   Rico Trench Inferred From Single Cell Genomes.";
RL   Submitted (AUG-2014) 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: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003345}.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPU84026.1}.
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DR   EMBL; JPUR01000193; KPU84026.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P8YAM5; -.
DR   PATRIC; fig|1527300.3.peg.1335; -.
DR   UniPathway; UPA00261; UER00373.
DR   Proteomes; UP000054415; 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; IPR029510; Ald_DH_CS_GLU.
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.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 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:UP000054415};
KW   Repressor {ECO:0000256|PIRNR:PIRNR000197};
KW   Transcription {ECO:0000256|PIRNR:PIRNR000197};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR000197}.
FT   DOMAIN          4..50
FT                   /note="Proline utilization A proline dehydrogenase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18327"
FT   DOMAIN          58..168
FT                   /note="Proline dehydrogenase PutA"
FT                   /evidence="ECO:0000259|Pfam:PF14850"
FT   DOMAIN          177..474
FT                   /note="Proline dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF01619"
FT   DOMAIN          551..984
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        764
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000197-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU10007"
FT   ACT_SITE        798
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ   SEQUENCE   1144 AA;  122083 MW;  3701D2E032D32B65 CRC64;
     MLTQHRNTID AAQNAGEAKT LEALIKSAAL SPEMCAQISA RATQLVVDIR ASAKPGLMEV
     FLAEYGLSTD EGIALMCLAE ALLRVPDAST IDALIEDKIA PSNWGKHLGK SSSSLVNAST
     WALMLTGKVL DDTNPGIASQ LHGAVKRLGE PLIRHAVSRA MREMGRQFVL GENITKAMKR
     ATGMQKQGYT YSYDMLGEAA RTEADAKRYH LAYSKAITSI AAACTHKDIQ KNPGISVKLS
     ALHPRYEVAQ KDRVMAELVP RVRALAGLAK SAGMGFNIDA EEADRLSLSL DVIEAVLSDP
     SLAGWDGFGV VVQAFGQRTT PVIDWLYALS QKLDRRIMVR LVKGAYWDTE IKHAQVNGIE
     GFPVFTHKAA TDISYISNAQ RLLGMTDRIY PQFATHNAHT VAAILEMAQA GNNAADDYEF
     QRLHGMGERL HDIVLTAENS RCRIYAPVGA HRDLLAYLVR RLLENGANSS FVNQIVDAEV
     PPEVVAADPF EAPMPATSIT RAPDLFLPER RNSKGWDLAD VPTLAAIDAA REPHQTTSFT
     AAPLIAGKPS KSSAVPLLNP ADPADTVGHV TWASTADVNT ALTAAKPWDA PAAERAKILN
     KVADLYEENF GQIFAILTRE AGKTLPDAVG ELREAVDFLR YYAAQALRHT EPPVGLFTCI
     SPWNFPLAIF SGQIAASLAT GNATLAKPSE QTPLIAYFAT SLLHKAGVPA SALQLLPGDG
     SIGAALTSDA RIGGVCFTGS TATALLIRSA MAENLAPGAP LIAETGGLNA MIVDSTALFE
     QAVRDVVQSA FQSAGQRCSA LRCLYVQEDI AEDFTEMLQG AMDELSLTNP WQLSCDVGPV
     IDQAAHEQIA DYISAAKTEG RLIKQLPRPA VGHFIAPALI QVSGIIDMQR EIFGPVLHIA
     TFKSGDLGRV IHDINATGYG LTFGLHTRID DRVQYVVERL KAGNIYVNRN QIGAVVGSQP
     FGGEGLSGTG PKAGGTEYLT RFLTHETPGI SQDATPDDSR TPLKDLQNTL TNAAVSTEVS
     TVELPGPTGE SNRLSYHVRL PILCLGPTLG AAEQQAAAVR DLGGIAVLAT GLPPEALTTL
     TGFSSAIYWG NAGRAYMQAL AQRKGAILAL ITRRPTSADT QLERHTCVDT TASGGNATLL
     AEAG
//
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