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Database: UniProt
Entry: I1DY54_9GAMM
LinkDB: I1DY54_9GAMM
Original site: I1DY54_9GAMM 
ID   I1DY54_9GAMM            Unreviewed;      1258 AA.
AC   I1DY54;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 50.
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:GAB58982.1};
GN   ORFNames=RNAN_1971 {ECO:0000313|EMBL:GAB58982.1};
OS   Rheinheimera nanhaiensis E407-8.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Rheinheimera.
OX   NCBI_TaxID=562729 {ECO:0000313|EMBL:GAB58982.1, ECO:0000313|Proteomes:UP000004374};
RN   [1] {ECO:0000313|EMBL:GAB58982.1, ECO:0000313|Proteomes:UP000004374}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E407-8 {ECO:0000313|EMBL:GAB58982.1,
RC   ECO:0000313|Proteomes:UP000004374};
RX   PubMed=23209246; DOI=10.1128/JB.01922-12;
RA   Zhang X.-Y., Zhang Y.-J., Qin Q.-L., Xie B.-B., Chen X.-L., Zhou B.-C.,
RA   Zhang Y.-Z.;
RT   "Genome Sequence of the Protease-Producing Bacterium Rheinheimera
RT   nanhaiensis E407-8T, Isolated from Deep-Sea Sediment of the South China
RT   Sea.";
RL   J. Bacteriol. 194:7001-7002(2012).
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}.
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:GAB58982.1}.
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DR   EMBL; BAFK01000009; GAB58982.1; -; Genomic_DNA.
DR   RefSeq; WP_008221180.1; NZ_BAFK01000009.1.
DR   AlphaFoldDB; I1DY54; -.
DR   STRING; 562729.RNAN_1971; -.
DR   OrthoDB; 9812625at2; -.
DR   UniPathway; UPA00261; UER00373.
DR   Proteomes; UP000004374; 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; 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; 2.
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; 2.
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:UP000004374};
KW   Repressor {ECO:0000256|PIRNR:PIRNR000197};
KW   Transcription {ECO:0000256|PIRNR:PIRNR000197};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR000197}.
FT   DOMAIN          12..58
FT                   /note="Proline utilization A proline dehydrogenase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18327"
FT   DOMAIN          67..180
FT                   /note="Proline dehydrogenase PutA"
FT                   /evidence="ECO:0000259|Pfam:PF14850"
FT   DOMAIN          189..481
FT                   /note="Proline dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF01619"
FT   DOMAIN          559..996
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   DOMAIN          1014..1189
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        779
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
FT   ACT_SITE        813
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ   SEQUENCE   1258 AA;  138173 MW;  751CD0274BC2F42F CRC64;
     MLYHGSLVAT QPLRQTIRDF YRADEDKVLS YLLPLADIGV NARSRAWERA RQLVLTIRQA
     QVGKGGVDAL LNEFSLSTEE GLVLMCLAEA LLRVPDKTTA DRLIRDKLSQ GDWSSHLGNS
     SSLFVNASAW GLLLTGKLVN YSDEQKKQQF GLLKRTCGRL GEPVIRQAVR YAMQIMGAQF
     VMGTTIDAAL ERATEMEAKG FRYSYDMLGE GARTMADADR YFDSYMRAID TIGKAANGRG
     PFNSPGISVK LSAIHPRYEF SHRDRVINEL VPRVKQLALA AKAYDIGFTI DAEEADRLDL
     SLDIIEAVFS DPALEGWEGF GLAVQAYQKR GIHVIEWLRE LALKVGRKMM VRLVKGAYWD
     TEIKLSQLEG FSDFPVFSRK PSTDVSYQAC AKKMLSYRDS IYPQFATHNA YTVATIMEMT
     SDYSGFEFQR LHGMGDALYD EIVIKDKIPC RIYAPVGEHS DLLAYLVRRL LENGANSSFV
     NNIVDETIPV ESLLSDPVET VRGWQSVRNR QIPLPANLYG SERLNSNGLD LTDIDQLEQV
     KKVMSLWFDS IKQLPVQHDA VPVTNPANLD EIIGYLHYAD ENQMQQILAN ADSAFASWSQ
     TDVSERSALL RRIGDALEVH RNELLALCVK EAGKTLGDSV AEVREAIDFC RYYAARAEEL
     FAKPQQARGV FLCISPWNFP LAIFLGQVAA AIVTGNTVVA KPAEQTSLIA IRTVEIMRDC
     GMPEHVVQLV IAPGRQVGEH IVPDSRIQGV MFTGSTETGC WIARKLAERG GEPVPLIAET
     GGQNCMIVDS TALPEQVVDD VISSGFQSAG QRCSALRVLF LQEDVADKII TMLKGAMAQL
     HVGDPQWLST DLGPVIDAKA HERLSAHVQY LADKATLHYE CAIPQEGKHY FFAPRLYEIS
     DLTVLEREVF GPVVHIIRFK ADELDSIINQ INATGYGLTM GVHSRIEQFT RRIARDIKAG
     NIYVNRNMIG AVVGVQPFGG RGLSGTGPKA GGPLYLTRLV KDNLDVSCPE LSEQKRHSLL
     SETTSNAVAY AMPVAASAQQ AWAMLPINQR TSVLRQFLAS LAANSVVNKQ EPDLEQVLTL
     AQQKLQRVER ELQQPVSLPG PTGESNMLVL DPRGVLALVR DDSSSFSYWL VAIITALAAG
     NAVITAVEEQ DFAEAEACIK ALQQAGMPQH LLAVVRLDCL TTLLAHADLA GAMVDVSSAV
     KPLCAELIAA RPGAILPLIT APAGPQLLQR LVTEKTITIN TTAAGGNASL MTMADNLG
//
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