ID A0A0P0ACP1_9RHOB Unreviewed; 1145 AA.
AC A0A0P0ACP1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=IMCC12053_2757 {ECO:0000313|EMBL:ALI56704.1},
GN SAMN05444421_106142 {ECO:0000313|EMBL:SFK63524.1};
OS Celeribacter marinus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Celeribacter.
OX NCBI_TaxID=1397108 {ECO:0000313|EMBL:ALI56704.1, ECO:0000313|Proteomes:UP000064920};
RN [1] {ECO:0000313|EMBL:ALI56704.1, ECO:0000313|Proteomes:UP000064920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC 12053 {ECO:0000313|EMBL:ALI56704.1,
RC ECO:0000313|Proteomes:UP000064920};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SFK63524.1, ECO:0000313|Proteomes:UP000181863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100036 {ECO:0000313|EMBL:SFK63524.1,
RC ECO:0000313|Proteomes:UP000181863};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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; CP012023; ALI56704.1; -; Genomic_DNA.
DR EMBL; FOSM01000006; SFK63524.1; -; Genomic_DNA.
DR RefSeq; WP_062219874.1; NZ_FOSM01000006.1.
DR AlphaFoldDB; A0A0P0ACP1; -.
DR STRING; 1397108.IMCC12053_2757; -.
DR KEGG; cmar:IMCC12053_2757; -.
DR PATRIC; fig|1397108.4.peg.2819; -.
DR OrthoDB; 9812625at2; -.
DR UniPathway; UPA00261; UER00373.
DR Proteomes; UP000064920; Chromosome.
DR Proteomes; UP000181863; 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; 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:UP000064920};
KW Repressor {ECO:0000256|PIRNR:PIRNR000197};
KW Transcription {ECO:0000256|PIRNR:PIRNR000197};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR000197}.
FT DOMAIN 19..55
FT /note="Proline utilization A proline dehydrogenase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18327"
FT DOMAIN 63..173
FT /note="Proline dehydrogenase PutA"
FT /evidence="ECO:0000259|Pfam:PF14850"
FT DOMAIN 182..474
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 555..984
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 765
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
FT ACT_SITE 799
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 1145 AA; 121677 MW; 41B4F6B5E974EA2D CRC64;
MNAALISTAL SDHLTFDKCR PEGEVLDALI AQAALCAPVR AAISARAAGL ITRIRKESAP
TLMEHFLAEY GLSTREGVAL MCLAEAMLRV PDRETMDELI EDKIAPSDWS RHLGAASSPM
VNASTWALML TGRVLDDEKP GLAGTLRGAI KRLGEPVIRT AVSRAMKEMG RQFVLGQSID
AALDRAARQE AKGYTYSYDM LGEAAMTAGD AARYAKAYGA AMTQIAARCD KGSVRDNPGI
SIKLSALHPR YEVAKEDRVM AELVPIVRDL ARQARAANMG FNIDAEEQDR LVLSLKVIHA
VLADPELAGW DGFGVVVQAY GRRAGAVIHW LNDTAIALDR KLMVRLVKGA YWDTEMKHAQ
VEGHADFPLF TTKCATDVSY IANAKTLLGY ADRLYPQFAT HNAHTVAAIL ELADGQAYEF
QRLHGMGERL HDIVLRDEAA RCRIYAPVGA HRDLLAYLVR RLLENGANSS FVNQIVDEDV
SPEEVARDPF AQLEEHHAHS GLVAPHALFG SERENSRGFD LTDEATLAEI NVARASAVLP
QAAPRCAVEV HDTPRDVINP ATGARIGTAI DANSDTVASA LAAAMPWSAP VAQRADALRR
AADLYEAEFG AIFAALAVEA GKSLSDAVGE LREAVDFLRY YAAQAEGLGD VKPLGCVVAI
SPWNFPLAIF TGQIAAALAA GNSVLAKPAE QTPIIATMAV DLLHKAGVPR EALQLLIGDG
ATVGAALTRD ARVNGVVFTG STETALRIRT SMAQHLSPDA PLIAETGGLN AMIVDSTALP
EQAARDIVAS AFQSAGQRCS ALRCLYVQED IAPALITMIK GAMDELAVGD PWDLSTDIGP
VIDAAACDQI NAYIEAAIKG GQLLYRTLPP KDGTFVAPCL IKVDGISDLD REVFGPVLHV
ATFKATDLDG VIDDINARGY GLTFGLHTRI DSRVQEIADK VHVGNVYVNR NQIGAVVGSQ
PFGGEGLSGT GPKAGGPLYL TRFCAGQART ASGVWTCDDD IADLQRLVDD ARATVHAMPR
HAVAMPGPTG EANRLTTLPR GPILCLGPTQ AGVNEQAAEV ERLGGIAVRA RGHIPSSVLE
TLGGIAGVIY WGDDGQDYTQ ALARRAGAIV PLIPCMPDTG HVMHERHLCV DTTAAGGNVA
LIAGG
//