ID A0A1H7NC76_9GAMM Unreviewed; 1274 AA.
AC A0A1H7NC76;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=SAMN05216262_10792 {ECO:0000313|EMBL:SEL20911.1};
OS Colwellia chukchiensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Colwellia.
OX NCBI_TaxID=641665 {ECO:0000313|EMBL:SEL20911.1, ECO:0000313|Proteomes:UP000199297};
RN [1] {ECO:0000313|Proteomes:UP000199297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.9127 {ECO:0000313|Proteomes:UP000199297};
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; FOBI01000007; SEL20911.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7NC76; -.
DR STRING; 641665.GCA_002104455_03371; -.
DR OrthoDB; 9812625at2; -.
DR UniPathway; UPA00261; UER00373.
DR Proteomes; UP000199297; 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; 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:UP000199297};
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 190..485
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 570..1012
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 790
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
FT ACT_SITE 824
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 1274 AA; 140542 MW; A7E284B2E9363C37 CRC64;
MLFNDSLITD CPIRQKIRDF YRIDENVAVD HILPLAEVNV SARSRAWERA RKMVLKIRQD
QSGNGAIDAL LNEYSLSSEE GVVLMCLAEA LLRVPDKDTQ DALIRDKISQ GQWSSHLGSS
ESLFVNASSW GLLITGAMVN YADRRKQDSF GLLKKTIGRL GEPVIRKAMN YAMKIMGKQF
VMGETITAAT ERAAEKEQKG YVYSYDMLGE GARTMADAER YLKAYQDAIE VIGQVAQATG
KNDPRKVPGI SVKLSAIHPR YEFTHKARVM AEIVPKLKAL CLQAKSYNIG LTVDAEESER
LDISLDIIEA VFSDNELGSW DGFGIALQAY QKRAIFVVDW LRELTLRVNR KMMVRLVKGA
YWDTEIKNAQ KDGHSHFPVF TRKSSTDVSY HACANKLLEY RDSIYPQFAT HNAYTAATIV
ELAGDDKEGF EFQCLHGMGD SLYDQIVAGE QIQCRIYAPV GHHEDLLAYL VRRLLENGAN
SSFVNAIVDE SQPVESLLGD PVEKTQRLKD KYNTQIVKPI ALYHEEMGSA RDNSKGLDLT
DINVITPLKA SLDSWFESHL ISASDVPEGA FAVKNPANHS EIIGYHHHHS KDDMLAMIDV
AEATFATWST TPVAERAALL CRVADILERH TDELIALCIK EAGKVTQDGI DEVREAVDFC
RYYANRAIDI AADERLEARG VVLCISPWNF PLAIFLGQVA AAIATGNTVL AKPAEQTSLI
ALRTIELMKS VGLPEGVVQA VIARGSQVGS VIIPDERIQT VMFTGSTETG TVISQTLAAR
GGDQVPLIAE TGGQNCMIVD STALPEQVVD DVISSGFQSA GQRCSALRVL FLQEDIADTV
ITMLKGALAE LHVGNPEYLS TDIGPVIDSK ALAALNAHSD YMKKHGKLLY QCQLGAEVKD
NEHYFFAPRL YEISDISVLK QEVFGPCVHV VRFKGNDIEA IIDQINGTGF GLTMGIHTRI
EHRAFELAKL SRAGNVYINR NMIGAIVGVQ PFGGRGLSGT GPKAGGPNYL SRLVIEKATP
DPEEFNLLPW QVDALDGDQT SEKEANLIME KANAAEKGWR LTELNTRISC VRQLLAKIAH
VEIVDDLADD LNRSLKAARS QLINIEKHLK KPTFLPGPTG ESNVLYLENR GNIICFADKN
VSFHFWLLSI VTALATGNTV IAVVSDLYYD EAIAFRDKFI AIGEGENVFQ VARLRHLTTM
LAHPALSGIV VDSNCDRKHF FSEKLAERQG AILPVISSEY FDNLIQRLLT EKTISIDTTA
SGGNTSLMTL VEED
//
