ID B7KZ28_METC4 Unreviewed; 1035 AA.
AC B7KZ28;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 91.
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=Mchl_0364 {ECO:0000313|EMBL:ACK81301.1};
OS Methylorubrum extorquens (strain CM4 / NCIMB 13688) (Methylobacterium
OS extorquens).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=440085 {ECO:0000313|EMBL:ACK81301.1, ECO:0000313|Proteomes:UP000002385};
RN [1] {ECO:0000313|Proteomes:UP000002385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM4 / NCIMB 13688 {ECO:0000313|Proteomes:UP000002385};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Marx C., Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium chloromethanicum
RT CM4.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACK81301.1, ECO:0000313|Proteomes:UP000002385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM4 / NCIMB 13688 {ECO:0000313|Proteomes:UP000002385};
RX PubMed=22887658; DOI=10.1128/JB.01009-12;
RA Marx C.J., Bringel F., Chistoserdova L., Moulin L., Farhan Ul Haque M.,
RA Fleischman D.E., Gruffaz C., Jourand P., Knief C., Lee M.C., Muller E.E.,
RA Nadalig T., Peyraud R., Roselli S., Russ L., Goodwin L.A., Ivanova N.,
RA Kyrpides N., Lajus A., Land M.L., Medigue C., Mikhailova N., Nolan M.,
RA Woyke T., Stolyar S., Vorholt J.A., Vuilleumier S.;
RT "Complete genome sequences of six strains of the genus Methylobacterium.";
RL J. Bacteriol. 194:4746-4748(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}.
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DR EMBL; CP001298; ACK81301.1; -; Genomic_DNA.
DR RefSeq; WP_012605493.1; NC_011757.1.
DR AlphaFoldDB; B7KZ28; -.
DR KEGG; mch:Mchl_0364; -.
DR HOGENOM; CLU_005682_1_0_5; -.
DR UniPathway; UPA00261; UER00373.
DR Proteomes; UP000002385; 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 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; 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 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 60..169
FT /note="Proline dehydrogenase PutA"
FT /evidence="ECO:0000259|Pfam:PF14850"
FT DOMAIN 179..479
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 562..1014
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 794
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
FT ACT_SITE 828
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 1035 AA; 108545 MW; 0653EAB225E8FBD8 CRC64;
MTDGPMSALR FQAAYAPDDA ALAEALLREA PLPAATEAAV DRLASDLIGA IRADAGHGAV
EALLREYALT TREGLALMSL AEALLRVPDA ATADRLIADK LREGDFAHHA VRSESGLAHA
ASWALGLGAR LVGPQDTPEA TLGSMVRRLG RPAVRAAAHR AMRVMGGQFV LAEEIGAALK
RAGSGTARRS RFSFDMLGEG ARTADDAESY RQAYARAIAR IGREAGNAPL PARPGISVKL
SALHPRYTPT QGARVMAELV PVVRDLARDA RAHDLNFTLD AEEAERLELS LDVFEAVLAD
PALAGWDGFG LAIQAYSKRC LPVIDYVAGL AERHDRRLMV RLVKGAYWDT EVKLAQTQGA
ADYPVFTRKA MTDLNYLAAA RRLLALRPRL YPQFATHNAQ TVASVLGLAG LLDRPADEEA
GFEFQRLHGM GEALYQRLAE RAPGVGQRVY APVGGHRELL AYLVRRLLEN GANSSFVARA
ADPSVPAAEL LARPQALVET PSQARHPKIP LPRDLFGPER RNSPGLAFGD GAALRRWTDA
VARAAGPADA APIIDGAVQT DRARPVVSPI DGAALGSVIE ADPVTAALAM EAASRGFPAW
AATPARERAA CLERAADAFV REKGRLLHLL QAEAGKTLDD AVAEWREAID FLRYYAAQGR
DLFCEPQDLP GPAGEANSLR LVGRGVFVAV SPWNFPLAIF TGQVAAALMA GNAVVAKPAP
QTPLVADLAV RLLHAAGIPG SALHLVPGGP ETGAALIEHP ALSGVVFTGS TTTAQRINRA
LAARDGAILP LIAETGGINA MIVDATALPE QVADDVVVSA FRSAGQRCSA LRLLLVQEDV
ADRMIAAVAG AGRELTVGDP RDLATDLGPV IDAGAKQRLD AHIAAMTASA RLHYAGAAPG
GLTVAPHIFE IGGVADLREE VFGPILHVAR YPADGLGSVL AAIRAGGYGL TLGIHSRIEE
TAERIAEALP HGNVYVNRNM IGAVVGSQPF GGSGLSGTGP KAGGPHYLAR FATERTLTVN
TAAAGGSVGL ITLEG
//
