ID A0A0B4EQK9_9RHOB Unreviewed; 1137 AA.
AC A0A0B4EQK9;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
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=GC1_04270 {ECO:0000313|EMBL:KID10887.1};
OS Leisingera sp. ANG1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Leisingera.
OX NCBI_TaxID=1002340 {ECO:0000313|EMBL:KID10887.1, ECO:0000313|Proteomes:UP000031201};
RN [1] {ECO:0000313|EMBL:KID10887.1, ECO:0000313|Proteomes:UP000031201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANG1 {ECO:0000313|EMBL:KID10887.1,
RC ECO:0000313|Proteomes:UP000031201};
RX PubMed=21551313; DOI=10.1128/JB.05139-11;
RA Collins A.J., Nyholm S.V.;
RT "Draft genome of Phaeobacter gallaeciensis ANG1, a dominant member of the
RT accessory nidamental gland of Euprymna scolopes.";
RL J. Bacteriol. 193:3397-3398(2011).
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:KID10887.1}.
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DR EMBL; AFCF02000001; KID10887.1; -; Genomic_DNA.
DR RefSeq; WP_019295565.1; NZ_AFCF02000001.1.
DR AlphaFoldDB; A0A0B4EQK9; -.
DR STRING; 1002340.GC1_04270; -.
DR eggNOG; COG0506; Bacteria.
DR eggNOG; COG4230; Bacteria.
DR OrthoDB; 9812625at2; -.
DR UniPathway; UPA00261; UER00373.
DR Proteomes; UP000031201; 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; 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..473
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 555..981
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT REGION 999..1023
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 762
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
FT ACT_SITE 796
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 1137 AA; 121451 MW; 387496666356EF0D CRC64;
MTAQTKLRYR IDAGTYADQT AMRDLLVAQA ALTDADREKI CANAAALVRD IRGHSAPGLM
EVFLAEYGLS TDEGVALMCL AEALLRVPDA DTIDALIEDK IAPSDWGKHL GKSTSSLVNA
STWALMLTGK VLDEERSPIG ALRGAIKRLG EPVIRTAVSR AMKEMGRQFV LGETIESAMN
RAAGMEAKGY TYSYDMLGEA ARTEADASRY HLAYSKAISA IAAACNSDDI RRNPGISVKL
SALHPRYELA HEHSVMEALV PRLKALALLA KAAKMGLNVD AEEADRLSLS LEVIEAVVSD
PALAGWDGFG VVVQAYGPRT GLAIDALHEM AEKYDRRFMV RLVKGAYWDT EIKRAQVEGV
DGFPVFTSKP LTDVSYISNA RKLLGMTDRI YPQFATHNAH TVAAILHMAE GVGNERYEFQ
RLHGMGETLH QMVLEQNKTN CRIYAPVGAH RDLLAYLVRR LLENGANSSF VNQIVDDNVP
PEVVAADPFE AIADVTRKIP TGPELYAPER PNSKGFDLGH APTLVKIEEA RAPWRSHQWE
AAPLLAGDAQ PEAAKDVTSP TDHSVVGTVS QCSQDDIELA LALADPWDAP AAERAAILNK
AADLYEENFG ELFAILAREA GKTIPDAVAE LREAVDFLRY YAARNSDAPP AGIFSCISPW
NFPLAIFTGQ VSAALSAGNA VLAKPADQTP LIAHRAVQLM HEAGVPRSAL QLVPGRGSVV
GAAITSDPRV NGVAFTGSTA TALRIRKAMA DNLQPGAPLI AETGGLNAMI VDSTALPEQA
VQAVIESAFQ SAGQRCSALR CLYLQDDIAD NVLKMLKGAM DCLQLDDPWN LSTDSGPVID
ETARAGILAH VGKARAEGRV LKEMRAPQAG TFVAPTMIEV SGISDLKEEI FGPVLHVARF
KSQQLDQVIS DINATGYGLT FGLHTRIDDR VQHVCDRVHA GNIYVNRNQI GAIVGSQPFG
GEGLSGTGPK AGGPLYLSRF CAPDRQSSAN SWDSNITDLK APSGVPSQPV TTSLPGPTGE
SNRLTVSARP PLLCMGPGAE AAAAQAKEVI SLGGTAIEAH GLLDMRQLES IEGIAGVLWW
GDEATGREIE QSLAKREGAI VPLIPGKPDR ARVLAERHVC VDTTASGGNA QLLGGMA
//
