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Database: UniProt
Entry: J1JU65_BARVI
LinkDB: J1JU65_BARVI
Original site: J1JU65_BARVI 
ID   J1JU65_BARVI            Unreviewed;       263 AA.
AC   J1JU65;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Pyrroline-5-carboxylate reductase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ME1_00628 {ECO:0000313|EMBL:EJF88457.1};
OS   Bartonella vinsonii subsp. arupensis OK-94-513.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=1094562 {ECO:0000313|EMBL:EJF88457.1, ECO:0000313|Proteomes:UP000002304};
RN   [1] {ECO:0000313|EMBL:EJF88457.1, ECO:0000313|Proteomes:UP000002304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK-94-513 {ECO:0000313|EMBL:EJF88457.1,
RC   ECO:0000313|Proteomes:UP000002304};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Feldgarden M., Kirby J., Kosoy M., Birtles R., Probert W.S.,
RA   Chiaraviglio L., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA   Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D.,
RA   Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Bartonella vinsonii subsp. arupensis OK-94-513.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC       {ECO:0000256|ARBA:ARBA00005525}.
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:EJF88457.1}.
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DR   EMBL; AILZ01000013; EJF88457.1; -; Genomic_DNA.
DR   RefSeq; WP_004863176.1; NZ_JH725037.1.
DR   AlphaFoldDB; J1JU65; -.
DR   STRING; 1094562.ME1_00628; -.
DR   PATRIC; fig|1094562.3.peg.718; -.
DR   HOGENOM; CLU_066353_0_0_5; -.
DR   Proteomes; UP000002304; Unassembled WGS sequence.
DR   GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; IEA:InterPro.
DR   GO; GO:0006561; P:proline biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR028939; P5C_Rdtase_cat_N.
DR   InterPro; IPR029036; P5CR_dimer.
DR   InterPro; IPR000304; Pyrroline-COOH_reductase.
DR   PANTHER; PTHR11645:SF13; -; 1.
DR   PANTHER; PTHR11645; PYRROLINE-5-CARBOXYLATE REDUCTASE; 1.
DR   Pfam; PF03807; F420_oxidored; 1.
DR   Pfam; PF14748; P5CR_dimer; 1.
DR   PIRSF; PIRSF000193; Pyrrol-5-carb_rd; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   NADP {ECO:0000256|PIRSR:PIRSR000193-1}.
FT   DOMAIN          2..94
FT                   /note="Pyrroline-5-carboxylate reductase catalytic N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03807"
FT   DOMAIN          156..257
FT                   /note="Pyrroline-5-carboxylate reductase dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF14748"
FT   BINDING         55
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
SQ   SEQUENCE   263 AA;  29353 MW;  C75BFE95B095DE2D CRC64;
     MKIGFLGTGK ISTSMIDGLI KSNFDVPSLI ISPRNAQSAE RLSHKYDKVI IAENNQALLD
     MSDCVFLCLP NQVAKEVLSS LRFHSEQLVV SVLAMAKAAE VEEWINHKVY RAVPLPFVAE
     CKNLTPIYPD HPFLRRLFDA LGGTLVLDAE EQFNLFMTAG SLMGVYFNFI ETAHQWFITQ
     GLKKQQSADF LAMMFGNLTD EMRRITEIDG PSSLDFALLE KEFSTKGGTN ELLSNCFSRQ
     GGRDALITAL ETTLQKMNAS FSH
//
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