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Database: UniProt
Entry: A0A0A5GNN0_9BACI
LinkDB: A0A0A5GNN0_9BACI
Original site: A0A0A5GNN0_9BACI 
ID   A0A0A5GNN0_9BACI        Unreviewed;       274 AA.
AC   A0A0A5GNN0;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Competence protein ComER {ECO:0000313|EMBL:KGX93559.1};
GN   ORFNames=N781_11055 {ECO:0000313|EMBL:KGX93559.1};
OS   Pontibacillus halophilus JSM 076056 = DSM 19796.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pontibacillus.
OX   NCBI_TaxID=1385510 {ECO:0000313|EMBL:KGX93559.1, ECO:0000313|Proteomes:UP000030528};
RN   [1] {ECO:0000313|EMBL:KGX93559.1, ECO:0000313|Proteomes:UP000030528}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JSM 076056 {ECO:0000313|EMBL:KGX93559.1,
RC   ECO:0000313|Proteomes:UP000030528};
RA   Huang J., Wang G.;
RL   Submitted (AUG-2013) 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:KGX93559.1}.
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DR   EMBL; AVPE01000002; KGX93559.1; -; Genomic_DNA.
DR   RefSeq; WP_026802137.1; NZ_KE384328.1.
DR   AlphaFoldDB; A0A0A5GNN0; -.
DR   STRING; 1385510.GCA_000425205_01120; -.
DR   eggNOG; COG0345; Bacteria.
DR   OrthoDB; 9805754at2; -.
DR   Proteomes; UP000030528; 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   Gene3D; 1.10.3730.10; ProC C-terminal domain-like; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
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:SF51; COME OPERON PROTEIN 4; 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; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00521; P5CR; 1.
PE   3: Inferred from homology;
KW   NADP {ECO:0000256|PIRSR:PIRSR000193-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030528}.
FT   DOMAIN          3..97
FT                   /note="Pyrroline-5-carboxylate reductase catalytic N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03807"
FT   DOMAIN          159..262
FT                   /note="Pyrroline-5-carboxylate reductase dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF14748"
FT   BINDING         6..11
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
SQ   SEQUENCE   274 AA;  30450 MW;  6AC407F999C2AA6C CRC64;
     MKWGIIGTGN MGRMLAEVWI EKQVVKPEDL YVTNRNLDKA IGLQALYREI TIVESVEELA
     EHADVLFICT KPLDIHPLLV RMSPYLTKQQ CLVSITSPYS VEELEELVPC QVARIIPSIT
     NRAHAGVSLV TYGSGVSPVM KAYLEQSVKL YSTPLNIKEE ITRVASDIVS CGPAFYSFVT
     QKFVEAATSE TEISKDEATI MATEMLIGLG KLLEEGHYTL KTLQEKVSVK GGVTGEGIRV
     MEKEMATVFH HVIQATHDKY AEDKDKIEGQ RTTT
//
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