ID W5W9Z8_9PSEU Unreviewed; 254 AA.
AC W5W9Z8;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AHH97361.1};
GN ORFNames=KALB_3997 {ECO:0000313|EMBL:AHH97361.1};
OS Kutzneria albida DSM 43870.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Kutzneria.
OX NCBI_TaxID=1449976 {ECO:0000313|EMBL:AHH97361.1, ECO:0000313|Proteomes:UP000019225};
RN [1] {ECO:0000313|EMBL:AHH97361.1, ECO:0000313|Proteomes:UP000019225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43870 {ECO:0000313|EMBL:AHH97361.1};
RX PubMed=25301375; DOI=10.1186/1471-2164-15-885;
RA Rebets Y., Tokovenko B., Lushchyk I., Ruckert C., Zaburannyi N.,
RA Bechthold A., Kalinowski J., Luzhetskyy A.;
RT "Complete genome sequence of producer of the glycopeptide antibiotic
RT Aculeximycin Kutzneria albida DSM 43870T, a representative of minor genus
RT of Pseudonocardiaceae.";
RL BMC Genomics 15:885-885(2014).
CC -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC {ECO:0000256|ARBA:ARBA00005525}.
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DR EMBL; CP007155; AHH97361.1; -; Genomic_DNA.
DR RefSeq; WP_025357450.1; NZ_CP007155.1.
DR AlphaFoldDB; W5W9Z8; -.
DR STRING; 1449976.KALB_3997; -.
DR KEGG; kal:KALB_3997; -.
DR PATRIC; fig|1449976.3.peg.4029; -.
DR eggNOG; COG0345; Bacteria.
DR HOGENOM; CLU_066353_0_0_11; -.
DR OrthoDB; 4425838at2; -.
DR Proteomes; UP000019225; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000019225}.
FT DOMAIN 3..96
FT /note="Pyrroline-5-carboxylate reductase catalytic N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF03807"
FT DOMAIN 153..247
FT /note="Pyrroline-5-carboxylate reductase dimerisation"
FT /evidence="ECO:0000259|Pfam:PF14748"
FT BINDING 56
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
SQ SEQUENCE 254 AA; 27743 MW; C62EF3266EC5D76B CRC64;
MQRIGIIGVG EIGRAIVAGL CEGDDQSTEV FLSPRGARIA SELSERYEGV QVCADNQEVV
DRSELVIIAV RRQDRHDALA SLRVDDDKIV VNVMAGVGND DLRQTLATDA PLVRAIPLPA
VRERRSVTVV YPSQPAVNSL FEHLGGVLPV ADEAAFNVFS ALTGTLTAHY WYLATLTSWA
AGQGIAFQDA DRYVRSLFQG LGRSLNDETR SLRQLAADHE TPNGSNERIR TTWFDQANSE
ALQKALDDLL ADLQ
//
