P5CR_TREPA
ID P5CR_TREPA Reviewed; 263 AA.
AC P27771; O83775;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=Pyrroline-5-carboxylate reductase {ECO:0000255|HAMAP-Rule:MF_01925};
DE Short=P5C reductase {ECO:0000255|HAMAP-Rule:MF_01925};
DE Short=P5CR {ECO:0000255|HAMAP-Rule:MF_01925};
DE EC=1.5.1.2 {ECO:0000255|HAMAP-Rule:MF_01925};
DE AltName: Full=PCA reductase {ECO:0000255|HAMAP-Rule:MF_01925};
GN Name=proC {ECO:0000255|HAMAP-Rule:MF_01925}; OrderedLocusNames=TP_0797;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RC STRAIN=Nichols;
RX PubMed=2188947; DOI=10.1128/jb.172.6.2996-3002.1990;
RA Gherardini F.C., Hobbs M.M., Stamm L.V., Bassford P.J. Jr.;
RT "Complementation of an Escherichia coli proC mutation by a gene cloned from
RT Treponema pallidum.";
RL J. Bacteriol. 172:2996-3002(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
CC -!- FUNCTION: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to
CC L-proline. {ECO:0000255|HAMAP-Rule:MF_01925,
CC ECO:0000269|PubMed:2188947}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-proline + NADP(+) = 1-pyrroline-5-carboxylate + 2 H(+) +
CC NADPH; Xref=Rhea:RHEA:14109, ChEBI:CHEBI:15378, ChEBI:CHEBI:15893,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:60039; EC=1.5.1.2;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01925,
CC ECO:0000269|PubMed:2188947};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-proline + NAD(+) = 1-pyrroline-5-carboxylate + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:14105, ChEBI:CHEBI:15378, ChEBI:CHEBI:15893,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:60039; EC=1.5.1.2;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01925,
CC ECO:0000269|PubMed:2188947};
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-proline
CC from L-glutamate 5-semialdehyde: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_01925, ECO:0000269|PubMed:2188947}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01925}.
CC -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC {ECO:0000255|HAMAP-Rule:MF_01925}.
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DR EMBL; M73825; AAA27478.1; -; Genomic_DNA.
DR EMBL; AE000520; AAC65760.1; -; Genomic_DNA.
DR PIR; D71281; D71281.
DR RefSeq; WP_010882242.1; NC_021490.2.
DR AlphaFoldDB; P27771; -.
DR SMR; P27771; -.
DR IntAct; P27771; 5.
DR STRING; 243276.TPANIC_0797; -.
DR EnsemblBacteria; AAC65760; AAC65760; TP_0797.
DR GeneID; 57879317; -.
DR KEGG; tpa:TP_0797; -.
DR eggNOG; COG0345; Bacteria.
DR HOGENOM; CLU_042344_3_1_12; -.
DR OMA; VVRVMTN; -.
DR OrthoDB; 1349288at2; -.
DR UniPathway; UPA00098; UER00361.
DR Proteomes; UP000000811; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR HAMAP; MF_01925; P5C_reductase; 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; PTHR11645; 1.
DR Pfam; PF03807; F420_oxidored; 1.
DR Pfam; PF14748; P5CR_dimer; 1.
DR PIRSF; PIRSF000193; Pyrrol-5-carb_rd; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00112; proC; 1.
DR PROSITE; PS00521; P5CR; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Cytoplasm; NADP; Oxidoreductase;
KW Proline biosynthesis; Reference proteome.
FT CHAIN 1..263
FT /note="Pyrroline-5-carboxylate reductase"
FT /id="PRO_0000187310"
FT CONFLICT 1..65
FT /note="MNVGFLGFGAMGRALAEGLVHAGALQAAQVYACALNQEKLRAQCTSLGIGAC
FT ASVQELVQKSEWI -> MTWDFWVLEQWDGRWQKGWCTQERCKRSSVRLCVKSGKVACA
FT VYIFGHRCLRVSSGTGTEKVNGF (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 77..93
FT /note="VLRDRQSFQGKVLISLA -> GTARSPIFQESAISC (in Ref. 1;
FT AAA27478)"
FT /evidence="ECO:0000305"
FT CONFLICT 256..260
FT /note="VRAAL -> CRWLS (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 263 AA; 27645 MW; ED4AD7C54BAF9D61 CRC64;
MNVGFLGFGA MGRALAEGLV HAGALQAAQV YACALNQEKL RAQCTSLGIG ACASVQELVQ
KSEWIFLAVK PSQISTVLRD RQSFQGKVLI SLAAGMSCAA YEALFAADPH QGIRHLSLLP
NLPCQVARGV IIAEARHTLH HDEHAALLAV LRTVAQVEVV DTAYFAIAGV IAGCAPAFAA
QFIEALADAG VRYGLARDQA YRLAAHMLEG TAALIQHSGV HPAQLKDRVC SPAGSTIRGV
LALEEQGLRR AVIHAVRAAL SSS
