ID   P5CR_METAC              Reviewed;         270 AA.
AC   Q9HH99;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 118.
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=MA_4102;
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11844777; DOI=10.1128/jb.184.5.1449-1454.2002;
RA   Zhang J.K., White A.K., Kuettner H.C., Boccazzi P., Metcalf W.W.;
RT   "Directed mutagenesis and plasmid-based complementation in the methanogenic
RT   archaeon Methanosarcina acetivorans C2A demonstrated by genetic analysis of
RT   proline biosynthesis.";
RL   J. Bacteriol. 184:1449-1454(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA   Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA   Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA   White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA   Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA   Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(2002).
CC   -!- FUNCTION: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to
CC       L-proline. {ECO:0000305|PubMed:11844777}.
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   -!- 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   -!- 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:11844777}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01925}.
CC   -!- DISRUPTION PHENOTYPE: Mutants are auxotrophic for proline.
CC       {ECO:0000269|PubMed:11844777}.
CC   -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01925}.
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DR   EMBL; AF305580; AAG22033.1; -; Genomic_DNA.
DR   EMBL; AE010299; AAM07450.1; -; Genomic_DNA.
DR   RefSeq; WP_011023994.1; NC_003552.1.
DR   AlphaFoldDB; Q9HH99; -.
DR   SMR; Q9HH99; -.
DR   STRING; 188937.MA_4102; -.
DR   EnsemblBacteria; AAM07450; AAM07450; MA_4102.
DR   GeneID; 1475996; -.
DR   KEGG; mac:MA_4102; -.
DR   HOGENOM; CLU_042344_3_1_2; -.
DR   InParanoid; Q9HH99; -.
DR   OMA; VVRVMTN; -.
DR   OrthoDB; 70966at2157; -.
DR   PhylomeDB; Q9HH99; -.
DR   UniPathway; UPA00098; UER00361.
DR   Proteomes; UP000002487; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; IBA:GO_Central.
DR   GO; GO:0055129; P:L-proline biosynthetic process; IBA:GO_Central.
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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; NADP; Oxidoreductase;
KW   Proline biosynthesis; Reference proteome.
FT   CHAIN           1..270
FT                   /note="Pyrroline-5-carboxylate reductase"
FT                   /id="PRO_0000187312"
SQ   SEQUENCE   270 AA;  27943 MW;  50EC656AFC10B1CF CRC64;
     MENQKIGFIG AGKMGSALMQ GTIKAGIVTP ENIGASDVYE PFLKDLQAKL GIRVSTDNAV
     IVRESDILIL AVKPQTLSSV LSNLKNEITS EKLVISIAAG VPLSTYEDAL LEGTRVVRVM
     PNIAATVSEA ASGIAPGKNA TPEDLKAALE IFSAVGTAVQ VPESLMDAVT GLSGSGPAFI
     FPVIEAMADG AVLEGMDRKS ALTLAAQTVL GAAKMALETG MHPGELKDMV TSPAGTTIQG
     IHSLEEAGIR AAFMNAVIRA SERSKELGKK