ID A0A1D8S4E6_9EURY Unreviewed; 225 AA.
AC A0A1D8S4E6; A0A1J1AD87;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Pyrroline-5-carboxylate reductase {ECO:0000256|HAMAP-Rule:MF_01925};
DE Short=P5C reductase {ECO:0000256|HAMAP-Rule:MF_01925};
DE Short=P5CR {ECO:0000256|HAMAP-Rule:MF_01925};
DE EC=1.5.1.2 {ECO:0000256|HAMAP-Rule:MF_01925};
DE AltName: Full=PCA reductase {ECO:0000256|HAMAP-Rule:MF_01925};
GN Name=proC {ECO:0000256|HAMAP-Rule:MF_01925,
GN ECO:0000313|EMBL:AOW80236.1};
GN ORFNames=HSR6_1087 {ECO:0000313|EMBL:APE95537.1}, HTSR_1054
GN {ECO:0000313|EMBL:AOW80236.1};
OS Halodesulfurarchaeum formicicum.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halodesulfurarchaeum.
OX NCBI_TaxID=1873524 {ECO:0000313|EMBL:AOW80236.1, ECO:0000313|Proteomes:UP000185608};
RN [1] {ECO:0000313|EMBL:AOW80236.1, ECO:0000313|Proteomes:UP000185608}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTSR1 {ECO:0000313|EMBL:AOW80236.1,
RC ECO:0000313|Proteomes:UP000185608};
RA Sorokin D.Y., Kublanov I.V., Roman P., Sinninghe Damste J.S.,
RA Golyshin P.N., Rojo D., Ciordia S., Mena Md.C., Ferrer M., Smedile F.,
RA Messina E., La Cono V., Yakimov M.M.;
RT "Discovery of anaerobic lithoheterotrophic haloarchaeon capable of sulfur
RT respiration by hydrogen and formate.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000186165}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HSR6 {ECO:0000313|Proteomes:UP000186165};
RA Sorokin D.Y., Kublanov I.V., Roman P., Sinninghe Damste J.S.,
RA Golyshin P.N., Rojo D., Ciordia S., Mena Md.C., Ferrer M., Smedile F.,
RA Messina E., La Cono V., Yakimov M.M.;
RT "Discovery of first anaerobic lithoheterotrophic haloarchae widely
RT represented in hypersaline habitats.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:APE95537.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HSR6 {ECO:0000313|EMBL:APE95537.1};
RX PubMed=28106880; DOI=10.1038/ismej.2016.203;
RA Sorokin D.Y., Messina E., Smedile F., Roman P., Damste J.S.S., Ciordia S.,
RA Mena M.C., Ferrer M., Golyshin P.N., Kublanov I.V., Samarov N.I.,
RA Toshchakov S.V., La Cono V., Yakimov M.M.;
RT "Discovery of anaerobic lithoheterotrophic haloarchaea, ubiquitous in
RT hypersaline habitats.";
RL ISME J. 11:1245-1260(2017).
CC -!- FUNCTION: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to
CC L-proline. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01925};
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:0000256|HAMAP-Rule:MF_01925};
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-proline
CC from L-glutamate 5-semialdehyde: step 1/1. {ECO:0000256|HAMAP-
CC Rule:MF_01925}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01925}.
CC -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC {ECO:0000256|ARBA:ARBA00005525, ECO:0000256|HAMAP-Rule:MF_01925}.
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DR EMBL; CP016070; AOW80236.1; -; Genomic_DNA.
DR EMBL; CP016804; APE95537.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D8S4E6; -.
DR STRING; 1873524.HSR6_1087; -.
DR KEGG; halh:HTSR_1054; -.
DR KEGG; hhsr:HSR6_1087; -.
DR PATRIC; fig|1855411.3.peg.1055; -.
DR UniPathway; UPA00098; UER00361.
DR Proteomes; UP000185608; Chromosome.
DR Proteomes; UP000186165; 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 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 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; PYRROLINE-5-CARBOXYLATE REDUCTASE; 1.
DR PANTHER; PTHR11645:SF0; 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.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01925};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01925};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_01925};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01925,
KW ECO:0000313|EMBL:AOW80236.1};
KW Proline biosynthesis {ECO:0000256|HAMAP-Rule:MF_01925};
KW Reference proteome {ECO:0000313|Proteomes:UP000186165}.
FT DOMAIN 16..58
FT /note="Pyrroline-5-carboxylate reductase catalytic N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF03807"
FT DOMAIN 114..217
FT /note="Pyrroline-5-carboxylate reductase dimerisation"
FT /evidence="ECO:0000259|Pfam:PF14748"
FT BINDING 32..35
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
SQ SEQUENCE 225 AA; 23215 MW; D507D2C1CB8320FC CRC64;
MSEAALAGVS EAADQTTTDL TTAAEAEVVV LAVKPGTVGT VLDELTLSSD QTLLSFAAAV
PVEFLESRTQ ATVVRGMPNL AAETATMACA VTPTATDQVA AILSDLGEFV EIEEAQMDIA
TAVNGSGPAF VFYLIKALAA AGVESGLDEA EARVLAAQTF KGAAETVLQS EESLEALIDA
VSSDGGTTIE GMEVLWDSDV DTVLGDAVRA AEDRSIEISR EFQHD
//
