ROCA2_BACSU
ID ROCA2_BACSU Reviewed; 515 AA.
AC P94391;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=1-pyrroline-5-carboxylate dehydrogenase 2 {ECO:0000305};
DE Short=P5C dehydrogenase 2 {ECO:0000305};
DE EC=1.2.1.88 {ECO:0000255|HAMAP-Rule:MF_00733};
DE AltName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00733};
GN Name=putC {ECO:0000303|PubMed:22139509}; Synonyms=ycgN;
GN OrderedLocusNames=BSU03210;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969502; DOI=10.1099/13500872-142-11-3047;
RA Yamane K., Kumano M., Kurita K.;
RT "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome:
RT determination of the sequence of a 146 kb segment and identification of 113
RT genes.";
RL Microbiology 142:3047-3056(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP SEQUENCE REVISION TO 18 AND 239.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP INDUCTION.
RX PubMed=21840319; DOI=10.1016/j.jmb.2011.08.003;
RA Belitsky B.R.;
RT "Indirect repression by Bacillus subtilis CodY via displacement of the
RT activator of the proline utilization operon.";
RL J. Mol. Biol. 413:321-336(2011).
RN [5]
RP INDUCTION.
RC STRAIN=168;
RX PubMed=21964733; DOI=10.1099/mic.0.054197-0;
RA Huang S.C., Lin T.H., Shaw G.C.;
RT "PrcR, a PucR-type transcriptional activator, is essential for proline
RT utilization and mediates proline-responsive expression of the proline
RT utilization operon putBCP in Bacillus subtilis.";
RL Microbiology 157:3370-3377(2011).
RN [6]
RP FUNCTION, PATHWAY, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / JH642;
RX PubMed=22139509; DOI=10.1128/jb.06380-11;
RA Moses S., Sinner T., Zaprasis A., Stoeveken N., Hoffmann T., Belitsky B.R.,
RA Sonenshein A.L., Bremer E.;
RT "Proline utilization by Bacillus subtilis: uptake and catabolism.";
RL J. Bacteriol. 194:745-758(2012).
CC -!- FUNCTION: Important for the use of proline as a sole carbon and energy
CC source or a sole nitrogen source. {ECO:0000269|PubMed:22139509}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamate 5-semialdehyde + NAD(+) = 2 H(+) + L-
CC glutamate + NADH; Xref=Rhea:RHEA:30235, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58066; EC=1.2.1.88;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00733};
CC -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC glutamate; L-glutamate from L-proline: step 2/2. {ECO:0000255|HAMAP-
CC Rule:MF_00733, ECO:0000269|PubMed:22139509}.
CC -!- INDUCTION: The expression of the putBCP operon is induced in a PutR-
CC dependent fashion by very low concentrations of L-proline in the growth
CC medium. CodY represses the operon by displacing PutR from DNA.
CC {ECO:0000269|PubMed:21840319, ECO:0000269|PubMed:21964733,
CC ECO:0000269|PubMed:22139509}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the putBCP operon abolishes L-proline
CC utilization. {ECO:0000269|PubMed:22139509}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. RocA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00733}.
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DR EMBL; D50453; BAA08955.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12115.2; -; Genomic_DNA.
DR PIR; A69759; A69759.
DR RefSeq; NP_388203.2; NC_000964.3.
DR RefSeq; WP_003234655.1; NZ_JNCM01000030.1.
DR AlphaFoldDB; P94391; -.
DR SMR; P94391; -.
DR STRING; 224308.BSU03210; -.
DR jPOST; P94391; -.
DR PaxDb; P94391; -.
DR PRIDE; P94391; -.
DR EnsemblBacteria; CAB12115; CAB12115; BSU_03210.
DR GeneID; 938333; -.
DR KEGG; bsu:BSU03210; -.
DR PATRIC; fig|224308.179.peg.335; -.
DR eggNOG; COG1012; Bacteria.
DR InParanoid; P94391; -.
DR OMA; LMVMRET; -.
DR PhylomeDB; P94391; -.
DR BioCyc; BSUB:BSU03210-MON; -.
DR UniPathway; UPA00261; UER00374.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0004657; F:proline dehydrogenase activity; IMP:CACAO.
DR GO; GO:0006537; P:glutamate biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0010133; P:proline catabolic process to glutamate; IBA:GO_Central.
DR CDD; cd07124; ALDH_PutA-P5CDH-RocA; 1.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR HAMAP; MF_00733; RocA; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR005932; RocA.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR TIGRFAMs; TIGR01237; D1pyr5carbox2; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 2: Evidence at transcript level;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..515
FT /note="1-pyrroline-5-carboxylate dehydrogenase 2"
FT /id="PRO_0000056512"
FT ACT_SITE 286
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00733"
FT ACT_SITE 320
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00733"
FT CONFLICT 18
FT /note="N -> Y (in Ref. 1; BAA08955)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="A -> S (in Ref. 1; BAA08955)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 515 AA; 56424 MW; 937CAAFF1F97A009 CRC64;
MTTPYKHEPF TNFQDQNNVE AFKKALATVS EYLGKDYPLV INGERVETEA KIVSINPADK
EEVVGRVSKA SQEHAEQAIQ AAAKAFEEWR YTSPEERAAV LFRAAAKVRR RKHEFSALLV
KEAGKPWNEA DADTAEAIDF MEYYARQMIE LAKGKPVNSR EGEKNQYVYT PTGVTVVIPP
WNFLFAIMAG TTVAPIVTGN TVVLKPASAT PVIAAKFVEV LEESGLPKGV VNFVPGSGAE
VGDYLVDHPK TSLITFTGSR EVGTRIFERA AKVQPGQQHL KRVIAEMGGK DTVVVDEDAD
IELAAQSIFT SAFGFAGQKC SAGSRAVVHE KVYDQVLERV IEITESKVTA KPDSADVYMG
PVIDQGSYDK IMSYIEIGKQ EGRLVSGGTG DDSKGYFIKP TIFADLDPKA RLMQEEIFGP
VVAFCKVSDF DEALEVANNT EYGLTGAVIT NNRKHIERAK QEFHVGNLYF NRNCTGAIVG
YHPFGGFKMS GTDSKAGGPD YLALHMQAKT ISEMF
