ID   ROCA_BACSU              Reviewed;         515 AA.
AC   P39634;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=1-pyrroline-5-carboxylate dehydrogenase;
DE            Short=P5C dehydrogenase;
DE            EC=1.2.1.88;
DE   AltName: Full=L-glutamate gamma-semialdehyde dehydrogenase;
GN   Name=rocA; OrderedLocusNames=BSU37780; ORFNames=ipa-76d;
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=7934828; DOI=10.1111/j.1365-2958.1993.tb01963.x;
RA   Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F.,
RA   Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E.,
RA   Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A.;
RT   "Bacillus subtilis genome project: cloning and sequencing of the 97 kb
RT   region from 325 degrees to 333 degrees.";
RL   Mol. Microbiol. 10:371-384(1993).
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).
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   -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC       glutamate; L-glutamate from L-proline: step 2/2.
CC   -!- INDUCTION: Expression is sigma L dependent and induced by arginine.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. RocA
CC       subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X73124; CAA51632.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15805.1; -; Genomic_DNA.
DR   PIR; S39731; S39731.
DR   RefSeq; NP_391658.1; NC_000964.3.
DR   RefSeq; WP_003243454.1; NZ_JNCM01000034.1.
DR   AlphaFoldDB; P39634; -.
DR   SMR; P39634; -.
DR   STRING; 224308.BSU37780; -.
DR   jPOST; P39634; -.
DR   PaxDb; P39634; -.
DR   PRIDE; P39634; -.
DR   EnsemblBacteria; CAB15805; CAB15805; BSU_37780.
DR   GeneID; 937222; -.
DR   KEGG; bsu:BSU37780; -.
DR   PATRIC; fig|224308.179.peg.4090; -.
DR   eggNOG; COG1012; Bacteria.
DR   InParanoid; P39634; -.
DR   OMA; NWNKQLT; -.
DR   PhylomeDB; P39634; -.
DR   BioCyc; BSUB:BSU37780-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: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"
FT                   /id="PRO_0000056511"
FT   ACT_SITE        286
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        320
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   515 AA;  56320 MW;  C8115B4AEB4C979F CRC64;
     MTVTYAHEPF TDFTEAKNKT AFGESLAFVN TQLGKHYPLV INGEKIETDR KIISINPANK
     EEIIGYASTA DQELAEKAMQ AALQAFDSWK KQRPEHRANI LFKAAAILRR RKHEFSSYLV
     KEAGKPWKEA DADTAEAIDF LEFYARQMLK LKEGAPVKSR AGEVNQYHYE ALGVGIVISP
     FNFPLAIMAG TAVAAIVTGN TILLKPADAA PVVAAKFVEV MEEAGLPNGV LNYIPGDGAE
     IGDFLVEHPK TRFVSFTGSR AVGCRIYERA AKVQPGQKWL KRVIAEMGGK DTVLVDKDAD
     LDLAASSIVY SAFGYSGQKC SAGSRAVIHQ DVYDEVVEKA VALTKTLTVG NPEDPDTYMG
     PVIHEASYNK VMKYIEIGKS EGKLLAGGEG DDSKGYFIQP TIFADVDENA RLMQEEIFGP
     VVAICKARDF DHMLEIANNT EYGLTGALLT KNRAHIERAR EDFHVGNLYF NRGCTGAIVG
     YQPFGGFNMS GTDSKAGGPD YLILHMQAKT TSEAF