ID   ROCA2_ALKHC             Reviewed;         515 AA.
AC   Q9K5Z5;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 114.
DE   RecName: Full=1-pyrroline-5-carboxylate dehydrogenase 2;
DE            Short=P5C dehydrogenase 2;
DE            EC=1.2.1.88;
DE   AltName: Full=L-glutamate gamma-semialdehyde dehydrogenase;
GN   Name=rocA2; OrderedLocusNames=BH3940;
OS   Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
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   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. RocA
CC       subfamily. {ECO:0000305}.
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DR   EMBL; BA000004; BAB07659.1; -; Genomic_DNA.
DR   PIR; D84142; D84142.
DR   RefSeq; WP_010900065.1; NC_002570.2.
DR   AlphaFoldDB; Q9K5Z5; -.
DR   SMR; Q9K5Z5; -.
DR   STRING; 272558.10176565; -.
DR   EnsemblBacteria; BAB07659; BAB07659; BAB07659.
DR   KEGG; bha:BH3940; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_0_0_9; -.
DR   OMA; LMVMRET; -.
DR   OrthoDB; 744602at2; -.
DR   UniPathway; UPA00261; UER00374.
DR   Proteomes; UP000001258; Chromosome.
DR   GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IEA:UniProtKB-UniRule.
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; IEA:UniProtKB-UniPathway.
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   3: Inferred from homology;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..515
FT                   /note="1-pyrroline-5-carboxylate dehydrogenase 2"
FT                   /id="PRO_0000056508"
FT   ACT_SITE        286
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        320
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   515 AA;  56308 MW;  A6742C0030D67C30 CRC64;
     MLTPYKHEPF TDFSVEENRS AFEAALKNVE GELGKDYPLV INGERVTTDD KIVSVNPAMK
     EQVIGVVSKA SREIVDDAFK SAETAFHTWK NVNPEERANI LIRAAAIIRR RKHEFSAWLV
     KEAGKPWKEA DADTAEAIDF LEYYARQMIT LKDGKPVNSR EGEHNRYFYT PIGVCVTISP
     WNFALAIMAG TTVAPIVTGN TVLLKPASTT PVVAAKFVEV LEEAGLPKGV VNFVPGSGTD
     IGDYLIDHPK TSLITFTGSR DVGVRLYERA AVVHPGQQHL KRVIVEMGGK DTVVVDKDAD
     LDLAAQSIVT SAFGFSGQKC SAGSRAVIHQ DVYDVVLEKA VALTKQLSVG EPTAPDVYMG
     PVVDQGAFSK IMSYIEVGKE EGRLMVGGEG DDSKGFFIQP TIFADVDPHA RIMQEEIFGP
     VVAFSKARDF DHALEIANNT EYGLTGAVIT TNRHHIEKAK RDFHVGNLYF NRNCTGAIVG
     YHPFGGFKMS GTDSKAGGPD YLALHMQAKT VSEMY