ID ROCA_BACAA Reviewed; 515 AA. AC C3PBP4; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2009, sequence version 1. DT 27-MAR-2024, entry version 79. DE RecName: Full=1-pyrroline-5-carboxylate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00733}; DE Short=P5C dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00733}; 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=rocA {ECO:0000255|HAMAP-Rule:MF_00733}; GN OrderedLocusNames=BAA_0363; OS Bacillus anthracis (strain A0248). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=592021; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A0248; RA Dodson R.J., Munk A.C., Bruce D., Detter C., Tapia R., Sutton G., Sims D., RA Brettin T.; RT "Genome sequence of Bacillus anthracis A0248."; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. 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}. CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. RocA CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00733}. 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; CP001598; ACQ48277.1; -; Genomic_DNA. DR RefSeq; WP_000259550.1; NC_012659.1. DR AlphaFoldDB; C3PBP4; -. DR SMR; C3PBP4; -. DR GeneID; 75083619; -. DR KEGG; bai:BAA_0363; -. DR HOGENOM; CLU_005391_0_0_9; -. DR UniPathway; UPA00261; UER00374. DR GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IEA:UniProtKB-UniRule. 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 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 InterPro; IPR047597; RocA_bacillales. DR NCBIfam; TIGR01237; D1pyr5carbox2; 1. DR PANTHER; PTHR42862; DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE 1, ISOFORM A-RELATED; 1. DR PANTHER; PTHR42862:SF1; DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE 2, ISOFORM A-RELATED; 1. DR Pfam; PF00171; Aldedh; 1. DR SUPFAM; SSF53720; ALDH-like; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. PE 3: Inferred from homology; KW NAD; Oxidoreductase. FT CHAIN 1..515 FT /note="1-pyrroline-5-carboxylate dehydrogenase" FT /id="PRO_1000148095" FT ACT_SITE 286 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00733" FT ACT_SITE 320 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00733" SQ SEQUENCE 515 AA; 56225 MW; 13A0909998818332 CRC64; MVVAYKHEPF TDFSVEANKL AFEEGLKKVE SYLGQDYPLI IGGEKITTED KIVSVNPANK EELVGRVSKA SRELAEKAMQ VADETFQTWR KSKPEMRADI LFRAAAIVRR RKHEFSAILV KEAGKPWNEA DADTAEAIDF MEYYGRQMLK LKDGIPVESR PIEYNRFSYI PLGVGVIISP WNFPFAIMAG MTTAALVSGN TVLLKPASTT PVVAAKFMEV LEEAGLPAGV VNFVPGNGSE VGDYLVDHPR TRFISFTGSR DVGIRIYERA AKVNPGQIWL KRVIAEMGGK DTIVVDKEAD LELAAKSIVA SAFGFSGQKC SACSRAVIHE DVYDHVLNRA VELTKELTVA NPAVLGTNMG PVNDQAAFDK VMSYVAIGKE EGRILAGGEG DDSKGWFIQP TIVADVAEDA RLMKEEIFGP VVAFCKAKDF DHALAIANNT EYGLTGAVIS NNRDHIEKAR EDFHVGNLYF NRGCTGAIVG YQPFGGFNMS GTDSKAGGPD YLALHMQAKT TSETL //