ID ROCA_BACAC Reviewed; 515 AA.
AC C3L546;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 78.
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}; OrderedLocusNames=BAMEG_0366;
OS Bacillus anthracis (strain CDC 684 / NRRL 3495).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=568206;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 684 / NRRL 3495;
RA Dodson R.J., Munk A.C., Brettin T., Bruce D., Detter C., Tapia R., Han C.,
RA Sutton G., Sims D.;
RT "Genome sequence of Bacillus anthracis str. CDC 684.";
RL Submitted (OCT-2008) 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}.
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DR EMBL; CP001215; ACP13077.1; -; Genomic_DNA.
DR RefSeq; WP_000259550.1; NC_012581.1.
DR AlphaFoldDB; C3L546; -.
DR SMR; C3L546; -.
DR GeneID; 75083619; -.
DR KEGG; bah:BAMEG_0366; -.
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_1000148096"
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
//
