(data stored in SCRATCH zone)
SWISSPROT: D6XXY3_BACIE
ID D6XXY3_BACIE Unreviewed; 516 AA.
AC D6XXY3;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 08-MAY-2019, entry version 67.
DE RecName: Full=1-pyrroline-5-carboxylate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00733};
DE Short=P5C dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00733};
DE EC=1.2.1.88 {ECO:0000256|HAMAP-Rule:MF_00733};
DE AltName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00733};
GN Name=rocA {ECO:0000256|HAMAP-Rule:MF_00733};
GN OrderedLocusNames=Bsel_0520 {ECO:0000313|EMBL:ADH98056.1};
OS Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC unclassified Sporolactobacillaceae.
OX NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH98056.1, ECO:0000313|Proteomes:UP000000271};
RN [1] {ECO:0000313|EMBL:ADH98056.1, ECO:0000313|Proteomes:UP000000271}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC {ECO:0000313|Proteomes:UP000000271};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ovchinnikova G., Stolz J.;
RT "Complete sequence of Bacillus selenitireducens MLS10.";
RL Submitted (OCT-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:0000256|HAMAP-Rule:MF_00733};
CC -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC glutamate; L-glutamate from L-proline: step 2/2.
CC {ECO:0000256|HAMAP-Rule:MF_00733}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. RocA
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00733}.
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DR EMBL; CP001791; ADH98056.1; -; Genomic_DNA.
DR RefSeq; WP_013171485.1; NC_014219.1.
DR SMR; D6XXY3; -.
DR STRING; 439292.Bsel_0520; -.
DR EnsemblBacteria; ADH98056; ADH98056; Bsel_0520.
DR KEGG; bse:Bsel_0520; -.
DR eggNOG; ENOG4105C26; Bacteria.
DR eggNOG; COG1012; LUCA.
DR HOGENOM; HOG000271511; -.
DR KO; K00294; -.
DR OMA; NWNKQLT; -.
DR OrthoDB; 744602at2; -.
DR BioCyc; BSEL439292:G1GLR-548-MONOMER; -.
DR UniPathway; UPA00261; UER00374.
DR Proteomes; UP000000271; 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; 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.
PE 3: Inferred from homology;
DR PRODOM; D6XXY3.
DR SWISS-2DPAGE; D6XXY3.
KW Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW NAD {ECO:0000256|HAMAP-Rule:MF_00733};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00733};
KW Reference proteome {ECO:0000313|Proteomes:UP000000271}.
FT DOMAIN 52 512 Aldedh. {ECO:0000259|Pfam:PF00171}.
FT ACT_SITE 286 286 {ECO:0000256|HAMAP-Rule:MF_00733}.
FT ACT_SITE 320 320 {ECO:0000256|HAMAP-Rule:MF_00733,
FT ECO:0000256|PROSITE-ProRule:PRU10008}.
SQ SEQUENCE 516 AA; 57564 MW; 7EB04189B49AD16E CRC64;
MVVPYRHEPF TDFTVEENRK DYQEALDYVK SQLGKEYPLI INGEKVFTEK KSVSENPANH
KEVVGYVSQC SQDLAKQAME AADEAFTSWK KWDPAARANI LFRASAMIRR RKHEFSAWLT
YEAGKPWKEA DADTAEAIDF LEYYARQILR LKDGIPINSR DGENNTFNYI PLGIGITISP
WNFAFAIMAG TTVGPMVAGN TILLKPARTT PVIAYKFMEV LLEAGLPKGV VNYVPGSSRE
IGDYLVDHPR TRFINFTGSK EVGLHIAERA AKVNEGQIWM KRMISEMGGK DTIIVDSDAD
LELAAEAITY SAFGFSGQKC SACSRVIAHK DVYDDVLNRV VERTKKLTVG PTFKDNSNFM
GPVNDQDAFD KILDYIEVGK KEGRLMVGGT GDNSEGYFIH PTVFADVDSK ARVMQEEIFG
PVVAFDKAED FDELIEKANN TEYGLTGAVI SNNRDHLEQA RQDFHVGNLY FNRGCTAAIV
GYHPFGGFNM SGTDSKAGGP DYLLHFLQPK TVSDMF
//
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