(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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