(data stored in SCRATCH zone)

SWISSPROT: Q47SU6_THEFY

ID   Q47SU6_THEFY            Unreviewed;       542 AA.
AC   Q47SU6;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 92.
DE   SubName: Full=Delta-1-pyrroline-5-carboxylate dehydrogenase 1 {ECO:0000313|EMBL:AAZ54471.1};
GN   OrderedLocusNames=Tfu_0433 {ECO:0000313|EMBL:AAZ54471.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54471.1, ECO:0000313|Proteomes:UP000000434};
RN   [1] {ECO:0000313|Proteomes:UP000000434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX {ECO:0000313|Proteomes:UP000000434};
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; CP000088; AAZ54471.1; -; Genomic_DNA.
DR   RefSeq; WP_011290880.1; NC_007333.1.
DR   STRING; 269800.Tfu_0433; -.
DR   EnsemblBacteria; AAZ54471; AAZ54471; Tfu_0433.
DR   KEGG; tfu:Tfu_0433; -.
DR   eggNOG; ENOG4107RMK; Bacteria.
DR   eggNOG; COG1012; LUCA.
DR   HOGENOM; HOG000271511; -.
DR   KO; K00294; -.
DR   OMA; FAGIHFT; -.
DR   OrthoDB; 744602at2; -.
DR   BioCyc; TFUS269800:G1G4Q-440-MONOMER; -.
DR   Proteomes; UP000000434; Chromosome.
DR   GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IEA:InterPro.
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:0010133; P:proline catabolic process to glutamate; IEA:InterPro.
DR   CDD; cd07123; ALDH_F4-17_P5CDH; 1.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 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; IPR005931; P5CDH/ALDH4A1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   TIGRFAMs; TIGR01236; D1pyr5carbox1; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q47SU6.
DR   SWISS-2DPAGE; Q47SU6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003345};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000434}.
FT   DOMAIN       56    523       Aldedh. {ECO:0000259|Pfam:PF00171}.
FT   ACT_SITE    294    294       {ECO:0000256|PROSITE-ProRule:PRU10007}.
FT   ACT_SITE    328    328       {ECO:0000256|PROSITE-ProRule:PRU10008}.
SQ   SEQUENCE   542 AA;  59061 MW;  8D876AE8ECFDF439 CRC64;
     MDAVTNVPAP VNEPVLSYAP GSPERAELTR YLTALADQPR ELPMTIGGTR RLGGGARIDV
     VQPHRHASVL GILGNATHED ARDAIAAALH AAPAWRDTPF DERAAILLRA ADLLSGPWRQ
     RLNAATMLGQ SKTVIQAEID AVCELADFWR FNVHFARQIL AEQPLVHAPG TWNRTDHRPL
     EGFVYAITPF NFTAIAGNLP TAPALMGNVV VWKPSPTQTL AACLTMELLE AAGLPPGVIN
     LVTGDGVALS EVALTHPDLA GIHFTGSTRT FQYLWRTVGE NIARYRSYPR IVGETGGKDF
     VVAHASADVD VLRTALLRGA FEYQGQKCSA ASRAFIARSV WERMRDDFLA QVDALPMGDV
     TDFRNFLGAV IDRRAYDRLA RLLDRVRTDP TIDVLVGGTA DDSVGYFVRP TVLLGSDPSH
     EVFTTEYFGP VLAVYVYDDH AYEEVLRLVD RGAPYGLTGA IIATDRAAIL AATRQLRFAA
     GNFYINDKPT GSIVGQQPFG GSRASGTNDK AGSMANLMRW TSPRVIKETF VPPTDHRYPH
     QD
//

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