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ABDH_ECO57
ID   ABDH_ECO57              Reviewed;         474 AA.
AC   Q8X9W5; Q7AE53;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Gamma-aminobutyraldehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01275};
DE            Short=ABALDH {ECO:0000255|HAMAP-Rule:MF_01275};
DE            EC=1.2.1.19 {ECO:0000255|HAMAP-Rule:MF_01275};
DE   AltName: Full=1-pyrroline dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01275};
DE   AltName: Full=4-aminobutanal dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01275};
DE   AltName: Full=5-aminopentanal dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01275};
DE            EC=1.2.1.- {ECO:0000255|HAMAP-Rule:MF_01275};
GN   Name=patD {ECO:0000255|HAMAP-Rule:MF_01275};
GN   OrderedLocusNames=Z2275, ECs2048;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Catalyzes the oxidation 4-aminobutanal (gamma-
CC       aminobutyraldehyde) to 4-aminobutanoate (gamma-aminobutyrate or GABA).
CC       This is the second step in one of two pathways for putrescine
CC       degradation, where putrescine is converted into 4-aminobutanoate via 4-
CC       aminobutanal. Also functions as a 5-aminopentanal dehydrogenase in a a
CC       L-lysine degradation pathway to succinate that proceeds via cadaverine,
CC       glutarate and L-2-hydroxyglutarate. {ECO:0000255|HAMAP-Rule:MF_01275}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-aminobutanal + H2O + NAD(+) = 4-aminobutanoate + 2 H(+) +
CC         NADH; Xref=Rhea:RHEA:19105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58264,
CC         ChEBI:CHEBI:59888; EC=1.2.1.19; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01275};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19106;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01275};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-aminopentanal + H2O + NAD(+) = 5-aminopentanoate + 2 H(+) +
CC         NADH; Xref=Rhea:RHEA:61632, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:144896,
CC         ChEBI:CHEBI:356010; Evidence={ECO:0000255|HAMAP-Rule:MF_01275};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61633;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01275};
CC   -!- PATHWAY: Amine and polyamine degradation; putrescine degradation; 4-
CC       aminobutanoate from 4-aminobutanal: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01275}.
CC   -!- PATHWAY: Amino-acid degradation. {ECO:0000255|HAMAP-Rule:MF_01275}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01275}.
CC   -!- MISCELLANEOUS: 4-aminobutanal can spontaneously cyclize to 1-pyrroline,
CC       and 5-aminopentanal to 1-piperideine. {ECO:0000255|HAMAP-
CC       Rule:MF_01275}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. Gamma-
CC       aminobutyraldehyde dehydrogenase subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_01275}.
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DR   EMBL; AE005174; AAG56331.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB35471.1; -; Genomic_DNA.
DR   PIR; G85733; G85733.
DR   PIR; H90884; H90884.
DR   RefSeq; NP_310075.1; NC_002695.1.
DR   RefSeq; WP_001163885.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; Q8X9W5; -.
DR   SMR; Q8X9W5; -.
DR   STRING; 155864.EDL933_2206; -.
DR   EnsemblBacteria; AAG56331; AAG56331; Z2275.
DR   EnsemblBacteria; BAB35471; BAB35471; ECs_2048.
DR   GeneID; 917246; -.
DR   KEGG; ece:Z2275; -.
DR   KEGG; ecs:ECs_2048; -.
DR   PATRIC; fig|386585.9.peg.2148; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_0_0_6; -.
DR   OMA; NDDLGEV; -.
DR   UniPathway; UPA00188; UER00292.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0033737; F:1-pyrroline dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019145; F:aminobutyraldehyde dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019477; P:L-lysine catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009447; P:putrescine catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd07092; ALDH_ABALDH-YdcW; 1.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 1.
DR   HAMAP; MF_01275; Aldedh_Prr; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR015657; Aminobutyraldehyde_DH.
DR   InterPro; IPR017749; PatD.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   TIGRFAMs; TIGR03374; ABALDH; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..474
FT                   /note="Gamma-aminobutyraldehyde dehydrogenase"
FT                   /id="PRO_0000269692"
FT   ACT_SITE        246
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01275"
FT   ACT_SITE        280
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01275"
FT   BINDING         146..148
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01275"
FT   BINDING         172..175
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01275"
FT   BINDING         209
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01275"
FT   BINDING         225..228
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01275"
FT   BINDING         280
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01275"
SQ   SEQUENCE   474 AA;  50900 MW;  3C5A470E8869FA11 CRC64;
     MQHKLLINGE LVSGEGEKQP VYNPATGDVL LEIAEASAEQ VDAAVRAADA AFAEWGQTTP
     KVRAECLLKL ADVIEENGQV FAELESRNCG KPLHSAFNDE IPAIVDVFRF FAGAARCLNG
     LAAGEYLEGH TSMIRRDPLG VVASIAPWNY PLMMAAWKLA PALAAGNCVV LKPSEITPLT
     ALKLAELAKD IFPAGVINVL FGRGKTVGDP LTGHPKVRMV SLTGSIATGE HIISHTAPSI
     KRTHMELGGK APVIVFDDAD IEAVVEGVRT FGYYNAGQDC TVACRIYAQK GIYDTLVEKL
     GAAVATLKSG APDDESTELG PLSSLAHLER VSKAVEEAKA TGHIKVITGG EKRKGNGYYY
     APTLLAGALQ DDAIVQKEVF GPVVSVTLFD NEEQVVNWAN DSQYGLASSV WTKDVGRAHR
     VSARLQYGCT WVNTHFMLVS EMPHGGQKLS GYGKDMSLYG LEDYTVVRHV MVKH
 
 
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