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SSDH_PONPY
ID   SSDH_PONPY              Reviewed;         535 AA.
AC   Q6A2H2; Q6A2H3;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2004, sequence version 2.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Succinate-semialdehyde dehydrogenase, mitochondrial;
DE            EC=1.2.1.24;
DE   AltName: Full=Aldehyde dehydrogenase family 5 member A1;
DE   AltName: Full=NAD(+)-dependent succinic semialdehyde dehydrogenase;
DE   Flags: Precursor;
GN   Name=ALDH5A1;
OS   Pongo pygmaeus (Bornean orangutan).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT CYS-10.
RA   Blasi P., Malaspina P.;
RT   "Comparative analysis of succinic semialdehyde dehydrogenase in non three
RT   ape species.";
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes one step in the degradation of the inhibitory
CC       neurotransmitter gamma-aminobutyric acid (GABA). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + NAD(+) + succinate semialdehyde = 2 H(+) + NADH +
CC         succinate; Xref=Rhea:RHEA:13217, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30031, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57706, ChEBI:CHEBI:57945; EC=1.2.1.24;
CC   -!- ACTIVITY REGULATION: Redox-regulated. Inhibited under oxydizing
CC       conditions (By similarity). {ECO:0000250}.
CC   -!- PATHWAY: Amino-acid degradation; 4-aminobutanoate degradation.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; AJ621749; CAF21866.1; -; mRNA.
DR   EMBL; AJ621750; CAF21867.1; -; mRNA.
DR   BRENDA; 1.2.1.24; 9015.
DR   UniPathway; UPA00733; -.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0004777; F:succinate-semialdehyde dehydrogenase (NAD+) activity; ISS:UniProtKB.
DR   GO; GO:0007417; P:central nervous system development; ISS:UniProtKB.
DR   GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; ISS:UniProtKB.
DR   GO; GO:0006105; P:succinate metabolic process; ISS:UniProtKB.
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; IPR010102; Succ_semiAld_DH.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   TIGRFAMs; TIGR01780; SSADH; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Disulfide bond; Mitochondrion; NAD; Oxidoreductase;
KW   Phosphoprotein; Transit peptide.
FT   TRANSIT         1..47
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           48..535
FT                   /note="Succinate-semialdehyde dehydrogenase, mitochondrial"
FT                   /id="PRO_0000007187"
FT   ACT_SITE        306
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008"
FT   ACT_SITE        340
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008"
FT   BINDING         213
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         213
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         228..231
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         284..289
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         334
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         498
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            205
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         126
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P51649"
FT   MOD_RES         126
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWF0"
FT   MOD_RES         135
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWF0"
FT   MOD_RES         184
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWF0"
FT   MOD_RES         265
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWF0"
FT   MOD_RES         265
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWF0"
FT   MOD_RES         365
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWF0"
FT   MOD_RES         402
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWF0"
FT   MOD_RES         411
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWF0"
FT   MOD_RES         499
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P51649"
FT   DISULFID        340..342
FT                   /note="In inhibited form"
FT                   /evidence="ECO:0000250"
FT   VARIANT         10
FT                   /note="S -> C"
FT                   /evidence="ECO:0000269|Ref.1"
FT                   /id="VAR_019705"
SQ   SEQUENCE   535 AA;  57109 MW;  A324B14F4BC694F3 CRC64;
     MATCFWLRSS GAQRLGSTFP GCRLRPRAGG LVPASRPAPG PAQLRGYAGG LAGLSAALLR
     TDSFVGGRWL PAAATFPVQD PASGAALGMV ADCGVREARA AVRAAYEAFC SWREVSAKER
     SSLLRKWYXL MIXNKDDLAR IITAESGKPL KEAHGEILYS AFFLEWFSEE ARRVYGDIIY
     TPAKDRRALV LKQPIGVAAV ITPWNFPSAM ITRKVGAALA AGCTVVVKPA EDTPFSALAL
     AELASQAGIP SGVYNVIPCS RKNAKEVGEA ICTDPLVSKI SFTGSTTTGK ILLHHAANSV
     KRVSMELGGL APFIVFDSAN VDQAVAGAMA SKFRNTGQTC VCSNQFLVQR GIHDAFVKAF
     AEAMKKNLRV GNGFEEGTTQ GPLINEKAVE KVEKQVNDAV SKGATIVTGG KRHQLGKNFF
     EPTLLCNVTQ DMLCTHEETF GPLAPVIKFN TEEEAIAIAN AADVGLAGYF YSQDPAQIWR
     VAEQLEVGMV GVNEGLISSV ECPFGGVKQS GLGREGSKYG IDEYLELKYV CYGGL
 
 
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