GABD_SINFN
ID GABD_SINFN Reviewed; 491 AA.
AC P55653;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Probable succinate-semialdehyde dehydrogenase [NADP(+)];
DE Short=SSDH;
DE EC=1.2.1.79;
GN Name=gabD; OrderedLocusNames=NGR_a01630; ORFNames=y4sJ;
OS Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OG Plasmid sym pNGR234a.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=394;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234;
RX PubMed=9163424; DOI=10.1038/387394a0;
RA Freiberg C.A., Fellay R., Bairoch A., Broughton W.J., Rosenthal A.,
RA Perret X.;
RT "Molecular basis of symbiosis between Rhizobium and legumes.";
RL Nature 387:394-401(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234;
RX PubMed=19376903; DOI=10.1128/aem.00515-09;
RA Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT systems.";
RL Appl. Environ. Microbiol. 75:4035-4045(2009).
CC -!- FUNCTION: Catalyzes the NADP(+) dependent oxidation of succinate
CC semialdehyde to succinate. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NADP(+) + succinate semialdehyde = 2 H(+) + NADPH +
CC succinate; Xref=Rhea:RHEA:13213, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30031, ChEBI:CHEBI:57706,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.2.1.79;
CC -!- PATHWAY: Amino-acid degradation; 4-aminobutanoate degradation.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; U00090; AAB91849.1; -; Genomic_DNA.
DR PIR; S43963; S43963.
DR RefSeq; NP_444062.1; NC_000914.2.
DR RefSeq; WP_010875199.1; NC_000914.2.
DR AlphaFoldDB; P55653; -.
DR SMR; P55653; -.
DR STRING; 394.NGR_a01630; -.
DR PRIDE; P55653; -.
DR EnsemblBacteria; AAB91849; AAB91849; NGR_a01630.
DR KEGG; rhi:NGR_a01630; -.
DR PATRIC; fig|394.7.peg.153; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_5_1_5; -.
DR OMA; RRCFELM; -.
DR OrthoDB; 384611at2; -.
DR UniPathway; UPA00733; -.
DR Proteomes; UP000001054; Plasmid sym pNGR234a.
DR GO; GO:0036243; F:succinate-semialdehyde dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; IEA:UniProtKB-UniPathway.
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; 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; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW NADP; Oxidoreductase; Plasmid; Reference proteome.
FT CHAIN 1..491
FT /note="Probable succinate-semialdehyde dehydrogenase
FT [NADP(+)]"
FT /id="PRO_0000056573"
FT ACT_SITE 263
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT ACT_SITE 297
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT BINDING 163..164
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 187..190
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 241..242
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 394
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 491 AA; 53254 MW; FC54C5DF7B4D1B14 CRC64;
MTLTSALTRH LKCPELFRNL ANEPHPSVAG QRQRFSVFNP STGELLAEVP DMGAADAHAA
IERADAAQEP WSGLTARARS DILWKWHRFI LEHSDDLAAI LTAEMGKPLG EAKSEVQHAA
AYLQWYAEEA NRIYGETISA PSTDRRMLVI KQPIGVVGAI TPWNFPASMV ARKISPALAA
GCTVVLKPAE QTPLVAGAMF ALAKLAGFPD GVLNLVYASE GDAIGRELCT NPKVRKISFT
GSTEVGRLLM RQCSDQIKRI SFELGGNAPF IVFDDADIDA AVDGAIQAKF RNAGQTCVSA
NRIYVQSGVY AEFAEKFTER VRTLKVGDGF DPNVAIGPLI NQEALKKIEL HISDAVQKGA
RVRSGGRRTG SSGTFFEPTV VTDVSKTMRL AEEETFGPLA PLLRFDDADH VVREANDTIY
GLAAYFYASN LKRVWRVAEA LEYGMVGINT GRMSSEAAPF GGVKQSGIGR EGSRHGLEDY
LDMKYLCVGG L