TGNE_ACIAD
ID TGNE_ACIAD Reviewed; 483 AA.
AC Q6F9G0;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Succinate semialdehyde dehydrogenase {ECO:0000303|PubMed:29686076};
DE Short=SSA dehydrogenase {ECO:0000303|PubMed:29686076};
DE EC=1.2.1.24 {ECO:0000269|PubMed:29686076};
GN Name=tgnE {ECO:0000303|PubMed:29686076};
GN Synonyms=gabD {ECO:0000312|EMBL:CAG69304.1};
GN OrderedLocusNames=ACIAD2539 {ECO:0000312|EMBL:CAG69304.1};
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1 {ECO:0000312|Proteomes:UP000000430};
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=29686076; DOI=10.1073/pnas.1722368115;
RA Perchat N., Saaidi P.L., Darii E., Pelle C., Petit J.L., Besnard-Gonnet M.,
RA de Berardinis V., Dupont M., Gimbernat A., Salanoubat M., Fischer C.,
RA Perret A.;
RT "Elucidation of the trigonelline degradation pathway reveals previously
RT undescribed enzymes and metabolites.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E4358-E4367(2018).
CC -!- FUNCTION: Involved in the degradation of the pyridine ring of
CC trigonelline (TG; N-methylnicotinate) into succinate and methylamine as
CC carbon and nitrogen sources, respectively. Catalyzes the NAD(+)-
CC dependent oxidation of succinate semialdehyde to succinate.
CC {ECO:0000269|PubMed:29686076}.
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 Evidence={ECO:0000269|PubMed:29686076};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=72 uM for succinate semialdehyde (SSA)
CC {ECO:0000269|PubMed:29686076};
CC KM=107 uM for NAD {ECO:0000269|PubMed:29686076};
CC Note=kcat is 61.5 sec(-1) for NAD as substrate.
CC {ECO:0000269|PubMed:29686076};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:29686076}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR543861; CAG69304.1; -; Genomic_DNA.
DR RefSeq; WP_004928612.1; NC_005966.1.
DR AlphaFoldDB; Q6F9G0; -.
DR SMR; Q6F9G0; -.
DR STRING; 62977.ACIAD2539; -.
DR EnsemblBacteria; CAG69304; CAG69304; ACIAD2539.
DR GeneID; 45234823; -.
DR KEGG; aci:ACIAD2539; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_5_1_6; -.
DR OMA; WHKLIEQ; -.
DR OrthoDB; 384611at2; -.
DR BioCyc; ASP62977:ACIAD_RS11530-MON; -.
DR Proteomes; UP000000430; Chromosome.
DR GO; GO:0004777; F:succinate-semialdehyde dehydrogenase (NAD+) activity; IDA:UniProtKB.
DR GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; IEA:InterPro.
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 1: Evidence at protein level;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..483
FT /note="Succinate semialdehyde dehydrogenase"
FT /id="PRO_0000445263"
FT ACT_SITE 255
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P25526"
FT ACT_SITE 289
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P25526"
FT BINDING 156..157
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P25526"
FT BINDING 180..183
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P25526"
FT BINDING 233..234
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P25526"
FT BINDING 256
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P25526"
FT BINDING 386
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P25526"
SQ SEQUENCE 483 AA; 52472 MW; 7895707A52CC17F5 CRC64;
MDLQQQPLFR QKALVAGQWC DADNAEKTPI FNPATQELIG YVPNMGRAET ERAIEAAYAS
WEMWKTKTAK ERSALLKKWY DLILLNLDVL AEILTTEQGK PFNEAKGEII YAASFIEWFA
EEAKRIYGDI IPSPYPDARI VVNKQPIGVV AAITPWNFPA AMITRKVAPA LAAGCPCIVK
PAPETPFTAL ALADLAIQAG IPAEIMSVVT GDAAQIGDAI FASDHVRKFT FTGSTPIGKL
LLEKSAKTLK KVSLELGGNA PFIVFDDADI EAAVEGALIA KFRNAGQTCV CVNRFLVQSG
VYEKFIQVFK AKIESLKIGN GLEAGSEIGP LINAQAVAKV QSHIEDALSK NGRLITGGQV
HATGELFFEP TLIADANTEM MVATQETFGP LAAIFKFDTE QQAIQMANDT EFGLAAYCYT
RDLGRAWRMS EQLEYGMVGI NKGLISNEVA PFGGIKHSGL GREGSKYGIE DYLEIKYTLF
GGL
