GABD2_MYCBO
ID GABD2_MYCBO Reviewed; 518 AA.
AC Q7TZP3; A0A1R3Y1A6; X2BIY8;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Putative succinate-semialdehyde dehydrogenase [NADP(+)] 2;
DE Short=SSADH 2;
DE Short=SSDH 2;
DE EC=1.2.1.79;
GN Name=gabD2; OrderedLocusNames=BQ2027_MB1760;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
CC -!- FUNCTION: Catalyzes the NADP(+)-dependent oxidation of succinate
CC semialdehyde to succinate. Although it has succinate semialdehyde
CC dehydrogenase activity, is likely to act physiologically on a different
CC aldehyde(s) (By similarity). {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 -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; LT708304; SIU00363.1; -; Genomic_DNA.
DR RefSeq; NP_855412.1; NC_002945.3.
DR RefSeq; WP_003898989.1; NC_002945.4.
DR AlphaFoldDB; Q7TZP3; -.
DR SMR; Q7TZP3; -.
DR EnsemblBacteria; SIU00363; SIU00363; BQ2027_MB1760.
DR PATRIC; fig|233413.5.peg.1921; -.
DR OMA; NWNKQLT; -.
DR Proteomes; UP000001419; Chromosome.
DR GO; GO:0036243; F:succinate-semialdehyde dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
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 Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW NADP; Oxidoreductase.
FT CHAIN 1..518
FT /note="Putative succinate-semialdehyde dehydrogenase
FT [NADP(+)] 2"
FT /id="PRO_0000310708"
FT ACT_SITE 254
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT ACT_SITE 288
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT BINDING 157..158
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 181..184
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 232..233
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 255
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 386
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 518 AA; 55324 MW; E3AC9E895EB46270 CRC64;
MPAPSAEVFD RLRNLAAIKD VAARPTRTID EVFTGKPLTT IPVGTAADVE AAFAEARAAQ
TDWAKRPVIE RAAVIRRYRD LVIENREFLM DLLQAEAGKA RWAAQEEIVD LIANANYYAR
VCVDLLKPRK AQPLLPGIGK TTVCYQPKGV VGVISPWNYP MTLTVSDSVP ALVAGNAVVL
KPDSQTPYCA LACAELLYRA GLPRALYAIV PGPGSVVGTA ITDNCDYLMF TGSSATGSRL
AEHAGRRLIG FSAELGGKNP MIVARGANLD KVAKAATRAC FSNAGQLCIS IERIYVEKDI
AEEFTRKFGD AVRNMKLGTA YDFSVDMGSL ISEAQLKTVS GHVDDATAKG AKVIAGGKAR
PDIGPLFYEP TVLTNVAPEM ECAANETFGP VVSIYPVADV DEAVEKANDT DYGLNASVWA
GSTAEGQRIA ARLRSGTVNV DEGYAFAWGS LSAPMGGMGL SGVGRRHGPE GLLKYTESQT
IATARVFNLD PPFGIPATVW QKSLLPIVRT VMKLPGRR