ID GABD2_MYCTU Reviewed; 518 AA.
AC P9WNX7; L0T7R6; P96417; Q7D824;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=Rv1731;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16027371; DOI=10.1073/pnas.0501605102;
RA Tian J., Bryk R., Itoh M., Suematsu M., Nathan C.;
RT "Variant tricarboxylic acid cycle in Mycobacterium tuberculosis:
RT identification of alpha-ketoglutarate decarboxylase.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:10670-10675(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011445;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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). NAD(+) can substitute for NADP(+), but enzymatic activity
CC is three times reduced. {ECO:0000269|PubMed:16027371}.
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 Evidence={ECO:0000269|PubMed:16027371};
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP44497.1; -; Genomic_DNA.
DR PIR; H70962; H70962.
DR RefSeq; NP_214748.2; NC_000962.3.
DR RefSeq; WP_003898989.1; NZ_NVQJ01000010.1.
DR AlphaFoldDB; P9WNX7; -.
DR SMR; P9WNX7; -.
DR STRING; 83332.Rv1731; -.
DR PaxDb; 83332-Rv1731; -.
DR GeneID; 885204; -.
DR KEGG; mtu:Rv1731; -.
DR TubercuList; Rv1731; -.
DR eggNOG; COG1012; Bacteria.
DR InParanoid; P9WNX7; -.
DR OrthoDB; 6882680at2; -.
DR PhylomeDB; P9WNX7; -.
DR SABIO-RK; P9WNX7; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0036243; F:succinate-semialdehyde dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0009013; F:succinate-semialdehyde dehydrogenase [NAD(P)+] activity; IDA:MTBBASE.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IDA:MTBBASE.
DR CDD; cd07101; ALDH_SSADH2_GabD2; 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 PANTHER; PTHR11699:SF211; ALDEHYDE DEHYDROGENASE FAMILY 16 MEMBER A1; 1.
DR PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..518
FT /note="Putative succinate-semialdehyde dehydrogenase
FT [NADP(+)] 2"
FT /id="PRO_0000310711"
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
//
