GABD1_MYCTU
ID GABD1_MYCTU Reviewed; 457 AA.
AC P9WNX9; L0T5V9; P71989; Q7DA77;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Succinate-semialdehyde dehydrogenase [NADP(+)] 1;
DE Short=SSADH 1;
DE Short=SSDH 1;
DE EC=1.2.1.79;
GN Name=gabD1; OrderedLocusNames=Rv0234c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; 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, CATALYTIC ACTIVITY, AND ROLE IN TRICARBOXYLIC ACID CYCLE.
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.m111.011627;
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. It is believed to be the main source of
CC succinate semialdehyde dehydrogenase activity in Mycobacterium. NAD(+)
CC can substitute for NADP(+), but enzymatic activity is three times
CC 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CCP42962.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL123456; CCP42962.1; ALT_INIT; Genomic_DNA.
DR PIR; F70687; F70687.
DR RefSeq; NP_216247.2; NC_000962.3.
DR RefSeq; WP_003912534.1; NC_018143.2.
DR AlphaFoldDB; P9WNX9; -.
DR SMR; P9WNX9; -.
DR STRING; 83332.Rv0234c; -.
DR PaxDb; P9WNX9; -.
DR DNASU; 886732; -.
DR GeneID; 45424206; -.
DR GeneID; 886732; -.
DR KEGG; mtu:Rv0234c; -.
DR PATRIC; fig|83332.12.peg.263; -.
DR TubercuList; Rv0234c; -.
DR eggNOG; COG1012; Bacteria.
DR OMA; KAMRWYA; -.
DR BioCyc; MetaCyc:G185E-4354-MON; -.
DR BRENDA; 1.2.1.79; 3445.
DR SABIO-RK; P9WNX9; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0004030; F:aldehyde dehydrogenase [NAD(P)+] activity; IEA:InterPro.
DR GO; GO:0004777; F:succinate-semialdehyde dehydrogenase (NAD+) activity; IBA:GO_Central.
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; cd07100; ALDH_SSADH1_GabD1; 1.
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; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR044148; ALDH_GabD1-like.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE 1: Evidence at protein level;
KW NADP; Oxidoreductase; Reference proteome; Tricarboxylic acid cycle.
FT CHAIN 1..457
FT /note="Succinate-semialdehyde dehydrogenase [NADP(+)] 1"
FT /id="PRO_0000310705"
FT ACT_SITE 231
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT ACT_SITE 265
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 133..134
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 157..160
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 209..210
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 362
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 457 AA; 48545 MW; B391266C5441A05F CRC64;
MPIATINPAT GETVKTFTAA TDDEVDAAIA RAHRRFADYR QTSFAQRARW ANATADLLEA
EADQAAAMMT LEMGKTLAAA KAEALKCAKG FRYYAENAEA LLADEPADAA KVGASAAYGR
YQPLGVILAV MPWNFPLWQA VRFAAPALMA GNVGLLKHAS NVPQCALYLA DVIARGGFPD
GCFQTLLVSS GAVEAILRDP RVAAATLTGS EPAGQSVGAI AGNEIKPTVL ELGGSDPFIV
MPSADLDAAV STAVTGRVQN NGQSCIAAKR FIVHADIYDD FVDKFVARMA ALRVGDPTDP
DTDVGPLATE QGRNEVAKQV EDAAAAGAVI RCGGKRLDRP GWFYPPTVIT DISKDMALYT
EEVFGPVASV FRAANIDEAV EIANATTFGL GSNAWTRDET EQRRFIDDIV AGQVFINGMT
VSYPELPFGG VKRSGYGREL SAHGIREFCN IKTVWIA
