[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 25618 / H37Rv; DOI=10.1038/31159; PubMed=9634230 [NCBI, ExPASy, EBI, Israel, Japan] Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G.; "Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence."; Nature 393:537-544(1998).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=CDC 1551 / Oshkosh; DOI=10.1128/JB.184.19.5479-5490.2002; PubMed=12218036 [NCBI, ExPASy, EBI, Israel, Japan] Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.; "Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains."; J. Bacteriol. 184:5479-5490(2002).
[3]	FUNCTION, CATALYTIC ACTIVITY, AND ROLE IN TRICARBOXYLIC ACID CYCLE. STRAIN=ATCC 25618 / H37Rv; DOI=10.1073/pnas.0501605102; PubMed=16027371 [NCBI, ExPASy, EBI, Israel, Japan] Tian J., Bryk R., Itoh M., Suematsu M., Nathan C.; "Variant tricarboxylic acid cycle in Mycobacterium tuberculosis: identification of alpha-ketoglutarate decarboxylase."; Proc. Natl. Acad. Sci. U.S.A. 102:10670-10675(2005).

Comments

FUNCTION: Catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. It is believed to be the main source of succinate semialdehyde dehydrogenase activity in Mycobacterium. NAD(+) can substitute for NADP(+), but enzymatic activity is three times reduced.
CATALYTIC ACTIVITY: Succinate semialdehyde + NAD(P)⁺ + H₂O = succinate + NAD(P)H.
SIMILARITY: Belongs to the aldehyde dehydrogenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

BX842572; CAB03694.2; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE000516; AAK44465.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

F70687; F70687.

RefSeq

NP_216247.2; -.
NP_334651.1; -.

3D structure databases

HSSP

P20000; 1AG8. [HSSP ENTRY / PDB]

ModBase

P71989.

Organism-specific databases

TubercuList

Rv0234c; -.

Ontologies

GO:0009013;	Molecular function: succinate-semialdehyde dehydrogenase [NAD(P)+] activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006099;	Biological process: tricarboxylic acid cycle (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR016160; Ald_DHase_CS.
IPR016162; Ald_DHase_N.
IPR015590; Aldehyde_DHase.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.

PANTHER

PTHR11699; Aldehyde_dehyd; 1.

Pfam

PF00171; Aldedh; 1.
Pfam graphical view of domain structure.

PROSITE

PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PS00687; ALDEHYDE_DEHYDR_GLU; FALSE_NEG.

ProtoNet

P71989.

Genome annotation databases

GeneID

886732; -.
923143; -.

GenomeReviews

AE000516_GR; MT0245.
AL123456_GR; Rv0234c.

KEGG

mtc:MT0245; -.
mtu:Rv0234c; -.

TIGR

MT0245; -.

Phylogenomic databases

HOGENOM

P71989; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; NADP; Oxidoreductase; Tricarboxylic acid cycle.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 457`	`457`	`Succinate-semialdehyde dehydrogenase [NADP+] 1.`	`PRO_0000310705`
`NP_BIND`	`209 214`	`6`	`NAD or NADP (By similarity).`
`COMPBIAS`	`19 117`	`99`	`Ala-rich.`
`ACT_SITE`	`231 231`		`By similarity.`
`ACT_SITE`	`265 265`		`By similarity.`

Sequence information

Length: 457 AA [This is the length of the unprocessed precursor]

Molecular weight: 48545 Da [This is the MW of the unprocessed precursor]

CRC64: B391266C5441A05F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPIATINPAT GETVKTFTAA TDDEVDAAIA RAHRRFADYR QTSFAQRARW ANATADLLEA 

        70         80         90        100        110        120 
EADQAAAMMT LEMGKTLAAA KAEALKCAKG FRYYAENAEA LLADEPADAA KVGASAAYGR 

       130        140        150        160        170        180 
YQPLGVILAV MPWNFPLWQA VRFAAPALMA GNVGLLKHAS NVPQCALYLA DVIARGGFPD 

       190        200        210        220        230        240 
GCFQTLLVSS GAVEAILRDP RVAAATLTGS EPAGQSVGAI AGNEIKPTVL ELGGSDPFIV 

       250        260        270        280        290        300 
MPSADLDAAV STAVTGRVQN NGQSCIAAKR FIVHADIYDD FVDKFVARMA ALRVGDPTDP 

       310        320        330        340        350        360 
DTDVGPLATE QGRNEVAKQV EDAAAAGAVI RCGGKRLDRP GWFYPPTVIT DISKDMALYT 

       370        380        390        400        410        420 
EEVFGPVASV FRAANIDEAV EIANATTFGL GSNAWTRDET EQRRFIDDIV AGQVFINGMT 

       430        440        450 
VSYPELPFGG VKRSGYGREL SAHGIREFCN IKTVWIA

P71989 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools