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P71989 (GABD1_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Succinate-semialdehyde dehydrogenase [NADP+] 1
Short name=SSADH 1
Short name=SSDH 1
EC=1.2.1.79
Gene names
Name:gabD1
Ordered Locus Names:Rv0234c, MT0245
OrganismMycobacterium tuberculosis
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length457 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (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. Ref.3

Catalytic activity

Succinate semialdehyde + NADP+ + H2O = succinate + NADPH. Ref.3

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Sequence caution

The sequence AAK44465.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAB03694.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processtricarboxylic acid cycle

Inferred from direct assay Ref.3. Source: MTBBASE

   Cellular componentplasma membrane

Inferred from direct assay. Source: MTBBASE

   Molecular functionsuccinate-semialdehyde dehydrogenase [NAD(P)+] activity

Inferred from direct assay Ref.3. Source: MTBBASE

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 457457Succinate-semialdehyde dehydrogenase [NADP+] 1
PRO_0000310705

Regions

Nucleotide binding133 – 1342NADP By similarity
Nucleotide binding157 – 1604NADP By similarity
Nucleotide binding209 – 2102NADP By similarity
Compositional bias19 – 11799Ala-rich

Sites

Active site2311Proton acceptor By similarity
Active site2651Nucleophile By similarity
Binding site2321NADP; via carbonyl oxygen By similarity
Binding site3621NADP By similarity

Sequences

Sequence LengthMass (Da)Tools
P71989 [UniParc].

Last modified November 13, 2007. Version 3.
Checksum: B391266C5441A05F

FASTA45748,545
        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

« Hide

References

« Hide 'large scale' references
[1]"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence."
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. expand/collapse author list , 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.
Nature 393:537-544(1998) [PubMed: 9634230] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25618 / H37Rv.
[2]"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains."
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. expand/collapse author list , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.
J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CDC 1551 / Oshkosh.
[3]"Variant tricarboxylic acid cycle in Mycobacterium tuberculosis: identification of alpha-ketoglutarate decarboxylase."
Tian J., Bryk R., Itoh M., Suematsu M., Nathan C.
Proc. Natl. Acad. Sci. U.S.A. 102:10670-10675(2005) [PubMed: 16027371] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, ROLE IN TRICARBOXYLIC ACID CYCLE.
Strain: ATCC 25618 / H37Rv.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX842572 Genomic DNA. Translation: CAB03694.2. Different initiation.
AE000516 Genomic DNA. Translation: AAK44465.1. Different initiation.
PIRF70687.
RefSeqNP_216247.2. NC_000962.2.
NP_334651.1. NC_002755.2.

3D structure databases

HSSPHSSP built from PDB template 1ZUM based on UniProtKB P05091.
ProteinModelPortalP71989.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000001861; EBMYCP00000001861; EBMYCG00000001859.
EBMYCT00000069175; EBMYCP00000067234; EBMYCG00000069170.
GeneID886732.
923143.
GenomeReviewsGene locus MT0245 in contig AE000516_GR.
Gene locus Rv0234c in contig AL123456_GR.
KEGGmtc:MT0245.
mtu:Rv0234c.
PATRIC18122259. VBIMycTub22151_0264.
TIGRMT0245.

Organism-specific databases

TubercuListRv0234c.

Phylogenomic databases

GeneTreeEBGT00050000015659.
HOGENOMHBG752218.
OMAVPQSALY.
PhylomeDBP71989.
ProtClustDBPRK09406.

Family and domain databases

InterProIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view]
Gene3DG3DSA:3.40.309.10. Aldehyde_dehydrogenase_C. 1 hit.
G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
KOK00135.
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMSSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGABD1_MYCTU
AccessionPrimary (citable) accession number: P71989
Secondary accession number(s): Q7DA77
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: November 13, 2007
Last modified: January 25, 2012
This is version 73 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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