Reviewed, UniProtKB/Swiss-Prot Q9XBQ9 (STHA_AZOVI)

Names and origin

Protein names

Recommended name:
    Soluble pyridine nucleotide transhydrogenase
      Short name=STH
    EC=1.6.1.1
Alternative name(s):
    NAD(P)(+) transhydrogenase [B-specific]

Gene names

Name:	sthA
Synonyms:	sth

Organism

Azotobacter vinelandii

Taxonomic identifier

354 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Azotobacter

Protein attributes

Sequence length	464 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Conversion of NADPH, generated by peripheral catabolic pathways, to NADH, which can enter the respiratory chain for energy generation. HAMAP MF_00247
Catalytic activity	NADPH + NAD+ = NADP+ + NADH. HAMAP MF_00247
Cofactor	Binds 1 FAD per subunit. HAMAP MF_00247
Subunit structure	Homooctamer. Forms a polymeric filamentous structure in purified form. Ref.3
Subcellular location	Cytoplasm HAMAP MF_00247.
Sequence similarities	Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	FAD Flavoprotein NAD NADP
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	NADP metabolic process Inferred from electronic annotation. Source: HAMAP cell redox homeostasis Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro NAD(P)+ transhydrogenase (B-specific) activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 464	464	Soluble pyridine nucleotide transhydrogenase HAMAP MF_00247		PRO_0000068060
Regions
	Nucleotide binding	35 – 44	10	FAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9XBQ9-1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: B67F2A3365CE0781	FASTA	464	51,331
	10 20 30 40 50 60 MAVYNYDVVV IGTGPAGEGA AMNAVKAGRK VAVVDDRPQV GGNCTHLGTI PSKALRHSVR 70 80 90 100 110 120 QIMQYNNNPL FRQIGEPRWF SFADVLKSAE QVIAKQVSSR TGYYARNRID TFFGTASFCD 130 140 150 160 170 180 EHTIEVVHLN GMVETLVAKQ FVIATGSRPY RPADVDFTHP RIYDSDTILS LGHTPRRLII 190 200 210 220 230 240 YGAGVIGCEY ASIFSGLGVL VDLIDNRDQL LSFLDDEISD SLSYHLRNNN VLIRHNEEYE 250 260 270 280 290 300 RVEGLDNGVI LHLKSGKKIK ADAFLWSNGR TGNTDKLGLE NIGLKANGRG QIQVDEHYRT 310 320 330 340 350 360 EVSNIYAAGD VIGWPSLASA AYDQGRSAAG SITENDSWRF VDDVPTGIYT IPEISSVGKT 370 380 390 400 410 420 ERELTQAKVP YEVGKAFFKG MARAQIAVEK AGMLKILFHR ETLEILGVHC FGYQASEIVH 430 440 450 460 IGQAIMNQKG EANTLKYFIN TTFNYPTMAE AYRVAAYDGL NRLF

References

[1]	"Cloning of the sth gene from Azotobacter vinelandii and construction of chimeric soluble pyridine nucleotide transhydrogenases." Boonstra B., Bjorklund L., French C.E., Wainwright I., Bruce N.C. FEMS Microbiol. Lett. 191:87-93(2000) [PubMed: 11004404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 478 / NRS 16 / DSM 2289 / VKM B-1617.
[2]	"Pyridine nucleotide transhydrogenase from Azotobacter vinelandii. Improved purification, physical properties and subunit arrangement in purified polymers." Voordouw G., van der Vies S.M., Eweg J.K., Veeger C., van Breemen J.F.L., van Bruggen E.F.J. Eur. J. Biochem. 111:347-355(1980) [PubMed: 7460901] [Abstract] Cited for: CHARACTERIZATION. Strain: ATCC 478 / NRS 16 / DSM 2289 / VKM B-1617.
[3]	"Structure of pyridine nucleotide transhydrogenase from Azotobacter vinelandii." Voordouw G., Veeger C., van Breemen J.F.L., van Bruggen E.F.J. Eur. J. Biochem. 98:447-454(1979) [PubMed: 39756] [Abstract] Cited for: SUBUNIT. Strain: ATCC 478 / NRS 16 / DSM 2289 / VKM B-1617.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF159108 Genomic DNA. Translation: AAD40691.1.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.6.1.1. 883.
Family and domain databases
HAMAP	MF_00247. SthA. [Tree]
InterPro	IPR016156. FAD/NAD-linked_Rdtase_dimer. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR000815. Hg_reductase. IPR004099. Pyr_nucl-diS_OxRdtase_dimer. IPR001327. Pyr_OxRdtase_NAD_bd. [Graphical view]
Gene3D	G3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
Pfam	PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. PF02852. Pyr_redox_dim. 1 hit. [Graphical view]
PRINTS	PR00368. FADPNR. PR00945. HGRDTASE.
ProtoNet	Search...

Entry information

Entry name

STHA_AZOVI

Accession

Primary (citable) accession number: Q9XBQ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1999
Last modified:	February 9, 2010
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)