NAD-reducing hydrogenase hoxS subunit alpha - Ralstonia eutropha (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)

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Reviewed, UniProtKB/Swiss-Prot P22317 (HOXF_RALEH)

Last modified June 16, 2009. Version 79. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
NAD-reducing hydrogenase hoxS subunit alpha
EC=1.12.1.2

Gene names

Name:	hoxF
Ordered Locus Names:	PHG088

Encoded on

Plasmid megaplasmid pHG1

Organism

Ralstonia eutropha (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)) [Complete proteome] [HAMAP]

Taxonomic identifier

381666 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus

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Protein attributes

Sequence length	602 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Subunits alpha and gamma of hoxS constitute an NADH--oxidoreductase.
Catalytic activity	H₂ + NAD⁺ = H⁺ + NADH.
Cofactor	Binds 1 FMN Potential. Binds 1 4Fe-4S cluster Potential.
Subunit structure	Tetramer of an alpha and a gamma subunits (flavin-containing dimer), and a delta and a nickel-containing beta subunit (hydrogenase dimer).
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the complex I 51 kDa subunit family.

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Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	4Fe-4S FMN Flavoprotein Iron Iron-sulfur Metal-binding NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome Direct protein sequencing Plasmid
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW FMN binding Inferred from electronic annotation. Source: InterPro NAD or NADH binding Inferred from electronic annotation. Source: InterPro NADH dehydrogenase (ubiquinone) activity Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro hydrogen dehydrogenase activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 602

602

NAD-reducing hydrogenase hoxS subunit alpha

PRO_0000118564

Regions

Nucleotide binding

219 – 228

NAD By similarity

Nucleotide binding

332 – 379

FMN By similarity

Sites

Metal binding

499

Iron-sulfur (4Fe-4S) Potential

Metal binding

502

Iron-sulfur (4Fe-4S) Potential

Metal binding

505

Iron-sulfur (4Fe-4S) Potential

Metal binding

545

Iron-sulfur (4Fe-4S) Potential

Experimental info

Sequence conflict

W → G AA sequence Ref.3

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Sequences

Sequence

Length

Mass (Da)

Tools

P22317-1 [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: B7D9BBB11AB53F6C
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FASTA

602

66,784

        10         20         30         40         50         60 
MDSRITTILE RYRSDRTRLI DILWDVQHEY GHIPDAVLPQ LGAGLKLSPL DIRETASFYH 

        70         80         90        100        110        120 
FFLDKPSGKY RIYLCNSVIA KINGYQAVRE ALERETGIRF GETDPNGMFG LFDTPCIGLS 

       130        140        150        160        170        180 
DQEPAMLIDK VVFTRLRPGK ITDIIAQLKQ GRSPAEIANP AGLPSQDIAY VDAMVESNVR 

       190        200        210        220        230        240 
TKGPVFFRGR TDLRSLLDQC LLLKPEQVIE TIVDSRLRGR GGAGFSTGLK WRLCRDAESE 

       250        260        270        280        290        300 
QKYVICNADE GEPGTFKDRV LLTRAPKKVF VGMVIAAYAI GCRKGIVYLR GEYFYLKDYL 

       310        320        330        340        350        360 
ERQLQELRED GLLGRAIGGR AGFDFDIRIQ MGAGAYICGD ESALIESCEG KRGTPRVKPP 

       370        380        390        400        410        420 
FPVQQGYLGK PTSVNNVETF AAVSRIMEEG ADWFRAMGTP DSAGTRLLSV AGDCSKPGIY 

       430        440        450        460        470        480 
EVEWGVTLNE VLAMVGARDA RAVQISGPSG ECVSVAKDGE RKLAYEDLSC NGAFTIFNCK 

       490        500        510        520        530        540 
RDLLEIVRDH MQFFVEESCG ICVPCRAGNV DLHRKVEWVI AGKACQKDLD DMVSWGALVR 

       550        560        570        580        590        600 
RTSRCGLGAT SPKPILTTLE KFPEIYQNKL VRHEGPLLPS FDLDTALGGY EKALKDLEEV 


TR

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and nucleotide sequences of the genes for the subunits of NAD-reducing hydrogenase of Alcaligenes eutrophus H16." Tran-Betcke A., Warnecke U., Boecker C., Zaborosch C., Friedrich B. J. Bacteriol. 172:2920-2929(1990) [PubMed: 2188945] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16 megaplasmid encoding key enzymes of H(2)-based lithoautotrophy and anaerobiosis." Schwartz E., Henne A., Cramm R., Eitinger T., Friedrich B., Gottschalk G. J. Mol. Biol. 332:369-383(2003) [PubMed: 12948488] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Comparison of the NH2-terminal amino acid sequences of the four non-identical subunits of the NAD-linked hydrogenases from Nocardia opaca 1b and Alcaligenes eutrophus H16." Zaborosch C., Schneider K., Schlegel H.G., Kratzin H. Eur. J. Biochem. 181:175-180(1989) [PubMed: 2496982] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-27.

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Cross-references

Sequence databases
	M55230 Genomic DNA. Translation: AAC06140.1. AY305378 Genomic DNA. Translation: AAP85841.1.
PIR	A35385.
RefSeq	NP_942727.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2656814.
GenomeReviews	Gene locus PHG088 in contig AY305378_GR.
KEGG	reh:PHG088.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P22317.
OMA	P22317. FCTPCRV.
Enzyme and pathway databases
BioCyc	MetaCyc:HOXFALCA-MON.
BRENDA	1.12.1.2. 275933.
Family and domain databases
InterPro	IPR001949. NADH-UbQ_OxRdtase_51KDa_CS. IPR019575. NADH-UbQ_OxRdtase_Fsu_4Fe4S-bd. IPR011538. NADH_UbQ_OxRdtase_51KDa_su. IPR002023. NADH_UbQ_OxRdtase_su-24kDa. [Graphical view]
Pfam	PF01257. Complex1_24kDa. 1 hit. PF01512. Complex1_51K. 1 hit. PF10589. NADH_4Fe-4S. 1 hit. [Graphical view]
ProDom	PD003859. Cmplx1_24kDa. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00644. COMPLEX1_51K_1. 1 hit. PS00645. COMPLEX1_51K_2. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

HOXF_RALEH

Accession

Primary (citable) accession number: P22317

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	August 1, 1991
Last modified:	June 16, 2009
This is version 79 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)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents