[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=2188945 [NCBI, ExPASy, EBI, Israel, Japan] Tran-Betcke A., Warnecke U., Boecker C., Zaborosch C., Friedrich B.; "Cloning and nucleotide sequences of the genes for the subunits of NAD-reducing hydrogenase of Alcaligenes eutrophus H16."; J. Bacteriol. 172:2920-2929(1990).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1016/S0022-2836(03)00894-5; PubMed=12948488 [NCBI, ExPASy, EBI, Israel, Japan] Schwartz E., Henne A., Cramm R., Eitinger T., Friedrich B., Gottschalk G.; "Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16 megaplasmid encoding key enzymes of H(2)-based lithoautotrophy and anaerobiosis."; J. Mol. Biol. 332:369-383(2003).
[3]	PROTEIN SEQUENCE OF 1-27. PubMed=2496982 [NCBI, ExPASy, EBI, Israel, Japan] Zaborosch C., Schneider K., Schlegel H.G., Kratzin H.; "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."; Eur. J. Biochem. 181:175-180(1989).

Comments

FUNCTION: Subunits alpha and gamma of hoxS constitute an NADH--oxidoreductase.
CATALYTIC ACTIVITY: H₂ + NAD⁺ = H⁺ + NADH.
COFACTOR: Binds 1 FMN (Potential).
COFACTOR: Binds 1 4Fe-4S cluster (Potential).
SUBUNIT: 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.
SIMILARITY: Belongs to the complex I 51 kDa subunit 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

M55230; AAC06140.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY305378; AAP85841.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A35385; A35385.

RefSeq

NP_942727.1; -.

3D structure databases

ModBase

P22317.

Enzyme and pathway databases

BioCyc

MetaCyc:HOXFALCA-MON; -.

Family and domain databases

InterPro

IPR001949; NADH-ubq_OxRdtase_51KDa_CS.
IPR011538; NADH-UbQ_OxRdtase_51KDa_su.
IPR002023; NADH_DHase_Ub_24kDa_su.
Graphical view of domain structure.

Pfam

PF01257; Complex1_24kDa; 1.
PF01512; Complex1_51K; 1.
Pfam graphical view of domain structure.

ProDom

PD003859; Cmplx1_24kDa; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00644; COMPLEX1_51K_1; 1.
PS00645; COMPLEX1_51K_2; 1.

BLOCKS

P22317.

Genome annotation databases

GeneID

2656814; -.

GenomeReviews

AY305378_GR; PHG088.

KEGG

reh:PHG088; -.

Phylogenomic databases

HOGENOM

P22317; -.

Genome annotation databases

CMR

P22317; PHG088.

Other

ProtoNet

P22317.

UniRef

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

Keywords

4Fe-4S; Complete proteome; Cytoplasm; Direct protein sequencing; Flavoprotein; FMN; Iron; Iron-sulfur; Metal-binding; NAD; Oxidoreductase; Plasmid.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 602`	`602`	`NAD-reducing hydrogenase hoxS subunit alpha.`	`PRO_0000118564`
`NP_BIND`	`219 228`	`10`	`NAD (By similarity).`
`NP_BIND`	`332 379`	`48`	`FMN (By similarity).`
`METAL`	`499 499`		`Iron-sulfur (4Fe-4S) (Potential).`
`METAL`	`502 502`		`Iron-sulfur (4Fe-4S) (Potential).`
`METAL`	`505 505`		`Iron-sulfur (4Fe-4S) (Potential).`
`METAL`	`545 545`		`Iron-sulfur (4Fe-4S) (Potential).`
`CONFLICT`	`24 24`		`W -> G (in Ref. 3; AA sequence).`

Sequence information

Length: 602 AA [This is the length of the unprocessed precursor]

Molecular weight: 66784 Da [This is the MW of the unprocessed precursor]

CRC64: B7D9BBB11AB53F6C [This is a checksum on the sequence]

        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

P22317 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