P22320 (HOXH_CUPNH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	hoxH
Ordered Locus Names:	PHG091

Encoded on

Plasmid megaplasmid pHG1

Organism

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

Taxonomic identifier

381666 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus

Protein attributes

Sequence length	488 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	H2 + NAD+ = H+ + NADH.
Cofactor	FMN. Nickel.
Subunit structure	Tetramer of an alpha and a gamma subunits (flavin-containing dimer), and a delta and a nickel-containing beta subunits (hydrogenase dimer).
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Metal-binding NAD Nickel
Molecular function	Oxidoreductase
Technical term	Complete proteome Direct protein sequencing Plasmid
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ferredoxin hydrogenase activity Inferred from electronic annotation. Source: InterPro hydrogen dehydrogenase activity Inferred from electronic annotation. Source: EC nickel cation binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.3
	Chain	2 – 488	487	NAD-reducing hydrogenase hoxS subunit beta		PRO_0000199719
Sites
	Metal binding	62	1	Nickel Potential
	Metal binding	65	1	Nickel Potential
	Metal binding	458	1	Nickel Potential
	Metal binding	461	1	Nickel Potential
Experimental info
	Sequence conflict	30	1	V → R AA sequence Ref.3
	Sequence conflict	32	1	A → T AA sequence Ref.3
	Sequence conflict	37	1	V → R AA sequence Ref.3
	Sequence conflict	419	1	N → H in AAC06143. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P22320 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 751C509483818E6A	FASTA	488	54,863
	10 20 30 40 50 60 MSRKLVIDPV TRIEGHGKVV VHLDDDNKVV DAKLHVVEFR GFEKFVQGHP FWEAPMFLQR 70 80 90 100 110 120 ICGICFVSHH LCGAKALDDM VGVGLKSGIH VTPTAEKMRR LGHYAQMLQS HTTAYFYLIV 130 140 150 160 170 180 PEMLFGMDAP PAQRNVLGLI EANPDLVKRV VMLRKWGQEV IKAVFGKKMH GINSVPGGVN 190 200 210 220 230 240 NNLSIAERDR FLNGEEGLLS VDQVIDYAQD GLRLFYDFHQ KHRAQVDSFA DVPALSMCLV 250 260 270 280 290 300 GDDDNVDYYH GRLRIIDDDK HIVREFDYHD YLDHFSEAVE EWSYMKFPYL KELGREQGSV 310 320 330 340 350 360 RVGPLGRMNV TKSLPTPLAQ EALERFHAYT KGRTNNMTLH TNWARAIEIL HAAEVVKELL 370 380 390 400 410 420 HDPDLQKDQL VLTPPPNAWT GEGVGVVEAP RGTLLHHYRA DERGNITFAN LVVATTQNNQ 430 440 450 460 470 480 VMNRTVRSVA EDYLGGHGEI TEGMMNAIEV GIRAYDPCLS CATHALGQMP LVVSVFDAAG RLIDERAR

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]. Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.
[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 2-39.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M55230 Genomic DNA. Translation: AAC06143.1. AY305378 Genomic DNA. Translation: AAP85844.1.
PIR	D35385.
RefSeq	NP_942730.1. NC_005241.1.
3D structure databases
ProteinModelPortal	P22320.
ModBase	Search...
Protein-protein interaction databases
IntAct	P22320. 1 interaction.
STRING	P22320.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2656817.
GenomeReviews	Gene locus PHG091 in contig AY305378_GR.
KEGG	reh:PHG091.
PATRIC	35228792. VBIRalEut6770_0068.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG287963.
OMA	FFHLSSP.
PhylomeDB	P22320.
ProtClustDB	CLSK2761122.
Enzyme and pathway databases
BioCyc	MetaCyc:HOXHALCA-MONOMER. REUT381666:PHG091-MONOMER.
BRENDA	1.12.1.2. 7290.
Family and domain databases
InterPro	IPR001501. Ni-dep_hyd_lsu. IPR018194. Ni-dep_hyd_lsu_Ni_BS. [Graphical view]
KO	K00436.
Pfam	PF00374. NiFeSe_Hases. 2 hits. [Graphical view]
PROSITE	PS00507. NI_HGENASE_L_1. 1 hit. PS00508. NI_HGENASE_L_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HOXH_CUPNH

Accession

Primary (citable) accession number: P22320
Secondary accession number(s): Q7WXN0

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 81 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program