Hydrogenase-1 small chain precursor - Escherichia coli (strain K12)

Contribute

Send feedback

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P69739 (MBHS_ECOLI)

Last modified November 3, 2009. Version 43. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

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

Hide | Top

Names and origin

Protein names

Recommended name:
    Hydrogenase-1 small chain
      Short name=HYD1
    EC=1.12.99.6
Alternative name(s):
    Membrane-bound hydrogenase 1 small subunit
    NiFe hydrogenase

Gene names

Name:	hyaA
Ordered Locus Names:	b0972, JW0954

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Hide | Top

Protein attributes

Sequence length	372 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

Hide | Top

General annotation (Comments)

Function	This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD1 is believed to have a role in hydrogen cycling during fermentative growth.
Catalytic activity	H₂ + A = AH₂.
Cofactor	Binds 1 3Fe-4S cluster By similarity. Binds 2 4Fe-4S clusters By similarity.
Subunit structure	Heterodimer of a large and a small subunit.
Subcellular location	Cell inner membrane; Single-pass type I membrane protein; Periplasmic side.
Post-translational modification	Exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.
Sequence similarities	Belongs to the [NiFe]/[NiFeSe] hydrogenase small subunit family.

Hide | Top

Ontologies

Keywords
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Signal Transmembrane
Ligand	3Fe-4S 4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	ferredoxin hydrogenase complex Inferred from electronic annotation. Source: InterPro integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	3 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW NADH dehydrogenase (ubiquinone) activity Inferred from electronic annotation. Source: InterPro ferredoxin hydrogenase activity Inferred from electronic annotation. Source: InterPro hydrogenase (acceptor) activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW quinone binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 45

Tat-type signal Ref.1

Chain

46 – 372

327

Hydrogenase-1 small chain

PRO_0000013427

Regions

Topological domain

46 – 325

280

Periplasmic Potential

Transmembrane

326 – 348

Potential

Topological domain

349 – 372

Cytoplasmic Potential

Sites

Metal binding

Iron-sulfur 1 (4Fe-4S) By similarity

Metal binding

Iron-sulfur 1 (4Fe-4S) By similarity

Metal binding

160

Iron-sulfur 1 (4Fe-4S) By similarity

Metal binding

194

Iron-sulfur 1 (4Fe-4S) By similarity

Metal binding

232

Iron-sulfur 2 (4Fe-4S); via pros nitrogen By similarity

Metal binding

235

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

260

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

266

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

275

Iron-sulfur 3 (3Fe-4S) By similarity

Metal binding

294

Iron-sulfur 3 (3Fe-4S) By similarity

Metal binding

297

Iron-sulfur 3 (3Fe-4S) By similarity

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

P69739-1 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: 4AD3ECB4220D2826
Show »

FASTA

372

40,681

        10         20         30         40         50         60 
MNNEETFYQA MRRQGVTRRS FLKYCSLAAT SLGLGAGMAP KIAWALENKP RIPVVWIHGL 

        70         80         90        100        110        120 
ECTCCTESFI RSAHPLAKDV ILSLISLDYD DTLMAAAGTQ AEEVFEDIIT QYNGKYILAV 

       130        140        150        160        170        180 
EGNPPLGEQG MFCISSGRPF IEKLKRAAAG ASAIIAWGTC ASWGCVQAAR PNPTQATPID 

       190        200        210        220        230        240 
KVITDKPIIK VPGCPPIPDV MSAIITYMVT FDRLPDVDRM GRPLMFYGQR IHDKCYRRAH 

       250        260        270        280        290        300 
FDAGEFVQSW DDDAARKGYC LYKMGCKGPT TYNACSSTRW NDGVSFPIQS GHGCLGCAEN 

       310        320        330        340        350        360 
GFWDRGSFYS RVVDIPQMGT HSTADTVGLT ALGVVAAAVG VHAVASAVDQ RRRHNQQPTE 

       370 
TEHQPGNEDK QA

« Hide

Hide | Top

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequencing of a putative Escherichia coli [NiFe] hydrogenase-1 operon containing six open reading frames." Menon N.K., Robbins J., Peck H.D. Jr., Chatelus C.Y., Choi E.-S., Przybyla A.E. J. Bacteriol. 172:1969-1977(1990) [PubMed: 2180913] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 46-50.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. Horiuchi T. DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-57. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Global topology analysis of the Escherichia coli inner membrane proteome." Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G. Science 308:1321-1323(2005) [PubMed: 15919996] [Abstract] Cited for: TOPOLOGY [LARGE SCALE ANALYSIS]. Strain: K12 / MG1655 / ATCC 47076.
[6]	"Export pathway selectivity of Escherichia coli twin arginine translocation signal peptides." Tullman-Ercek D., DeLisa M.P., Kawarasaki Y., Iranpour P., Ribnicky B., Palmer T., Georgiou G. J. Biol. Chem. 282:8309-8316(2007) [PubMed: 17218314] [Abstract] Cited for: EXPORT VIA THE TAT-SYSTEM.

Hide | Top

Cross-references

Sequence databases
	M34825 Genomic DNA. Translation: AAA23997.1. U00096 Genomic DNA. Translation: AAC74057.1. AP009048 Genomic DNA. Translation: BAA35737.2.
PIR	HQECSN. JV0072.
RefSeq	AP_001601.1. NP_415491.1.
3D structure databases
HSSP	HSSP built from PDB template 1FRF based on UniProtKB P18187.
ModBase	Search...
Protein-protein interaction databases
STRING	P69739.
Genome annotation databases
GeneID	945579.
GenomeReviews	Gene locus JW0954 in contig AP009048_GR. Gene locus b0972 in contig U00096_GR.
KEGG	ecj:JW0954. eco:b0972.
Organism-specific databases
EchoBASE	EB0463.
EcoGene	EG10468. hyaA.
CMR	Search...
Phylogenomic databases
HOGENOM	P69739.
OMA	LEYHETV.
Enzyme and pathway databases
BioCyc	EcoCyc:HYAA-MON. MetaCyc:HYAA-MON.
Gene expression databases
Genevestigator	P69739.
Family and domain databases
InterPro	IPR006137. NADH_UbQ_OxRdtase-like_20kDa. IPR001821. NiFe_hydrogenase_ssu. IPR006311. TAT_signal. IPR017909. Twin_arg_translocation_Tat. [Graphical view]
Pfam	PF01058. Oxidored_q6. 1 hit. [Graphical view]
PIRSF	PIRSF000310. NiFe_hyd_ssu. 1 hit.
PRINTS	PR00614. NIHGNASESMLL.
TIGRFAMs	TIGR00391. hydA. 1 hit. TIGR01409. TAT_signal_seq. 1 hit.
PROSITE	PS51318. TAT. 1 hit. [Graphical view]
ProtoNet	Search...

Hide | Top

Entry information

Entry name

MBHS_ECOLI

Accession

Primary (citable) accession number: P69739
Secondary accession number(s): P19928

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2005
Last sequence update:	April 26, 2005
Last modified:	November 3, 2009
This is version 43 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)

Hide | Top

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents