[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 46-50. PubMed=2180913 [NCBI, ExPASy, EBI, Israel, Japan] Menon N.K., Robbins J., Peck H.D. Jr., Chatelus C.Y., Choi E.-S., Przybyla A.E.; "Cloning and sequencing of a putative Escherichia coli [NiFe] hydrogenase-1 operon containing six open reading frames."; J. Bacteriol. 172:1969-1977(1990).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-57. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1093/dnares/3.3.137; PubMed=8905232 [NCBI, ExPASy, EBI, Israel, Japan] 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., Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.; "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."; DNA Res. 3:137-155(1996).
[5]	TOPOLOGY [LARGE SCALE ANALYSIS]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.1109730; PubMed=15919996 [NCBI, ExPASy, EBI, Israel, Japan] Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.; "Global topology analysis of the Escherichia coli inner membrane proteome."; Science 308:1321-1323(2005).

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).
COFACTOR: Binds 2 4Fe-4S clusters (By similarity).
SUBUNIT: Heterodimer of a large and a small subunit.
SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type I membrane protein.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.
SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase small 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

M34825; AAA23997.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC74057.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA35737.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JV0072; HQECSN.

RefSeq

AP_001601.1; -.
NP_415491.1; -.

3D structure databases

HSSP

P18187; 1FRF. [HSSP ENTRY / PDB]

ModBase

P69739.

Enzyme and pathway databases

BioCyc

EcoCyc:HYAA-MON; -.
MetaCyc:HYAA-MON; -.

Organism-specific databases

EchoBASE

EB0463; -.

EcoGene

EG10468; hyaA.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0042597;	Cellular component: periplasmic space (inferred from electronic annotation from UniProtKB-KW).
GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0051538;	Molecular function: 3 iron, 4 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0051539;	Molecular function: 4 iron, 4 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0033748;	Molecular function: hydrogenase (acceptor) activity (inferred from electronic annotation from EC).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001821; NiFe_hyd_ssu.
IPR013634; NiFe_hyd_ssu_N.
IPR006137; OxRdtase_q6.
IPR006311; Tat.
Graphical view of domain structure.

Pfam

PF08425; NiFe_dehyd_N; 1.
PF01058; Oxidored_q6; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000310; NiFe_hyd_ssu; 1.

PRINTS

PR00614; NIHGNASESMLL.

TIGRFAMs

TIGR00391; hydA; 1.
TIGR01409; TAT_signal_seq; 1.

PROSITE

PS51318; TAT; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

GeneID

945579; -.

GenomeReviews

U00096_GR; b0972.
AP009048_GR; JW0954.

KEGG

ecj:JW0954; -.
eco:b0972; -.

Phylogenomic databases

HOGENOM

P69739; -.

Genome annotation databases

CMR

P69739; b0972.

Other

UniRef

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

Keywords

3Fe-4S; 4Fe-4S; Cell inner membrane; Cell membrane; Complete proteome; Direct protein sequencing; Iron; Iron-sulfur; Membrane; Metal-binding; Oxidoreductase; Periplasm; Signal; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 45`	`45`	`Tat-type signal.`
`CHAIN`	`46 372`	`327`	`Hydrogenase-1 small chain.`	`PRO_0000013427`
`TOPO_DOM`	`46 325`	`280`	`Periplasmic (Potential).`
`TRANSMEM`	`326 348`	`23`	`Potential.`
`TOPO_DOM`	`349 372`	`24`	`Cytoplasmic (Potential).`
`METAL`	`62 62`		`Iron-sulfur 1 (4Fe-4S) (By similarity).`
`METAL`	`65 65`		`Iron-sulfur 1 (4Fe-4S) (By similarity).`
`METAL`	`160 160`		`Iron-sulfur 1 (4Fe-4S) (By similarity).`
`METAL`	`194 194`		`Iron-sulfur 1 (4Fe-4S) (By similarity).`
`METAL`	`232 232`		`Iron-sulfur 2 (4Fe-4S); via pros nitrogen (By similarity).`
`METAL`	`235 235`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`260 260`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`266 266`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`275 275`		`Iron-sulfur 3 (3Fe-4S) (By similarity).`
`METAL`	`294 294`		`Iron-sulfur 3 (3Fe-4S) (By similarity).`
`METAL`	`297 297`		`Iron-sulfur 3 (3Fe-4S) (By similarity).`

Sequence information

Length: 372 AA [This is the length of the unprocessed precursor]

Molecular weight: 40681 Da [This is the MW of the unprocessed precursor]

CRC64: 4AD3ECB4220D2826 [This is a checksum on the sequence]

        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

P69739 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