P69739 (MBHS_ECOLI) Reviewed, UniProtKB/Swiss-Prot

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) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

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

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.

Ontologies

Keywords
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Signal Transmembrane Transmembrane helix
Ligand	3Fe-4S 4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
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-SubCell
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 metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW quinone 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

Signal peptide

1 – 45

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

23

Helical; Potential

Topological domain

349 – 372

24

Cytoplasmic Potential

Sites

Metal binding

62

1

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

Metal binding

65

1

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

Metal binding

160

1

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

Metal binding

194

1

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

Metal binding

232

1

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

Metal binding

235

1

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

Metal binding

260

1

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

Metal binding

266

1

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

Metal binding

275

1

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

Metal binding

294

1

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

Metal binding

297

1

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

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

372

Helix Strand Turn

Details...

Beta strand

52 – 58

7

Helix

64 – 70

7

Turn

73 – 76

4

Helix

77 – 83

7

Beta strand

85 – 90

6

Turn

91 – 93

3

Helix

98 – 111

14

Turn

112 – 115

4

Beta strand

116 – 123

8

Helix

127 – 130

4

Beta strand

133 – 135

3

Helix

140 – 150

11

Beta strand

151 – 157

7

Helix

158 – 162

5

Helix

165 – 168

4

Helix

179 – 181

3

Beta strand

188 – 191

4

Beta strand

193 – 195

3

Helix

198 – 211

14

Helix

224 – 227

4

Beta strand

228 – 230

3

Helix

231 – 233

3

Helix

238 – 243

6

Helix

255 – 257

3

Helix

262 – 264

3

Helix

268 – 270

3

Beta strand

272 – 274

3

Turn

275 – 277

3

Turn

281 – 284

4

Turn

287 – 291

5

Helix

302 – 304

3

Helix

320 – 338

19

Beta strand

346 – 349

4

Sequences

	Sequence		Length	Mass (Da)
	P69739 [UniParc]. Last modified April 26, 2005. Version 1. Checksum: 4AD3ECB4220D2826	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

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. , 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. DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: EXPORT VIA THE TAT-SYSTEM.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M34825 Genomic DNA. Translation: AAA23997.1.
U00096 Genomic DNA. Translation: AAC74057.1.
AP009048 Genomic DNA. Translation: BAA35737.2.

PIR

HQECSN. JV0072.

RefSeq

NP_415491.1. NC_000913.2.
YP_489243.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3UQY	X-ray	1.47	S/T	46-372	[»]
3USC	X-ray	2.00	S/T	46-372	[»]
3USE	X-ray	1.67	S/T	46-372	[»]
4GD3	X-ray	3.30	Q/R/S/T	46-372	[»]

ProteinModelPortal

P69739.

SMR

P69739. Positions 49-352.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-47848N.

STRING

511145.b0972.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC74057; AAC74057; b0972.
BAA35737; BAA35737; BAA35737.

GeneID

12932807.
945579.

KEGG

ecj:Y75_p0943.
eco:b0972.

PATRIC

32117165. VBIEscCol129921_1006.

Organism-specific databases

EchoBASE

EB0463.

EcoGene

EG10468. hyaA.

Phylogenomic databases

eggNOG

COG1740.

HOGENOM

HOG000278822.

KO

K06282.

OMA

QGRPAMF.

ProtClustDB

CLSK879888.

Enzyme and pathway databases

BioCyc

EcoCyc:HYAA-MONOMER.
ECOL316407:JW0954-MONOMER.
MetaCyc:HYAA-MONOMER.

Gene expression databases

Genevestigator

P69739.

Family and domain databases

Gene3D

3.40.50.700. 1 hit.

InterPro

IPR006137. NADH_UbQ_OxRdtase-like_20kDa.
IPR001821. NiFe_hydrogenase_ssu.
IPR006311. TAT_signal.
IPR019546. TAT_signal_bac_arc.
[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...

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:	May 1, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program