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Protein

Hydrogenase-1 large chain

Gene

hyaB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

H2 + A = AH2.

Cofactori

Ni2+By similarityNote: Binds 1 nickel ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi76 – 761NickelSequence Analysis
Metal bindingi79 – 791NickelSequence Analysis
Metal bindingi576 – 5761NickelSequence Analysis
Metal bindingi579 – 5791NickelSequence Analysis

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, Nickel

Enzyme and pathway databases

BioCyciEcoCyc:HYAB-MONOMER.
ECOL316407:JW0955-MONOMER.
MetaCyc:HYAB-MONOMER.
BRENDAi1.12.99.6. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
Hydrogenase-1 large chain (EC:1.12.99.6)
Short name:
HYD1
Alternative name(s):
Membrane-bound hydrogenase 1 large subunit
NiFe hydrogenase
Gene namesi
Name:hyaB
Ordered Locus Names:b0973, JW0955
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10469. hyaB.

Subcellular locationi

GO - Cellular componenti

  • membrane Source: UniProtKB
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 597597Hydrogenase-1 large chainPRO_0000199712Add
BLAST

Expressioni

Gene expression databases

GenevestigatoriP0ACD8.

Interactioni

Subunit structurei

Heterodimer of a large and a small subunit.

Binary interactionsi

WithEntry#Exp.IntActNotes
hyaDP199303EBI-851493,EBI-552940

Protein-protein interaction databases

DIPiDIP-36180N.
IntActiP0ACD8. 8 interactions.
STRINGi511145.b0973.

Structurei

Secondary structure

1
597
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 74Combined sources
Beta strandi10 – 134Combined sources
Beta strandi16 – 216Combined sources
Beta strandi26 – 294Combined sources
Beta strandi31 – 377Combined sources
Beta strandi41 – 5010Combined sources
Helixi56 – 594Combined sources
Turni60 – 623Combined sources
Helixi65 – 673Combined sources
Helixi68 – 736Combined sources
Beta strandi77 – 793Combined sources
Helixi82 – 9514Combined sources
Helixi101 – 12525Combined sources
Helixi128 – 1303Combined sources
Helixi135 – 1395Combined sources
Helixi142 – 15211Combined sources
Helixi160 – 17516Combined sources
Helixi180 – 1823Combined sources
Helixi196 – 21621Combined sources
Helixi218 – 2247Combined sources
Beta strandi227 – 2293Combined sources
Beta strandi243 – 2453Combined sources
Helixi248 – 2503Combined sources
Helixi254 – 27320Combined sources
Helixi275 – 28511Combined sources
Helixi287 – 2915Combined sources
Helixi295 – 2984Combined sources
Beta strandi301 – 3033Combined sources
Beta strandi306 – 3105Combined sources
Turni316 – 3183Combined sources
Beta strandi319 – 3213Combined sources
Beta strandi324 – 3263Combined sources
Beta strandi344 – 3485Combined sources
Beta strandi352 – 3543Combined sources
Helixi365 – 3673Combined sources
Beta strandi380 – 3823Combined sources
Beta strandi385 – 3884Combined sources
Beta strandi400 – 4034Combined sources
Helixi412 – 42211Combined sources
Helixi425 – 43713Combined sources
Helixi442 – 4454Combined sources
Helixi448 – 47831Combined sources
Helixi492 – 4943Combined sources
Beta strandi497 – 50711Combined sources
Beta strandi510 – 51910Combined sources
Beta strandi522 – 5298Combined sources
Helixi531 – 5355Combined sources
Helixi547 – 5526Combined sources
Beta strandi560 – 5623Combined sources
Helixi564 – 5729Combined sources
Helixi577 – 5815Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UQYX-ray1.47L/M1-582[»]
3USCX-ray2.00L/M1-582[»]
3USEX-ray1.67L/M1-582[»]
4GD3X-ray3.30J/K/L/M1-582[»]
4UE3X-ray1.40L/M1-582[»]
ProteinModelPortaliP0ACD8.
SMRiP0ACD8. Positions 2-582.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0374.
HOGENOMiHOG000278799.
InParanoidiP0ACD8.
KOiK06281.
OMAiEEVSHSW.
OrthoDBiEOG6M9DSB.
PhylomeDBiP0ACD8.

Family and domain databases

Gene3Di1.10.645.10. 1 hit.
InterProiIPR001501. Ni-dep_hyd_lsu.
IPR018194. Ni-dep_hyd_lsu_Ni_BS.
IPR029014. NiFe_Hase-like.
[Graphical view]
PfamiPF00374. NiFeSe_Hases. 1 hit.
[Graphical view]
SUPFAMiSSF56762. SSF56762. 1 hit.
PROSITEiPS00507. NI_HGENASE_L_1. 1 hit.
PS00508. NI_HGENASE_L_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0ACD8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTQYETQGY TINNAGRRLV VDPITRIEGH MRCEVNINDQ NVITNAVSCG
60 70 80 90 100
TMFRGLEIIL QGRDPRDAWA FVERICGVCT GVHALASVYA IEDAIGIKVP
110 120 130 140 150
DNANIIRNIM LATLWCHDHL VHFYQLAGMD WIDVLDALKA DPRKTSELAQ
160 170 180 190 200
SLSSWPKSSP GYFFDVQNRL KKFVEGGQLG IFRNGYWGHP QYKLPPEANL
210 220 230 240 250
MGFAHYLEAL DFQREIVKIH AVFGGKNPHP NWIVGGMPCA INIDESGAVG
260 270 280 290 300
AVNMERLNLV QSIITRTADF INNVMIPDAL AIGQFNKPWS EIGTGLSDKC
310 320 330 340 350
VLSYGAFPDI ANDFGEKSLL MPGGAVINGD FNNVLPVDLV DPQQVQEFVD
360 370 380 390 400
HAWYRYPNDQ VGRHPFDGIT DPWYNPGDVK GSDTNIQQLN EQERYSWIKA
410 420 430 440 450
PRWRGNAMEV GPLARTLIAY HKGDAATVES VDRMMSALNL PLSGIQSTLG
460 470 480 490 500
RILCRAHEAQ WAAGKLQYFF DKLMTNLKNG NLATASTEKW EPATWPTECR
510 520 530 540 550
GVGFTEAPRG ALGHWAAIRD GKIDLYQCVV PTTWNASPRD PKGQIGAYEA
560 570 580 590
ALMNTKMAIP EQPLEILRTL HSFDPCLACS THVLGDDGSE LISVQVR
Length:597
Mass (Da):66,253
Last modified:November 22, 2005 - v1
Checksum:i659DD7EDE16D6342
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti52 – 521M → I in AAA23998 (PubMed:2180913).Curated
Sequence conflicti69 – 691W → R in AAA23998 (PubMed:2180913).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34825 Genomic DNA. Translation: AAA23998.1.
U00096 Genomic DNA. Translation: AAC74058.1.
AP009048 Genomic DNA. Translation: BAA35738.2.
PIRiC64838. HQECL.
RefSeqiNP_415492.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC74058; AAC74058; b0973.
BAA35738; BAA35738; BAA35738.
GeneIDi945580.
KEGGiecj:Y75_p0944.
eco:b0973.
PATRICi32117167. VBIEscCol129921_1007.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34825 Genomic DNA. Translation: AAA23998.1.
U00096 Genomic DNA. Translation: AAC74058.1.
AP009048 Genomic DNA. Translation: BAA35738.2.
PIRiC64838. HQECL.
RefSeqiNP_415492.1. NC_000913.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UQYX-ray1.47L/M1-582[»]
3USCX-ray2.00L/M1-582[»]
3USEX-ray1.67L/M1-582[»]
4GD3X-ray3.30J/K/L/M1-582[»]
4UE3X-ray1.40L/M1-582[»]
ProteinModelPortaliP0ACD8.
SMRiP0ACD8. Positions 2-582.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-36180N.
IntActiP0ACD8. 8 interactions.
STRINGi511145.b0973.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74058; AAC74058; b0973.
BAA35738; BAA35738; BAA35738.
GeneIDi945580.
KEGGiecj:Y75_p0944.
eco:b0973.
PATRICi32117167. VBIEscCol129921_1007.

Organism-specific databases

EchoBASEiEB0464.
EcoGeneiEG10469. hyaB.

Phylogenomic databases

eggNOGiCOG0374.
HOGENOMiHOG000278799.
InParanoidiP0ACD8.
KOiK06281.
OMAiEEVSHSW.
OrthoDBiEOG6M9DSB.
PhylomeDBiP0ACD8.

Enzyme and pathway databases

BioCyciEcoCyc:HYAB-MONOMER.
ECOL316407:JW0955-MONOMER.
MetaCyc:HYAB-MONOMER.
BRENDAi1.12.99.6. 2026.

Miscellaneous databases

PROiP0ACD8.

Gene expression databases

GenevestigatoriP0ACD8.

Family and domain databases

Gene3Di1.10.645.10. 1 hit.
InterProiIPR001501. Ni-dep_hyd_lsu.
IPR018194. Ni-dep_hyd_lsu_Ni_BS.
IPR029014. NiFe_Hase-like.
[Graphical view]
PfamiPF00374. NiFeSe_Hases. 1 hit.
[Graphical view]
SUPFAMiSSF56762. SSF56762. 1 hit.
PROSITEiPS00507. NI_HGENASE_L_1. 1 hit.
PS00508. NI_HGENASE_L_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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 1-10.
  2. 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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 276-597.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

Entry informationi

Entry nameiMBHL_ECOLI
AccessioniPrimary (citable) accession number: P0ACD8
Secondary accession number(s): P19927, P78056
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 22, 2005
Last modified: May 27, 2015
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.