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Protein

Hydrogenase-1 large chain

Gene

hyaB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 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)DescriptionActionsGraphical viewLength
Metal bindingi76NickelSequence analysis1
Metal bindingi79NickelSequence analysis1
Metal bindingi576NickelSequence analysis1
Metal bindingi579NickelSequence analysis1

GO - Molecular functioni

  • electron carrier activity Source: EcoCyc
  • ferredoxin hydrogenase activity Source: InterPro
  • hydrogenase (acceptor) activity Source: UniProtKB-EC
  • nickel cation binding Source: EcoCyc

GO - Biological processi

  • anaerobic respiration Source: EcoCyc
  • fermentation Source: EcoCyc
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10469. hyaB.

Subcellular locationi

GO - Cellular componenti

  • [Ni-Fe] hydrogenase complex Source: EcoCyc
  • membrane Source: UniProtKB
  • outer membrane-bounded periplasmic space Source: EcoCyc
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001997121 – 597Hydrogenase-1 large chainAdd BLAST597

Proteomic databases

PaxDbiP0ACD8.
PRIDEiP0ACD8.

Interactioni

Subunit structurei

Heterodimer of a large and a small subunit.

Binary interactionsi

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

Protein-protein interaction databases

BioGridi4260043. 8 interactors.
DIPiDIP-36180N.
IntActiP0ACD8. 8 interactors.
STRINGi511145.b0973.

Structurei

Secondary structure

1597
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 7Combined sources4
Beta strandi10 – 13Combined sources4
Beta strandi16 – 21Combined sources6
Beta strandi26 – 29Combined sources4
Beta strandi31 – 37Combined sources7
Beta strandi41 – 50Combined sources10
Helixi56 – 59Combined sources4
Turni60 – 62Combined sources3
Helixi65 – 67Combined sources3
Helixi68 – 73Combined sources6
Beta strandi77 – 79Combined sources3
Helixi82 – 95Combined sources14
Helixi101 – 125Combined sources25
Helixi128 – 130Combined sources3
Helixi135 – 139Combined sources5
Helixi142 – 152Combined sources11
Helixi160 – 175Combined sources16
Helixi180 – 182Combined sources3
Helixi196 – 216Combined sources21
Helixi218 – 224Combined sources7
Beta strandi227 – 229Combined sources3
Beta strandi243 – 245Combined sources3
Helixi248 – 250Combined sources3
Helixi254 – 273Combined sources20
Helixi275 – 285Combined sources11
Helixi287 – 291Combined sources5
Helixi295 – 298Combined sources4
Beta strandi301 – 303Combined sources3
Beta strandi306 – 310Combined sources5
Turni316 – 318Combined sources3
Beta strandi319 – 321Combined sources3
Beta strandi324 – 326Combined sources3
Beta strandi344 – 348Combined sources5
Beta strandi352 – 354Combined sources3
Helixi365 – 367Combined sources3
Beta strandi380 – 382Combined sources3
Beta strandi385 – 388Combined sources4
Beta strandi400 – 403Combined sources4
Helixi412 – 421Combined sources10
Helixi425 – 437Combined sources13
Helixi442 – 445Combined sources4
Helixi448 – 478Combined sources31
Helixi492 – 494Combined sources3
Beta strandi497 – 507Combined sources11
Beta strandi510 – 519Combined sources10
Beta strandi522 – 529Combined sources8
Helixi531 – 535Combined sources5
Helixi547 – 552Combined sources6
Beta strandi560 – 562Combined sources3
Helixi564 – 571Combined sources8
Helixi577 – 581Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5A4FX-ray1.25L/M1-582[»]
5A4IX-ray1.23L/M1-582[»]
5A4MX-ray1.70L/M1-582[»]
5ADUX-ray1.10L/M1-582[»]
ProteinModelPortaliP0ACD8.
SMRiP0ACD8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105DPX. Bacteria.
COG0374. LUCA.
HOGENOMiHOG000278799.
InParanoidiP0ACD8.
KOiK06281.
OMAiEEVSHSW.
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)DescriptionActionsGraphical viewLength
Sequence conflicti52M → I in AAA23998 (PubMed:2180913).Curated1
Sequence conflicti69W → R in AAA23998 (PubMed:2180913).Curated1

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.
WP_000107384.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74058; AAC74058; b0973.
BAA35738; BAA35738; BAA35738.
GeneIDi945580.
KEGGiecj:JW0955.
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.
WP_000107384.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5A4FX-ray1.25L/M1-582[»]
5A4IX-ray1.23L/M1-582[»]
5A4MX-ray1.70L/M1-582[»]
5ADUX-ray1.10L/M1-582[»]
ProteinModelPortaliP0ACD8.
SMRiP0ACD8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260043. 8 interactors.
DIPiDIP-36180N.
IntActiP0ACD8. 8 interactors.
STRINGi511145.b0973.

Proteomic databases

PaxDbiP0ACD8.
PRIDEiP0ACD8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74058; AAC74058; b0973.
BAA35738; BAA35738; BAA35738.
GeneIDi945580.
KEGGiecj:JW0955.
eco:b0973.
PATRICi32117167. VBIEscCol129921_1007.

Organism-specific databases

EchoBASEiEB0464.
EcoGeneiEG10469. hyaB.

Phylogenomic databases

eggNOGiENOG4105DPX. Bacteria.
COG0374. LUCA.
HOGENOMiHOG000278799.
InParanoidiP0ACD8.
KOiK06281.
OMAiEEVSHSW.
PhylomeDBiP0ACD8.

Enzyme and pathway databases

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

Miscellaneous databases

PROiP0ACD8.

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...

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: November 2, 2016
This is version 87 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

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 one 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.