NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=301 / Serotype 2a;
DOI=10.1093/nar/gkf566; PubMed=12384590 [NCBI, ExPASy, EBI, Israel, Japan]
Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
"Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157.";
Nucleic Acids Res. 30:4432-4441(2002).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700930 / 2457T / Serotype 2a;
DOI=10.1128/IAI.71.5.2775-2786.2003; PubMed=12704152 [NCBI, ExPASy, EBI, Israel, Japan]
Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
"Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T.";
Infect. Immun. 71:2775-2786(2003).

Comments

FUNCTION: This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD2 is involved in hydrogen uptake (By similarity).
CATALYTIC ACTIVITY: H₂ + A = AH₂.
COFACTOR: Binds 1 nickel ion per subunit (By similarity).
SUBUNIT: Heterodimer of a large and a small subunit (By similarity).
SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein (By similarity).
SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large 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

AE005674; AAN44519.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014073; AAP18330.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_708812.1; -.
NP_838520.1; -.

3D structure databases

HSSP

P21852; 1UBL. [HSSP ENTRY / PDB]

ModBase

P0ACE2.

Enzyme and pathway databases

BioCyc

SFLE198214:AAN44519.1-MON; -.

Ontologies

GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0008901;	Molecular function: ferredoxin hydrogenase activity (inferred from electronic annotation from InterPro).
GO:0033748;	Molecular function: hydrogenase (acceptor) activity (inferred from electronic annotation from EC).
GO:0016151;	Molecular function: nickel ion binding (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001501; Ni-dep_hyd_lsu.
Graphical view of domain structure.

Pfam

PF00374; NiFeSe_Hases; 1.
Pfam graphical view of domain structure.

PROSITE

PS00507; NI_HGENASE_L_1; 1.
PS00508; NI_HGENASE_L_2; 1.

Genome annotation databases

GeneID

1026601; -.
1079496; -.

GenomeReviews

AE005674_GR; SF3041.
AE014073_GR; S3242.

KEGG

sfl:SF3041; -.
sfx:S3242; -.

Phylogenomic databases

HOGENOM

P0ACE2; -.

Genome annotation databases

CMR

P0ACE2; SF3041.

Other

ProtoNet

P0ACE2.

UniRef

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

Keywords

Cell membrane; Complete proteome; Membrane; Metal-binding; Nickel; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 552`	`551`	`Hydrogenase-2 large chain.`	`PRO_0000042992`
`PROPEP`	`553 567`	`15`		`PRO_0000042993`
`METAL`	`61 61`		`Nickel (Potential).`
`METAL`	`64 64`		`Nickel (Potential).`
`METAL`	`546 546`		`Nickel (Potential).`
`METAL`	`549 549`		`Nickel (Potential).`
`SITE`	`552 553`	`2`	`Cleavage; by hybD (By similarity).`

Sequence information

Length: 567 AA [This is the length of the unprocessed precursor]

Molecular weight: 62491 Da [This is the MW of the unprocessed precursor]

CRC64: A19E6F513390F29E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSQRITIDPV TRIEGHLRID CEIENGVVSK AWASGTMWRG MEEIVKNRDP RDAWMIVQRI 

        70         80         90        100        110        120 
CGVCTTTHAL SSVRAAESAL NIDVPVNAQY IRNIILAAHT THDHIVHFYQ LSALDWVDIT 

       130        140        150        160        170        180 
SALQADPTKA SEMLKGVSTW HLNSPEEFTK VQNKIKDLVA SGQLGIFANG YWGHPAMKLP 

       190        200        210        220        230        240 
PEVNLIAVAH YLQALECQRD ANRVVALLGG KTPHIQNLAV GGVANPINLD GLGVLNLERL 

       250        260        270        280        290        300 
MYIKSFIDKL SDFVEQVYKV DTAVIAAFYP EWLTRGKGAV NYLSVPEFPT DSKNGSFLFP 

       310        320        330        340        350        360 
GGYIENADLS SYRPITSHSD EYLIKGIQES AKHSWYKDEA PQAPWEGTTI PAYDGWSDDG 

       370        380        390        400        410        420 
KYSWVKSPTF YGKTVEVGPL ANMLVKLAAG RESTQNKLNE IVAIYQKLTG NTLEVAQLHS 

       430        440        450        460        470        480 
TLGRIIGRTV HCCELQDILQ NQYSALITNI GKGDHTTFVK PNIPATGEFK GVGFLEAPRG 

       490        500        510        520        530        540 
MLSHWMVIKD GIISNYQAVV PSTWNSGPRN FNDDVGPYEQ SLVGTPVADP NKPLEVVRTI 

       550        560 
HSFDPCMACA VHVVDADGNE VVSVKVL

P0ACE2 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