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

CATALYTIC ACTIVITY: (S)-malate + NAD⁺ = pyruvate + CO₂ + NADH.
COFACTOR: Divalent metal cations. Prefers magnesium or manganese (By similarity).
SUBUNIT: Homotetramer (By similarity).
SIMILARITY: Belongs to the malic enzymes 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; AAN43318.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014073; AAP17204.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_707611.2; -.
NP_837395.1; -.

3D structure databases

HSSP

P23368; 1GZ3. [HSSP ENTRY / PDB]

ModBase

Q83ML6.

Enzyme and pathway databases

BioCyc

SFLE198214:AAN43318.1-MON; -.

Ontologies

GO:0016619;	Molecular function: malate dehydrogenase (oxaloacetate-decarboxylating) activity (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01619; -; 1.
PBIL [Tree]

InterPro

IPR015884; Malic_enzyme_CS.
IPR012301; Malic_N.
IPR012302; Malic_NAD_bd.
IPR001891; Malic_OxRdtase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

Pfam

PF00390; malic; 1.
PF03949; Malic_M; 1.
Pfam graphical view of domain structure.

PRINTS

PR00072; MALOXRDTASE.

PROSITE

PS00331; MALIC_ENZYMES; 1.

BLOCKS

Q83ML6.

Genome annotation databases

GeneID

1023372; -.
1078212; -.

GenomeReviews

AE014073_GR; S1879.
AE005674_GR; SF1746.

KEGG

sfl:SF1746; -.
sfx:S1879; -.

Phylogenomic databases

HOGENOM

Q83ML6; -.

Genome annotation databases

CMR

Q83ML6; SF1746.

Other

ProtoNet

Q83ML6.

UniRef

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

Keywords

Complete proteome; Metal-binding; NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 565`	`565`	`NAD-dependent malic enzyme.`	`PRO_0000160233`
`ACT_SITE`	`104 104`		`Proton donor (By similarity).`
`ACT_SITE`	`175 175`		`Proton acceptor (By similarity).`
`METAL`	`246 246`		`Divalent metal cation (By similarity).`
`METAL`	`247 247`		`Divalent metal cation (By similarity).`
`METAL`	`270 270`		`Divalent metal cation (By similarity).`
`BINDING`	`157 157`		`NAD (By similarity).`
`BINDING`	`270 270`		`NAD (By similarity).`
`BINDING`	`418 418`		`NAD (By similarity).`
`SITE`	`270 270`	`1`	`Important for activity (By similarity).`

Sequence information

Length: 565 AA [This is the length of the unprocessed precursor]

Molecular weight: 63163 Da [This is the MW of the unprocessed precursor]

CRC64: FFD2C913F7028F3A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEPKTKKQRS LYIPYAGPVL LEFPLLNKGS AFSMEERRNF NLLGLLPEVV ETIEEQAERA 

        70         80         90        100        110        120 
WIQYQGFKTE IDKHIYLRNI QDTNETLFYR LVNNHLDEMM PVIYTPTVGA ACERFSEIYR 

       130        140        150        160        170        180 
RSRGVFISYQ NRHNMDDILQ NVPNHNIKVI VVTDGERILG LGDQGIGGMG IPIGKLSLYT 

       190        200        210        220        230        240 
ACGGISPAYT LPVVLDVGTN NQQLLNDPLY MGWRNPRITD DEYYEFVDEF IQAVKQRWPD 

       250        260        270        280        290        300 
VLLQFEDFAQ KNAMPLLNRY RNEICSFNDD IQGTAAVTVG TLIAASRAAG GQLSEKKIVF 

       310        320        330        340        350        360 
LGAGSAGCGI AEMIIAQTQR EGLSEEAARQ KVFMVDRFGL LTDKMPNLLP FQTKLVQKRE 

       370        380        390        400        410        420 
NLSDWDTDSD VLSLLDVVRN VKPDILIGVS GQTGLFTEEI IREMHKHCPR PIVMPLSNPT 

       430        440        450        460        470        480 
SRVEATPQDI IAWTEGNALV ATGSPFNPVV WKDKIYPIAQ CNNAFIFPGI GLGVIASGAS 

       490        500        510        520        530        540 
RITDEMLMSA SETLAQYSPL VLNGEGLVLP ELKDIQKVSR AIAFAVGKMA QQQGVAVKTS 

       550        560 
AEALQQAIDD NFWQAEYRDY RRTSI

Q83ML6 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