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)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c + 2 H⁺.
COFACTOR: FMN (By similarity).
SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family.
SIMILARITY: Contains 1 FMN hydroxy acid dehydrogenase domain.

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; AAN45091.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014073; AAP19101.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_709384.1; -.
NP_839290.1; -.

3D structure databases

HSSP

P05414; 1GOX. [HSSP ENTRY / SWISS-3DIMAGE / PDB]

ModBase

Q83PP7.

Enzyme and pathway databases

BioCyc

SFLE198214:AAN45091.1-MON; -.

Ontologies

GO:0004460;	Molecular function: L-lactate dehydrogenase (cytochrome) activity (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01559; -; 1.
PBIL [Tree]

InterPro

IPR013785; Aldolase_TIM.
IPR012133; Alpha_OHA_DHase_FMN.
IPR008259; FMN_hydac_DHase_AS.
IPR000262; FMN_OHA_DHase.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.70; Aldolase_TIM; 1.

Pfam

PF01070; FMN_dh; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000138; Al-hdrx_acd_dh; 1.

PROSITE

PS00557; FMN_HYDROXY_ACID_DH_1; 1.
PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

Q83PP7.

Genome annotation databases

GeneID

1026893; -.
1078229; -.

GenomeReviews

AE014073_GR; S4124.
AE005674_GR; SF3644.

KEGG

sfl:SF3644; -.
sfx:S4124; -.

Phylogenomic databases

HOGENOM

Q83PP7; -.

Genome annotation databases

CMR

Q83PP7; SF3644.

Other

ProtoNet

Q83PP7.

UniRef

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

Keywords

Complete proteome; Flavoprotein; FMN; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 396`	`396`	`L-lactate dehydrogenase [cytochrome].`	`PRO_0000206350`
`DOMAIN`	`1 380`	`380`	`FMN hydroxy acid dehydrogenase.`
`NP_BIND`	`306 330`	`25`	`FMN (By similarity).`
`ACT_SITE`	`275 275`		`Proton acceptor (By similarity).`
`BINDING`	`24 24`		`Substrate (Potential).`
`BINDING`	`106 106`		`FMN (By similarity).`
`BINDING`	`127 127`		`FMN (By similarity).`
`BINDING`	`129 129`		`Substrate (By similarity).`
`BINDING`	`155 155`		`FMN (By similarity).`
`BINDING`	`164 164`		`Substrate (By similarity).`
`BINDING`	`251 251`		`FMN (By similarity).`
`BINDING`	`278 278`		`Substrate (Potential).`

Sequence information

Length: 396 AA [This is the length of the unprocessed precursor]

Molecular weight: 42758 Da [This is the MW of the unprocessed precursor]

CRC64: CA0D8E208613BF83 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MIISAASDYR AAAQRILPPF LFHYMDGGAY SEYTLRRNVE DLSEVALRQR ILKNMSDLSL 

        70         80         90        100        110        120 
ETTLFNEKLS MPVALAPVGL CGMYARRGEV QAAKAADAHG IPFTLSTVSV CPIEEVAPAI 

       130        140        150        160        170        180 
KRPMWFQLYV LRDRGFMRNA LERAKAAGCS TLVFTVDMPT PGARYRDAHS GMSGPNAAMR 

       190        200        210        220        230        240 
RYLQAVTHPQ WAWDVGLNGR PHDLGNISAY LGKPTGLEDY IGWLGNNFDP SISWKDLEWI 

       250        260        270        280        290        300 
RDFWDGPMVI KGILDPEDAR DAVRFGADGI VVSNHGGRQL DGVLSSARAL PAIADAVKGD 

       310        320        330        340        350        360 
IAILADSGIR NGLDVVRMIA LGADTVLLGR AFLYALATAG QAGVANLLNL IEKEMKVAMT 

       370        380        390 
LTGAKSISEI TQDSLVQGLG KELPTALAPM AKGNAA

Q83PP7 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