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B2FIJ0

- LLDD_STRMK

UniProt

B2FIJ0 - LLDD_STRMK

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Protein
L-lactate dehydrogenase
Gene
lldD, Smlt2908
Organism
Stenotrophomonas maltophilia (strain K279a)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Catalyzes the conversion of L-lactate to pyruvate. Is coupled to the respiratory chain By similarity.

Catalytic activityi

(S)-lactate + an oxidized electron acceptor = pyruvate + a reduced electron acceptor.

Cofactori

FMN By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei24 – 241Substrate Reviewed prediction
Binding sitei106 – 1061FMN By similarity
Binding sitei127 – 1271FMN By similarity
Binding sitei129 – 1291Substrate By similarity
Binding sitei155 – 1551FMN By similarity
Binding sitei164 – 1641Substrate By similarity
Binding sitei251 – 2511FMN By similarity
Active sitei275 – 2751Proton acceptor By similarity
Binding sitei278 – 2781Substrate Reviewed prediction

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi306 – 33025FMN By similarity
Add
BLAST

GO - Molecular functioni

  1. FMN binding Source: InterPro
  2. L-lactate dehydrogenase (cytochrome) activity Source: UniProtKB-HAMAP
Complete GO annotation...

GO - Biological processi

  1. lactate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Flavoprotein, FMN

Enzyme and pathway databases

BioCyciSMAL522373:GJE8-2808-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
L-lactate dehydrogenase (EC:1.1.-.-)
Gene namesi
Name:lldD
Ordered Locus Names:Smlt2908
OrganismiStenotrophomonas maltophilia (strain K279a)
Taxonomic identifieri522373 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeStenotrophomonasStenotrophomonas maltophilia group
ProteomesiUP000008840: Chromosome

Subcellular locationi

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 379379L-lactate dehydrogenase
PRO_0000383449Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi522373.Smlt2908.

Structurei

3D structure databases

ProteinModelPortaliB2FIJ0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 379379FMN hydroxy acid dehydrogenase
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1304.
HOGENOMiHOG000217464.
KOiK00101.
OMAiDCTLLGR.
OrthoDBiEOG6HMXBG.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01559. L_lact_dehydr.
InterProiIPR013785. Aldolase_TIM.
IPR012133. Alpha-hydoxy_acid_DH_FMN.
IPR000262. FMN-dep_DH.
IPR008259. FMN_hydac_DH_AS.
IPR020920. L-lactate_DHase_bac.
[Graphical view]
PfamiPF01070. FMN_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF000138. Al-hdrx_acd_dh. 1 hit.
PROSITEiPS00557. FMN_HYDROXY_ACID_DH_1. 1 hit.
PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B2FIJ0-1 [UniParc]FASTAAdd to Basket

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MIISASTDYR AAAERRLPPF LFHYIDGGAY AEHTLKRNVS DLSDIALRQR    50
ILRNMSDLSL ETELFGETLA MPVALAPVGL TGMYARRGEV QAARAADSRG 100
IPFTLSTVSV CPIEEVAPAI QRPMWFQLYV LRDRGFMRNA LERAQAAGVT 150
TLVFTVDMPV PGARYRDAHS GMSGPNASLR RIGQAITHPH WAWDVGLFGR 200
PHDLGNISTY RGNPTGLEDY IGWLGSNFDP SISWKDLEWI REFWKGPMVI 250
KGILDPDDAR DAVRFGADGI VVSNHGGRQL DGVLSTARAL PAIADAVQGD 300
LKILADSGIR TGLDVVRMLA LGADTVLLGR AFVYALAAQG EAGVANLLDL 350
IAKEMRVAMT LTGARRIADI GRDSLVSLP 379
Length:379
Mass (Da):41,191
Last modified:June 10, 2008 - v1
Checksum:i0E6CC723FB9C3DFA
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM743169 Genomic DNA. Translation: CAQ46364.1.
RefSeqiWP_005410033.1. NC_010943.1.
YP_001972658.1. NC_010943.1.

Genome annotation databases

EnsemblBacteriaiCAQ46364; CAQ46364; Smlt2908.
GeneIDi6394487.
KEGGisml:Smlt2908.
PATRICi23701321. VBISteMal45202_2730.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM743169 Genomic DNA. Translation: CAQ46364.1 .
RefSeqi WP_005410033.1. NC_010943.1.
YP_001972658.1. NC_010943.1.

3D structure databases

ProteinModelPortali B2FIJ0.
ModBasei Search...

Protein-protein interaction databases

STRINGi 522373.Smlt2908.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAQ46364 ; CAQ46364 ; Smlt2908 .
GeneIDi 6394487.
KEGGi sml:Smlt2908.
PATRICi 23701321. VBISteMal45202_2730.

Phylogenomic databases

eggNOGi COG1304.
HOGENOMi HOG000217464.
KOi K00101.
OMAi DCTLLGR.
OrthoDBi EOG6HMXBG.

Enzyme and pathway databases

BioCyci SMAL522373:GJE8-2808-MONOMER.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_01559. L_lact_dehydr.
InterProi IPR013785. Aldolase_TIM.
IPR012133. Alpha-hydoxy_acid_DH_FMN.
IPR000262. FMN-dep_DH.
IPR008259. FMN_hydac_DH_AS.
IPR020920. L-lactate_DHase_bac.
[Graphical view ]
Pfami PF01070. FMN_dh. 1 hit.
[Graphical view ]
PIRSFi PIRSF000138. Al-hdrx_acd_dh. 1 hit.
PROSITEi PS00557. FMN_HYDROXY_ACID_DH_1. 1 hit.
PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The complete genome, comparative and functional analysis of Stenotrophomonas maltophilia reveals an organism heavily shielded by drug resistance determinants."
    Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A., Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E., Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S., Quail M.A.
    , Rajandream M.A., Harris D., Churcher C., Bentley S.D., Parkhill J., Thomson N.R., Avison M.B.
    Genome Biol. 9:R74.1-R74.13(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K279a.

Entry informationi

Entry nameiLLDD_STRMK
AccessioniPrimary (citable) accession number: B2FIJ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: June 10, 2008
Last modified: September 3, 2014
This is version 39 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

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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