[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=CCUG 2071 / LMG 3368 / NCIB 8687; Silver S., Phung L.T., Malo B.J.; "Genes for arsenite oxidation from Alcaligenes faecalis."; Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.

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

AY297781; AAQ19817.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P05414; 1AL8. [HSSP ENTRY / SWISS-3DIMAGE / PDB]

ModBase

Q6WB83.

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).

Other

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

Keywords

Flavoprotein; FMN; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 379`	`379`	`L-lactate dehydrogenase [cytochrome].`	`PRO_0000206330`
`DOMAIN`	`1 379`	`379`	`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: 379 AA [This is the length of the unprocessed precursor]

Molecular weight: 41414 Da [This is the MW of the unprocessed precursor]

CRC64: 9975D092C4DDF2F9 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MIISSSTDYR RAAQKRLPPF LFHYIDGGAY AEHTLRRNVD DLAEVALRQR VLKDMSQLDT 

        70         80         90        100        110        120 
SIDLFGEKLS MPVALSPVGL TGMYARRGEV QAARAADARG IPFTMSSVSV CPIEEVAPRL 

       130        140        150        160        170        180 
SRPMWFQLYV LKDRGFMRNA LERAQAAGCS TLVFTVDMPV PGARYRDAHS GMSGPNAALR 

       190        200        210        220        230        240 
RYAQAVMHPR WAWDVGLLGR PHDLGNISRY LGKPTGLEDY MGYLGANFDP SISWKDLEWI 

       250        260        270        280        290        300 
REFWKGPMLI KGILDPDDAR DAVRFGADGI IVSNHGGRQL DGVLSSARAL PAIADAVKGQ 

       310        320        330        340        350        360 
IKILADSGIR SGLDVVRMIA LGADAAMLGR AYIYALAAAG QSGVDHLLGL IEKEIRVAMT 

       370 
LTSVSSISQI TSELLVREP

Q6WB83 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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