[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=2324094 [NCBI, ExPASy, EBI, Israel, Japan] Giegel D.A., Williams C.H. Jr., Massey V.; "L-lactate 2-monooxygenase from Mycobacterium smegmatis. Cloning, nucleotide sequence, and primary structure homology within an enzyme family."; J. Biol. Chem. 265:6626-6632(1990).
[2]	PARTIAL PROTEIN SEQUENCE. PubMed=3571231 [NCBI, ExPASy, EBI, Israel, Japan] Giegel D.A., Massey V., Williams C.H. Jr.; "L-lactate-2-monooxygenase. Sequence of peptides containing residues modified by 1-fluoro-2,4-dinitrobenzene."; J. Biol. Chem. 262:5705-5710(1987).

Comments

CATALYTIC ACTIVITY: (S)-lactate + O₂ = acetate + CO₂ + H₂O.
COFACTOR: FMN.
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

J05402; AAA60429.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A35745; A35745.

3D structure databases

HSSP

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

ModBase

P21795.

Ontologies

GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0010181;	Molecular function: FMN binding (inferred from electronic annotation from InterPro).
GO:0050040;	Molecular function: lactate 2-monooxygenase activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

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

ProtoNet

P21795.

UniRef

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

Keywords

Direct protein sequencing; Flavoprotein; FMN; Monooxygenase; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 394`	`393`	`Lactate 2-monooxygenase.`	`PRO_0000206326`
`DOMAIN`	`19 394`	`376`	`FMN hydroxy acid dehydrogenase.`
`NP_BIND`	`321 345`	`25`	`FMN (By similarity).`
`ACT_SITE`	`291 291`		`Proton acceptor (By similarity).`
`BINDING`	`45 45`		`Substrate (Potential).`
`BINDING`	`129 129`		`FMN (By similarity).`
`BINDING`	`151 151`		`FMN (By similarity).`
`BINDING`	`153 153`		`Substrate (By similarity).`
`BINDING`	`179 179`		`FMN (By similarity).`
`BINDING`	`188 188`		`Substrate (By similarity).`
`BINDING`	`267 267`		`FMN (By similarity).`
`BINDING`	`294 294`		`Substrate (Potential).`

Sequence information

Length: 394 AA [This is the length of the unprocessed precursor]

Molecular weight: 42747 Da [This is the MW of the unprocessed precursor]

CRC64: D535A910E7F7232A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSNWGDYENE IYGQGLVGVA PTLPMSYADW EAHAQQALPP GVLSYVAGGS GDEHTQRANV 

        70         80         90        100        110        120 
EAFKHWGLMP RMLMAATERD LSVELWGKTW AAPMFFAPIG VIALCAQDGH GDAASAQASA 

       130        140        150        160        170        180 
RTGVPYITST LAVSSLEDIR KHAGDTPAYF QLYYPEDRDL AESFIRRAEE AGYDGLVITL 

       190        200        210        220        230        240 
DTWIFGWRPR DLTISNFPFL RGLCLTNYVT DPVFQKKFKA HSGVEAEGLR DNPRLAADFW 

       250        260        270        280        290        300 
HGLFGHSVTW EDIDWVRSIT KMPVILKGIQ HPDDARRAVD SGVDGIYCSN HGGRQANGGL 

       310        320        330        340        350        360 
PALDCLPEVV KASGDTPVLF DSGIRTGADV VKALAMGASA VGIGRPYAWG AALGGSKGIE 

       370        380        390 
HVARSLLAEA DLIMAVDGYR NLKELTIDAL RPTR

P21795 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