Lactate 2-monooxygenase - Mycobacterium smegmatis

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Reviewed, UniProtKB/Swiss-Prot P21795 (LA2M_MYCSM)

Last modified June 16, 2009. Version 55. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein names	Recommended name: Lactate 2-monooxygenase EC=1.13.12.4 Alternative name(s): Lactate oxidase
Organism	Mycobacterium smegmatis
Taxonomic identifier	1772 [NCBI]
Taxonomic lineage	Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length	394 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity

(S)-lactate + O₂ = acetate + CO₂ + H₂O.

Cofactor

FMN.

Sequence similarities

Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family.

Contains 1 FMN hydroxy acid dehydrogenase domain.

Ontologies

Keywords
Ligand	FMN Flavoprotein
Molecular function	Monooxygenase Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	FMN binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro lactate 2-monooxygenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

Removed

Chain

393

Lactate 2-monooxygenase

PRO_0000206326

Regions

Domain

376

FMN hydroxy acid dehydrogenase

Nucleotide binding

25

FMN By similarity

Sites

Active site

1

Proton acceptor By similarity

Binding site

1

Substrate Potential

Binding site

1

FMN By similarity

Binding site

1

FMN By similarity

Binding site

1

Substrate By similarity

Binding site

1

FMN By similarity

Binding site

1

Substrate By similarity

Binding site

1

FMN By similarity

Binding site

1

Substrate Potential

Sequences

Sequence

Length

Mass (Da)

Tools

P21795-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: D535A910E7F7232A
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394

42,747

        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

References

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

Cross-references

Sequence databases
	J05402 Genomic DNA. Translation: AAA60429.1.
PIR	A35745.
3D structure databases
HSSP	HSSP built from PDB template 1GOX based on UniProtKB P05414.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.13.12.4. 259.
Family and domain databases
InterPro	IPR012133. a-Hydoxy_acid_DH_FMN. IPR013785. Aldolase_TIM. IPR000262. FMN-dep_DH. IPR017934. FMN-dep_OHA_DH. IPR008259. FMN_hydac_DH_AS. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
Pfam	PF01070. FMN_dh. 1 hit. [Graphical view]
PIRSF	PIRSF000138. Al-hdrx_acd_dh. 1 hit.
PROSITE	PS00557. FMN_HYDROXY_ACID_DH_1. 1 hit. PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LA2M_MYCSM

Accession

Primary (citable) accession number: P21795

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 55 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents