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Protein

Lactate 2-monooxygenase

Gene
N/A
Organism
Mycobacterium smegmatis
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei45SubstratePROSITE-ProRule annotation1
Binding sitei129FMNPROSITE-ProRule annotation1
Binding sitei151FMNPROSITE-ProRule annotation1
Binding sitei153SubstratePROSITE-ProRule annotation1
Binding sitei179FMNPROSITE-ProRule annotation1
Binding sitei188SubstratePROSITE-ProRule annotation1
Binding sitei267FMNPROSITE-ProRule annotation1
Active sitei291Proton acceptorPROSITE-ProRule annotation1
Binding sitei294SubstratePROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi321 – 345FMNPROSITE-ProRule annotationAdd BLAST25

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

Flavoprotein, FMN

Names & Taxonomyi

Protein namesi
Recommended name:
Lactate 2-monooxygenase (EC:1.13.12.4)
Alternative name(s):
Lactate oxidase
OrganismiMycobacterium smegmatis
Taxonomic identifieri1772 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00002063262 – 394Lactate 2-monooxygenaseAdd BLAST393

Interactioni

Protein-protein interaction databases

STRINGi246196.MSMEG_3962.

Structurei

3D structure databases

ProteinModelPortaliP21795.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini19 – 394FMN hydroxy acid dehydrogenasePROSITE-ProRule annotationAdd BLAST376

Sequence similaritiesi

Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family.PROSITE-ProRule annotation
Contains 1 FMN hydroxy acid dehydrogenase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105DMF. Bacteria.
COG1304. LUCA.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR012133. Alpha-hydoxy_acid_DH_FMN.
IPR000262. FMN-dep_DH.
IPR008259. FMN_hydac_DH_AS.
[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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P21795-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNWGDYENE IYGQGLVGVA PTLPMSYADW EAHAQQALPP GVLSYVAGGS
60 70 80 90 100
GDEHTQRANV EAFKHWGLMP RMLMAATERD LSVELWGKTW AAPMFFAPIG
110 120 130 140 150
VIALCAQDGH GDAASAQASA RTGVPYITST LAVSSLEDIR KHAGDTPAYF
160 170 180 190 200
QLYYPEDRDL AESFIRRAEE AGYDGLVITL DTWIFGWRPR DLTISNFPFL
210 220 230 240 250
RGLCLTNYVT DPVFQKKFKA HSGVEAEGLR DNPRLAADFW HGLFGHSVTW
260 270 280 290 300
EDIDWVRSIT KMPVILKGIQ HPDDARRAVD SGVDGIYCSN HGGRQANGGL
310 320 330 340 350
PALDCLPEVV KASGDTPVLF DSGIRTGADV VKALAMGASA VGIGRPYAWG
360 370 380 390
AALGGSKGIE HVARSLLAEA DLIMAVDGYR NLKELTIDAL RPTR
Length:394
Mass (Da):42,747
Last modified:January 23, 2007 - v3
Checksum:iD535A910E7F7232A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05402 Genomic DNA. Translation: AAA60429.1.
PIRiA35745.
RefSeqiWP_003895417.1. NZ_LN831039.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05402 Genomic DNA. Translation: AAA60429.1.
PIRiA35745.
RefSeqiWP_003895417.1. NZ_LN831039.1.

3D structure databases

ProteinModelPortaliP21795.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi246196.MSMEG_3962.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105DMF. Bacteria.
COG1304. LUCA.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR012133. Alpha-hydoxy_acid_DH_FMN.
IPR000262. FMN-dep_DH.
IPR008259. FMN_hydac_DH_AS.
[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]
ProtoNetiSearch...

Entry informationi

Entry nameiLA2M_MYCSM
AccessioniPrimary (citable) accession number: P21795
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 77 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.