SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P21795

- LA2M_MYCSM

UniProt

P21795 - LA2M_MYCSM

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Lactate 2-monooxygenase

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

Functioni

Catalytic activityi

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

Cofactori

FMN.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei45 – 451Substrate Reviewed prediction
Binding sitei129 – 1291FMN By similarity
Binding sitei151 – 1511FMN By similarity
Binding sitei153 – 1531Substrate By similarity
Binding sitei179 – 1791FMN By similarity
Binding sitei188 – 1881Substrate By similarity
Binding sitei267 – 2671FMN By similarity
Active sitei291 – 2911Proton acceptor By similarity
Binding sitei294 – 2941Substrate Reviewed prediction

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi321 – 34525FMN By similarityAdd
BLAST

GO - Molecular functioni

  1. FMN binding Source: InterPro
  2. lactate 2-monooxygenase activity Source: UniProtKB-EC
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 lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 394393Lactate 2-monooxygenasePRO_0000206326Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP21795.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 394376FMN hydroxy acid dehydrogenaseAdd
BLAST

Sequence similaritiesi

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

MSNWGDYENE IYGQGLVGVA PTLPMSYADW EAHAQQALPP GVLSYVAGGS    50
GDEHTQRANV EAFKHWGLMP RMLMAATERD LSVELWGKTW AAPMFFAPIG 100
VIALCAQDGH GDAASAQASA RTGVPYITST LAVSSLEDIR KHAGDTPAYF 150
QLYYPEDRDL AESFIRRAEE AGYDGLVITL DTWIFGWRPR DLTISNFPFL 200
RGLCLTNYVT DPVFQKKFKA HSGVEAEGLR DNPRLAADFW HGLFGHSVTW 250
EDIDWVRSIT KMPVILKGIQ HPDDARRAVD SGVDGIYCSN HGGRQANGGL 300
PALDCLPEVV KASGDTPVLF DSGIRTGADV VKALAMGASA VGIGRPYAWG 350
AALGGSKGIE HVARSLLAEA DLIMAVDGYR NLKELTIDAL RPTR 394
Length:394
Mass (Da):42,747
Last modified:January 23, 2007 - v3
Checksum:iD535A910E7F7232A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05402 Genomic DNA. Translation: AAA60429.1.
PIRiA35745.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05402 Genomic DNA. Translation: AAA60429.1 .
PIRi A35745.

3D structure databases

ProteinModelPortali P21795.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
InterProi IPR013785. Aldolase_TIM.
IPR012133. Alpha-hydoxy_acid_DH_FMN.
IPR000262. FMN-dep_DH.
IPR008259. FMN_hydac_DH_AS.
[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. "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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.

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: October 16, 2013
This is version 68 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

External Data

Dasty 3

Similar proteinsi