C3SMQ7 (C3SMQ7_ECOLX) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
L-lactate dehydrogenase EMBL ACI75751.1

Gene names

ORF Names:

ECs4483 EMBL ACI75751.1

Organism

Escherichia coli EMBL ACI75751.1

Taxonomic identifier

562 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	396 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	(S)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c + 2 H+. SAAS SAAS020920
Cofactor	FMN By similarity. SAAS SAAS020920
Sequence similarities	Contains 1 FMN hydroxy acid dehydrogenase domain. SAAS SAAS020920

Ontologies

Keywords
Ligand	FMN SAAS SAAS020920 Flavoprotein SAAS SAAS020920
Molecular function	Oxidoreductase SAAS SAAS020920
Gene Ontology (GO)
Biological process	lactate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	FMN binding Inferred from electronic annotation. Source: InterPro L-lactate dehydrogenase (cytochrome) activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	C3SMQ7 [UniParc]. Last modified June 16, 2009. Version 1. Checksum: CA0D8E208613BF83	FASTA	396	42,758
	10 20 30 40 50 60 MIISAASDYR AAAQRILPPF LFHYMDGGAY SEYTLRRNVE DLSEVALRQR ILKNMSDLSL 70 80 90 100 110 120 ETTLFNEKLS MPVALAPVGL CGMYARRGEV QAAKAADAHG IPFTLSTVSV CPIEEVAPAI 130 140 150 160 170 180 KRPMWFQLYV LRDRGFMRNA LERAKAAGCS TLVFTVDMPT PGARYRDAHS GMSGPNAAMR 190 200 210 220 230 240 RYLQAVTHPQ WAWDVGLNGR PHDLGNISAY LGKPTGLEDY IGWLGNNFDP SISWKDLEWI 250 260 270 280 290 300 RDFWDGPMVI KGILDPEDAR DAVRFGADGI VVSNHGGRQL DGVLSSARAL PAIADAVKGD 310 320 330 340 350 360 IAILADSGIR NGLDVVRMIA LGADTVLLGR AFLYALATAG QAGVANLLNL IEKEMKVAMT 370 380 390 LTGAKSISEI TQDSLVQGLG KELPTALAPM AKGNAA

References

[1]

"A precise reconstruction of the emergence and constrained radiations of Escherichia coli O157 portrayed by backbone concatenomic analysis." Leopold S.R., Magrini V., Holt N.J., Shaikh N., Mardis E.R., Cagno J., Ogura Y., Iguchi A., Hayashi T., Mellmann A., Karch H., Besser T.E., Sawyer S.A., Whittam T.S., Tarr P.I. Proc. Natl. Acad. Sci. U.S.A. 106:8713-8718(2009) [PubMed: 19439656] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: 493/89 EMBL ACI75751.1, 86-24 EMBL ACI75752.1, 87-14 EMBL ACI75753.1 and TW14359 EMBL ACI75755.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	EU893185 Genomic DNA. Translation: ACI75751.1. EU893186 Genomic DNA. Translation: ACI75752.1. EU893187 Genomic DNA. Translation: ACI75753.1. EU893189 Genomic DNA. Translation: ACI75755.1.
3D structure databases
ProteinModelPortal	C3SMQ7.
SMR	C3SMQ7. Positions 3-377.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
HAMAP	MF_01559. L_lact_dehydr. [Tree]
InterPro	IPR013785. Aldolase_TIM. IPR012133. Alpha-hydoxy_acid_DH_FMN. IPR000262. FMN-dep_DH. IPR008259. FMN_hydac_DH_AS. IPR020920. L-lactate_DHase_cyt. [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

C3SMQ7_ECOLX

Accession

Primary (citable) accession number: C3SMQ7

Entry history

Integrated into UniProtKB/TrEMBL:	June 16, 2009
Last sequence update:	June 16, 2009
Last modified:	December 14, 2011
This is version 16 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)