Q8PE75 (LLDD_XANCP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
L-lactate dehydrogenase [cytochrome]
EC=1.1.2.3

Gene names

Name:	lldD
Ordered Locus Names:	XCC0106

Organism

Xanthomonas campestris pv. campestris (strain ATCC 33913 / NCPPB 528 / LMG 568) [Reference proteome] [HAMAP]

Taxonomic identifier

190485 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xanthomonas › Xanthomonas campestris › Xanthomonas campestris pv. campestris

Protein attributes

Sequence length	386 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+. HAMAP-Rule MF_01559
Cofactor	FMN By similarity.
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	Oxidoreductase
Technical term	Complete proteome Reference proteome
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: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 386	386	L-lactate dehydrogenase [cytochrome] HAMAP-Rule MF_01559		PRO_0000206355
Regions
	Domain	1 – 380	380	FMN hydroxy acid dehydrogenase
	Nucleotide binding	306 – 330	25	FMN By similarity
Sites
	Active site	275	1	Proton acceptor By similarity
	Binding site	24	1	Substrate Potential
	Binding site	106	1	FMN By similarity
	Binding site	127	1	FMN By similarity
	Binding site	129	1	Substrate By similarity
	Binding site	155	1	FMN By similarity
	Binding site	164	1	Substrate By similarity
	Binding site	251	1	FMN By similarity
	Binding site	278	1	Substrate Potential

Sequences

	Sequence		Length	Mass (Da)
	Q8PE75 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 5B3E3BD0B59E46C8	FASTA	386	41,622
	10 20 30 40 50 60 MIISAASDYR AAAEARLPPF LFHYIDGGAY AEHTLRRNVS DLADIALRQR VLRNMSDLSL 70 80 90 100 110 120 STELFGETLA MPVALAPVGL TGMYARRGEV QAARAAAARG IPFTLSTVSV CPIEEVAPAI 130 140 150 160 170 180 DRPMWFQLYV LKDRGFMRNA LERAKTAGVT TLVFTVDMPT PGARYRDAHS GMSGPNASLR 190 200 210 220 230 240 RMLQAMTHPR WAWDVGLLGK PHDLGNISTY RGSPTGLQDY IGWLAANFDP SISWKDLEWI 250 260 270 280 290 300 REFWTGPMVI KGILDPEDAR DAVRFGADGI VVSNHGGRQL DGVLSSARAL PAIADAVKGE 310 320 330 340 350 360 LKILADSGIR SGLDVVRMLA LGADAVLLGR AFVYALAAGG QAGVENLLTL IEREMRVAMI 370 380 LTGTHSVAEI SGDALSRVTR EAAVVP

References

[1]

"Comparison of the genomes of two Xanthomonas pathogens with differing host specificities." da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P. , Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P. Nature 417:459-463(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 33913 / NCPPB 528 / LMG 568.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE008922 Genomic DNA. Translation: AAM39425.1.
RefSeq	NP_635501.1. NC_003902.1.
3D structure databases
ProteinModelPortal	Q8PE75.
ModBase	Search...
Protein-protein interaction databases
STRING	190485.XCC0106.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAM39425; AAM39425; XCC0106.
GeneID	1002315.
KEGG	xcc:XCC0106.
PATRIC	24070761. VBIXanCam115730_0118.
Phylogenomic databases
eggNOG	COG1304.
HOGENOM	HOG000217464.
KO	K00101.
OMA	TYRGNPT.
ProtClustDB	PRK11197.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
HAMAP	MF_01559. L-lact_dehydr.
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]
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

LLDD_XANCP

Accession

Primary (citable) accession number: Q8PE75

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2006
Last sequence update:	October 1, 2002
Last modified:	May 1, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program