NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=SC510;
PubMed=2211521 [NCBI, ExPASy, EBI, Israel, Japan]
Crouzet J., Cameron B., Cauchois L., Rigault S., Rouyez M.-C., Blanche F., Thibaut D., Debussche L.;
"Genetic and sequence analysis of an 8.7-kilobase Pseudomonas denitrificans fragment carrying eight genes involved in transformation of precorrin-2 to cobyrinic acid.";
J. Bacteriol. 172:5980-5990(1990).

[2]

PROTEIN SEQUENCE OF 2-7; 60-69; 112-122 AND 143-148, SEQUENCE REVISION, AND CHARACTERIZATION.
PubMed=1732193 [NCBI, ExPASy, EBI, Israel, Japan]
Blanche F., Thibaut D., Famechon A., Debussche L., Cameron B., Crouzet J.;
"Precorrin-6x reductase from Pseudomonas denitrificans: purification and characterization of the enzyme and identification of the structural gene.";
J. Bacteriol. 174:1036-1042(1992).

Comments

FUNCTION: Catalyzes the reduction of the macrocycle of precorrin-6X into precorrin-6Y.
CATALYTIC ACTIVITY: Precorrin-6B + NADP⁺ = precorrin-6A + NADPH.
PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinic acid a,c-diamide from precorrin-2 (aerobic route): step 6/10 .
SIMILARITY: Belongs to the precorrin-6x reductase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M59301; AAA25799.1; ALT_SEQ; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

F36145; F36145.

3D structure databases

ModBase

P21920.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-113; -.

Ontologies

GO:0016994;	Molecular function: precorrin-6A reductase activity (inferred from electronic annotation from InterPro).
GO:0009236;	Biological process: cobalamin biosynthetic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR003723; Cbl_synth_CobK/CbiJ.
Graphical view of domain structure.

Pfam

PF02571; CbiJ; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR00715; precor6x_red; 1.

PROSITE

PS51014; COBK_CBIJ; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P21920.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cobalamin biosynthesis; Direct protein sequencing; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 261`	`260`	`Precorrin-6A reductase.`	`PRO_0000135920`

Sequence information

Length: 261 AA [This is the length of the unprocessed precursor]

Molecular weight: 28096 Da [This is the MW of the unprocessed precursor]

CRC64: B0AE2E902D35F02C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAGSLFDTSA MEKPRILILG GTTEARELAR RLAEDVRYDT AISLAGRTAD PRPQPVKTRI 

        70         80         90        100        110        120 
GGFGGADGLA HFVHDENIAL LVDATHPFAA RISHNAADAA QRTGVALIAL RRPEWVPLPG 

       130        140        150        160        170        180 
DRWTAVDSVV EAVSALGDRR RRVFLAIGRQ EAFHFEVAPQ HSYVIRSVDP VTPPLNLPDQ 

       190        200        210        220        230        240 
EAILATGPFA EADEAALLRS RQIDVIVAKN SGGSATYGKI AAARRLGIEV IMVERRKPAD 

       250        260 
VPTVGSCDEA LNRIAHWLAP A

P21920 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools