BACSU:BGAL2

Species (Taxon ID)	Bacillus subtilis (strain 168). (224308)
Gene Name(s)	ganA (synonyms: galO, lacA, yvfN)
Protein Name(s)	Beta-galactosidase GanA Beta-gal Beta-1,4-galactooligomerase Galactooligomerase
External Links
UniProt	O07012
EMBL	Z94043 AL009126
PIR	B69649
RefSeq	NP_391293.1
ProteinModelPortal	O07012
SMR	O07012
STRING	224308.BSU34130
CAZy	GH42
PaxDb	O07012
EnsemblBacteria	CAB15418
GeneID	936313
KEGG	bsu:BSU34130
PATRIC	18978828
GenoList	BSU34130
eggNOG	COG1874
HOGENOM	HOG000117811
InParanoid	O07012
KO	K12308
OrthoDB	EOG6GTZGG
BioCyc	BSUB:BSU34130-MONOMER
Proteomes	UP000001570
GO	GO:0009341 GO:0004565 GO:0046872 GO:0006012
Gene3D	3.20.20.80 3.40.50.880
InterPro	IPR013739 IPR013738 IPR029062 IPR003476 IPR013529 IPR013781 IPR017853
Pfam	PF02449 PF08533 PF08532
PIRSF	PIRSF001084
SUPFAM	SSF51445 SSF52317

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0004565	beta-galactosidase activity	PMID:9287030	ECO:0000315			F		LacR is known to be a regulator for lacA activity. Figure 2 shows that when mutant lacR strains are utilized, beta galactosidase activity is up regulated as long as there are no mutations in lacA. Mutant lacA strains results in decreased or no beta galactosidase activity showing that it is necessary for it to occur.	complete
	GO:0004565	beta-galactosidase activity	PMID:2104611	ECO:0000316		PMID:2104611	F		Figure 1 shows that lacR is responsible for regulating beta-galactosidase activity and the lacR1 mutation upregulates beta-galactosidase activity. Figure 2 shows that when the same mutation is applied along with the lacA17 mutation, beta-galactosidase activity decreases showing that lacA is directly responsible for beta-galactosidase activity and is regulated by lacR.	complete
	GO:0004565	beta-galactosidase activity	PMID:17056685	ECO:0000315			F		Figure 3 presents a wild type plate that has grown blue colonies as a result of beta-galactosidase activity. When lacA is interrupted by the insertion of the CAT cassette as in the second plate shown, this expression is eliminated resulting in plain white colonies.	complete
enables	GO:0004565	beta-galactosidase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR003476 InterPro:IPR013529 InterPro:IPR013738 InterPro:IPR013739	F		Seeded From UniProt	complete
involved_in	GO:0005975	carbohydrate metabolic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR003476 InterPro:IPR013529 InterPro:IPR013738	P		Seeded From UniProt	complete
involved_in	GO:0006012	galactose metabolic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR013739	P		Seeded From UniProt	complete
part_of	GO:0009341	beta-galactosidase complex	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR013529	C		Seeded From UniProt	complete
enables	GO:0004565	beta-galactosidase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:3.2.1.23	F		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F		Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F		Seeded From UniProt	complete
enables	GO:0016798	hydrolase activity, acting on glycosyl bonds	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0326	F		Seeded From UniProt	complete
involved_in	GO:0008152	metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0326	P		Seeded From UniProt	complete
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References

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