Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta - Lactobacillus rhamnosus (strain ATCC 53103 / GG)

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C7TEG3 (C7TEG3_LACRG) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 27. History...

Clusters with 100%, 90%, 50% identity |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info Customize order

Names and origin

Protein names

Recommended name:
Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta HAMAP-Rule MF_01395
Short name=ACCase subunit beta HAMAP-Rule MF_01395
Short name=Acetyl-CoA carboxylase carboxyltransferase subunit beta HAMAP-Rule MF_01395
EC=6.4.1.2 HAMAP-Rule MF_01395

Gene names

Name:	accD HAMAP-Rule MF_01395 EMBL CAR88006.1
Ordered Locus Names:	LGG_02111, LRHM_2030 EMBL BAI42557.1

Organism

Lactobacillus rhamnosus (strain ATCC 53103 / GG) [Complete proteome] [HAMAP]

Taxonomic identifier

568703 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacilli › Lactobacillales › Lactobacillaceae › Lactobacillus ›

Protein attributes

Sequence length	271 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO₂ group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA By similarity. HAMAP-Rule MF_01395
Catalytic activity	ATP + acetyl-CoA + HCO₃^- = ADP + phosphate + malonyl-CoA. HAMAP-Rule MF_01395
Cofactor	Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_01395
Pathway	Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. HAMAP-Rule MF_01395
Subunit structure	Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD) By similarity. HAMAP-Rule MF_01395 SAAS SAAS011762
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_01395 SAAS SAAS000022.
Sequence similarities	Belongs to the AccD/PCCB family. HAMAP-Rule MF_01395

Ontologies

Keywords
Biological process	Fatty acid biosynthesis HAMAP-Rule MF_01395 Fatty acid metabolism Lipid biosynthesis Lipid metabolism
Cellular component	Cytoplasm HAMAP-Rule MF_01395 SAAS SAAS000022
Domain	Zinc-finger HAMAP-Rule MF_01395
Ligand	ATP-binding HAMAP-Rule MF_01395 Metal-binding Nucleotide-binding Zinc
Molecular function	Ligase HAMAP-Rule MF_01395 Transferase EMBL CAR88006.1
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	fatty acid biosynthetic process Inferred from electronic annotation. Source: HAMAP malonyl-CoA biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	acetyl-CoA carboxylase complex Inferred from electronic annotation. Source: InterPro
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acetyl-CoA carboxylase activity Inferred from electronic annotation. Source: HAMAP transferase activity Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Regions

Zinc finger

25 – 46

C4-type By similarity HAMAP-Rule MF_01395

Sites

Metal binding

Zinc By similarity HAMAP-Rule MF_01395

Metal binding

Zinc By similarity HAMAP-Rule MF_01395

Metal binding

Zinc By similarity HAMAP-Rule MF_01395

Metal binding

Zinc By similarity HAMAP-Rule MF_01395

Sequences

Sequence

Length

Mass (Da)

Tools

C7TEG3 [UniParc].

Last modified October 13, 2009. Version 1.
Checksum: 75F9E4ACD4F69C71
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FASTA

271

29,469

        10         20         30         40         50         60 
MFQPQLTQEA LAREAALPEN LWIQCPYCKQ GSYRESLGDA QVCPHCHYGF RITAKKRLAL 

        70         80         90        100        110        120 
VATDATEWDA DLTTTDPLDF PGYEKKLAAG RQASGLEDSV WTGQAKIGGQ VCGLGIMDPK 

       130        140        150        160        170        180 
FMMGSLGTVT GERITRLFEK ATEANLPVVL YCASGGARMQ EGIHSLMQMA KVSAAVKNHS 

       190        200        210        220        230        240 
NAGLLFISVL TDPTMGGVTA SFAMQGDITL AEPHSLIGFA GRRVIEQTIN QKLPQNFQRA 

       250        260        270 
ETVLQSGFID AIVPRSEQVS YIGDMLQMHR A

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References

[1]

"Complete genome sequence of the probiotic Lactobacillus rhamnosus ATCC 53103."
Morita H., Toh H., Oshima K., Murakami M., Taylor T.D., Igimi S., Hattori M.
J. Bacteriol. 191:7630-7631(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 53103 EMBL BAI42557.1 and ATCC 53103 / GG [Tokyo].

[2]

"Comparative genomic analysis of Lactobacillus rhamnosus GG reveals pili containing a human- mucus binding protein."
Kankainen M., Paulin L., Tynkkynen S., von Ossowski I., Reunanen J., Partanen P., Satokari R., Vesterlund S., Hendrickx A.P.A., Lebeer S., De Keersmaecker S.C.J., Vanderleyden J., Hamalinen T., Laukkanen S., Salovuori N., Ritari J., Alatalo E., Korpela R.

de Vos W.M.
Proc. Natl. Acad. Sci. U.S.A. 106:17193-17198(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 53103 / GG [Helsinki].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP011548 Genomic DNA. Translation: BAI42557.1. FM179322 Genomic DNA. Translation: CAR88006.1.
RefSeq	YP_003171857.1. NC_013198.1. YP_005866522.1. NC_017482.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	568703.LGG_02111.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAI42557; BAI42557; LRHM_2030. CAR88006; CAR88006; LGG_02111.
GeneID	12475160. 8421827.
KEGG	lrg:LRHM_2030. lrh:LGG_02111.
PATRIC	22265472. VBILacRha2892_2004.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0777.
HOGENOM	HOG000021671.
KO	K01963.
OMA	GLWIKCP.
ProtClustDB	CLSK2318266.
Enzyme and pathway databases
UniPathway	UPA00655; UER00711.
Family and domain databases
HAMAP	MF_01395. AcetylCoA_CT_beta.
InterPro	IPR000438. Acetyl_CoA_COase_Trfase_b_su. IPR000022. Carboxyl_trans. IPR011762. COA_CT_N. [Graphical view]
Pfam	PF01039. Carboxyl_trans. 1 hit. [Graphical view]
PRINTS	PR01070. ACCCTRFRASEB.
PROSITE	PS50980. COA_CT_NTER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

C7TEG3_LACRG

Accession

Primary (citable) accession number: C7TEG3
Secondary accession number(s): C8UW03

Entry history

Integrated into UniProtKB/TrEMBL:	October 13, 2009
Last sequence update:	October 13, 2009
Last modified:	May 1, 2013
This is version 27 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information