UniProt: E7AAT5

Database: UniProt
Entry: E7AAT5_HELFC

LinkDB:  E7AAT5_HELFC 
Original site:  E7AAT5_HELFC

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (16)   
   InterPro (8)   
   Pfam (3)   
   PROSITE (4)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (28)   

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ID   E7AAT5_HELFC            Unreviewed;       449 AA.
AC   E7AAT5;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=Biotin carboxylase {ECO:0000256|ARBA:ARBA00013263, ECO:0000256|RuleBase:RU365063};
DE            EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263, ECO:0000256|RuleBase:RU365063};
DE   AltName: Full=Acetyl-coenzyme A carboxylase biotin carboxylase subunit A {ECO:0000256|RuleBase:RU365063};
GN   Name=accC {ECO:0000313|EMBL:CBY82756.1};
GN   OrderedLocusNames=Hfelis_06720 {ECO:0000313|EMBL:CBY82756.1};
OS   Helicobacter felis (strain ATCC 49179 / NCTC 12436 / CS1).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=936155 {ECO:0000313|EMBL:CBY82756.1, ECO:0000313|Proteomes:UP000007934};
RN   [1] {ECO:0000313|Proteomes:UP000007934}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49179 / NCTC 12436 / CS1
RC   {ECO:0000313|Proteomes:UP000007934};
RA   Arnold A., Zigova Z., Lawley T., Falkow S., Bentley S., Aslett M.,
RA   Muller A.;
RT   "Comparative whole genome analysis of the carcinogenic bacterial pathogen
RT   Helicobacter felis.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBY82756.1, ECO:0000313|Proteomes:UP000007934}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49179 / NCTC 12436 / CS1
RC   {ECO:0000313|Proteomes:UP000007934};
RX   PubMed=21402865;
RA   Arnold I.C., Zigova Z., Holden M., Lawley T.D., Rad R., Dougan G.,
RA   Falkow S., Bentley S.D., Muller A.;
RT   "Comparative whole genome sequence analysis of the carcinogenic bacterial
RT   model pathogen Helicobacter felis.";
RL   Genome Biol. Evol. 3:302-308(2011).
CC   -!- FUNCTION: This protein is a component of the acetyl coenzyme A
CC       carboxylase complex; first, biotin carboxylase catalyzes the
CC       carboxylation of the carrier protein and then the transcarboxylase
CC       transfers the carboxyl group to form malonyl-CoA.
CC       {ECO:0000256|ARBA:ARBA00003761, ECO:0000256|RuleBase:RU365063}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] =
CC         ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate;
CC         Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145,
CC         ChEBI:CHEBI:456216; EC=6.3.4.14;
CC         Evidence={ECO:0000256|ARBA:ARBA00000861,
CC         ECO:0000256|RuleBase:RU365063};
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC       acetyl-CoA: step 1/1. {ECO:0000256|ARBA:ARBA00004956,
CC       ECO:0000256|RuleBase:RU365063}.
CC   -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer of biotin carboxyl
CC       carrier protein, biotin carboxylase and the two subunits of carboxyl
CC       transferase in a 2:2 complex. {ECO:0000256|ARBA:ARBA00011750,
CC       ECO:0000256|RuleBase:RU365063}.
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DR   EMBL; FQ670179; CBY82756.1; -; Genomic_DNA.
DR   RefSeq; WP_013469125.1; NC_014810.2.
DR   AlphaFoldDB; E7AAT5; -.
DR   STRING; 936155.HFELIS_06720; -.
DR   GeneID; 36133467; -.
DR   KEGG; hfe:HFELIS_06720; -.
DR   eggNOG; COG0439; Bacteria.
DR   HOGENOM; CLU_000395_3_2_7; -.
DR   OrthoDB; 9763189at2; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000007934; Chromosome.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR004549; Acetyl_CoA_COase_biotin_COase.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR005481; BC-like_N.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   NCBIfam; TIGR00514; accC; 1.
DR   PANTHER; PTHR48095:SF2; BIOTIN CARBOXYLASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR48095; PYRUVATE CARBOXYLASE SUBUNIT A; 1.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS00866; CPSASE_1; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Biotin {ECO:0000256|RuleBase:RU365063};
KW   Fatty acid biosynthesis {ECO:0000256|RuleBase:RU365063};
KW   Fatty acid metabolism {ECO:0000256|RuleBase:RU365063};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU365063};
KW   Lipid biosynthesis {ECO:0000256|RuleBase:RU365063};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU365063};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000007934}.
FT   DOMAIN          8..449
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          127..325
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   449 AA;  49541 MW;  DBFA035DF109B5F1 CRC64;
     MQAPKTKNLQ RILIANRGEI ALRAIQTIAE MGKQSIAIYS SADKDAHYLN TASAKVCIGG
     PKSTESYLNV PAIISAAELF EADAIFPGYG FLSENQNFVE ICSHHGIEFI GPDAKVMALM
     GDKSKAKAVM REAGVPVIEG SEGVLRGYEE ALKVAERIGF PIIIKAANGG GGRGMRVVED
     PSLLKNLYLA AETEALSAFG DGSVYIEKFI KDPKHIEVQI LADKHGNVLH IGERDCSTQR
     RQQKLIEETP AMVLDPCVRA RLLETATKAA KHIGYVGAGT FEFLLDGNGQ DFYFMEMNTR
     LQVEHTVSEM VSGLNFIEWM IRIAEGEKLP LQQDICLQGH SIECRITAED PQSFYPSAGT
     IKTWIAPGGI GVRLDTHVYA GYSVPTFYDS MIGKLIVHAP NRDQAILKMK RALKEFKVEG
     IKTTIPFHLN MLDNPDFRQN KIHTKYLEV
//

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