ID A1K3A0_AZOSB Unreviewed; 668 AA.
AC A1K3A0;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 24-JAN-2024, entry version 98.
DE RecName: Full=Biotin carboxylase {ECO:0000256|ARBA:ARBA00017242};
DE EC=6.4.1.3 {ECO:0000256|ARBA:ARBA00013050};
DE AltName: Full=Acetyl-coenzyme A carboxylase biotin carboxylase subunit A {ECO:0000256|ARBA:ARBA00033786};
GN Name=pccA {ECO:0000313|EMBL:CAL93305.1};
GN OrderedLocusNames=azo0688 {ECO:0000313|EMBL:CAL93305.1};
OS Azoarcus sp. (strain BH72).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Azoarcus.
OX NCBI_TaxID=418699 {ECO:0000313|EMBL:CAL93305.1, ECO:0000313|Proteomes:UP000002588};
RN [1] {ECO:0000313|EMBL:CAL93305.1, ECO:0000313|Proteomes:UP000002588}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BH72 {ECO:0000313|EMBL:CAL93305.1,
RC ECO:0000313|Proteomes:UP000002588};
RX PubMed=17057704; DOI=10.1038/nbt1243;
RA Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J.,
RA Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C.,
RA Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J.,
RA Weidner S., Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.;
RT "Complete genome of the mutualistic, N2-fixing grass endophyte Azoarcus sp.
RT strain BH72.";
RL Nat. Biotechnol. 24:1385-1391(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + hydrogencarbonate + propanoyl-CoA = (S)-methylmalonyl-
CC CoA + ADP + H(+) + phosphate; Xref=Rhea:RHEA:23720,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57327, ChEBI:CHEBI:57392,
CC ChEBI:CHEBI:456216; EC=6.4.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00000634};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23721;
CC Evidence={ECO:0000256|ARBA:ARBA00000634};
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
CC -!- PATHWAY: Metabolic intermediate metabolism; propanoyl-CoA degradation;
CC succinyl-CoA from propanoyl-CoA: step 1/3.
CC {ECO:0000256|ARBA:ARBA00005060}.
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DR EMBL; AM406670; CAL93305.1; -; Genomic_DNA.
DR RefSeq; WP_011764423.1; NZ_CP016210.1.
DR AlphaFoldDB; A1K3A0; -.
DR STRING; 62928.azo0688; -.
DR KEGG; aoa:dqs_0758; -.
DR KEGG; azo:azo0688; -.
DR eggNOG; COG4770; Bacteria.
DR HOGENOM; CLU_000395_3_1_4; -.
DR OMA; MYYDSMI; -.
DR OrthoDB; 9803706at2; -.
DR UniPathway; UPA00655; UER00711.
DR UniPathway; UPA00945; UER00908.
DR Proteomes; UP000002588; 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:0004658; F:propionyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.700.30; -; 1.
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; IPR001882; Biotin_BS.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR041265; PCC_BT.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR NCBIfam; TIGR00514; accC; 1.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR Pfam; PF18140; PCC_BT; 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 SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 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|ARBA:ARBA00023267};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:CAL93305.1};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000002588}.
FT DOMAIN 1..449
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..318
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 589..668
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 668 AA; 73370 MW; 2207E7F61BE24B8C CRC64;
MFTKILIANR GEIACRVIKT ARKMGIKTVA VYSEADKDAL HVDLADEAVC IGPAPSKDSY
LVMDRIIAAC KQTGAEAVHP GYGFLSENAE FSRRLEEEGI KFIGPKHYSV AKMGDKIESK
KLAIEAKVNT IPGYNDAIAG PAEAVEIAKK IGYPVMIKAS AGGGGKGLRV AYNDEQAFEG
FSSCVNEARN SFGDDRVFIE KYVLEPRHIE IQVLGDSHGN YVYLNERDCS IQRRHQKVIE
EAPSPFVDAE MRKAMGEQAV ALARAVNYES AGTVEFVVSG ATKEFYFLEM NTRLQVEHPV
TELITGLDLV EQMIRVAAGE KLPLSQADVK INGWAMECRI NAEDPFRGFL PSTGRLVRFQ
PPAEVDGQVR VDTGVYDGGE ISMFYDSMIA KLIVHGATRD QAIGRMRDAL NAFVIRGISS
NIPFQAALMQ HPRFCSGNFN TGFIAEEFPK GFDASMVPHD DPALLAAVAA YVHRSYIDRA
ARVSGQLPGH ERAVGNEWVV IRLGTDNQNE LLPVTATPVA GGYAVTLNGE TYTIKSDWQL
GQALFNGTCN GNEFTLQVER HKMRYRLFHW GTQADFLVMS KRAAELQSLM PVKLPPDLSK
FLLSPMPGLL REVSVSEGQE VKAGEKLAVI EAMKMENLLK AEQDGKVKKV VIKPGASLAV
DDVIIEFE
//