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Database: UniProt
Entry: G7ZEQ9_AZOL4
LinkDB: G7ZEQ9_AZOL4
Original site: G7ZEQ9_AZOL4 
ID   G7ZEQ9_AZOL4            Unreviewed;       671 AA.
AC   G7ZEQ9;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   RecName: Full=propionyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00013050};
DE            EC=6.4.1.3 {ECO:0000256|ARBA:ARBA00013050};
GN   OrderedLocusNames=AZOLI_p30501 {ECO:0000313|EMBL:CBS90316.1};
OS   Azospirillum lipoferum (strain 4B).
OG   Plasmid AZO_p3 {ECO:0000313|EMBL:CBS90316.1,
OG   ECO:0000313|Proteomes:UP000005667}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=862719 {ECO:0000313|EMBL:CBS90316.1, ECO:0000313|Proteomes:UP000005667};
RN   [1] {ECO:0000313|Proteomes:UP000005667}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4B {ECO:0000313|Proteomes:UP000005667};
RC   PLASMID=Plasmid AZO_p3 {ECO:0000313|Proteomes:UP000005667};
RX   PubMed=22216014; DOI=10.1371/journal.pgen.1002430;
RA   Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G.,
RA   Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H., Robertson J.S.,
RA   Barbe V., Calteau A., Rouy Z., Mangenot S., Prigent-Combaret C.,
RA   Normand P., Boyer M., Siguier P., Dessaux Y., Elmerich C., Condemine G.,
RA   Krishnen G., Kennedy I., Paterson A.H., Gonzalez V., Mavingui P.,
RA   Zhulin I.B.;
RT   "Azospirillum genomes reveal transition of bacteria from aquatic to
RT   terrestrial environments.";
RL   PLoS Genet. 7:E1002430-E1002430(2011).
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; FQ311871; CBS90316.1; -; Genomic_DNA.
DR   RefSeq; WP_014249753.1; NC_016623.1.
DR   AlphaFoldDB; G7ZEQ9; -.
DR   KEGG; ali:AZOLI_p30501; -.
DR   HOGENOM; CLU_000395_3_1_5; -.
DR   OMA; MYYDSMI; -.
DR   OrthoDB; 9763189at2; -.
DR   UniPathway; UPA00945; UER00908.
DR   Proteomes; UP000005667; Plasmid AZO_p3.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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   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; 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   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:CBS90316.1};
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}; Plasmid {ECO:0000313|EMBL:CBS90316.1}.
FT   DOMAIN          1..447
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          120..317
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          592..671
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   671 AA;  73196 MW;  8D03A909C2370B1B CRC64;
     MFEKILIANR GEIACRVIRT ARRMGIKTVA VYSDADKNAL HVEMADEAVH IGAAPSAQSY
     LLVDRIVEAC KKTGAQAVHP GYGFLSEKRE FQEALAAAGI AFIGPDAHAI QAMGDKIESK
     KLAKEAGVST VPGYLGVIAD DEEAVTIARD IGYPVMIKAS AGGGGKGMRV AWNDEEAREG
     FRSATNEARS SFADDRVFVE KYIQQPRHIE IQLLADGQGT CLYLHERECS IQRRHQKVIE
     EAPSPFLDAA TRKAMGEQAV ALANAVQYKS AGTVEFIVDA ERNFYFLEMN TRLQVEHPVT
     ELITGLDLVE LMIRVAYGEK LTIRQEDVQL NGWAVEARVY AEDPFRNFLP STGRLTHYRP
     PAANPHVRVD TGVFEGGEIS MYYDPMIAKL CTWGSTRDAA IAGMREALDQ YYIRGVSHNI
     PFLASLMANQ RFVDGRLTTN FIAEEYPTGF HASDLPPEDP AVLIAVAAVI HRSLNDRDIQ
     ISGKMAGNKA KVRDDWVVVL DGTAHPVHLQ PAPLESTEGS PQRIGYMVDI AGKHHTVWSD
     WQIGEPLFRG SVNGTPVCVQ VDRVGIGYRL HHSGSQAIVK VLTPKAATLD ALMPVKAPPD
     MSKFLLSPMP GLLVSLAVTE GQEVKAGEVL AVVEAMKMEN ILRAAQDGTV AKIHAAPGSS
     LAVDQKIVEF A
//
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