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Database: UniProt
Entry: A7IPJ9_XANP2
LinkDB: A7IPJ9_XANP2
Original site: A7IPJ9_XANP2 
ID   A7IPJ9_XANP2            Unreviewed;       675 AA.
AC   A7IPJ9;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   24-JAN-2024, entry version 88.
DE   RecName: Full=propionyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00013050};
DE            EC=6.4.1.3 {ECO:0000256|ARBA:ARBA00013050};
GN   OrderedLocusNames=Xaut_4726 {ECO:0000313|EMBL:ABS69945.1};
OS   Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Xanthobacteraceae; Xanthobacter.
OX   NCBI_TaxID=78245 {ECO:0000313|EMBL:ABS69945.1, ECO:0000313|Proteomes:UP000002417};
RN   [1] {ECO:0000313|EMBL:ABS69945.1, ECO:0000313|Proteomes:UP000002417}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1158 / Py2 {ECO:0000313|Proteomes:UP000002417};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA   Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Tapia R., Brainard J., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Ensigns S.A., Richardson P.;
RT   "Complete sequence of chromosome of Xanthobacter autotrophicus Py2.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000781; ABS69945.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7IPJ9; -.
DR   STRING; 78245.Xaut_4726; -.
DR   KEGG; xau:Xaut_4726; -.
DR   eggNOG; COG4770; Bacteria.
DR   HOGENOM; CLU_000395_3_3_5; -.
DR   OMA; MYYDSMI; -.
DR   OrthoDB; 9763189at2; -.
DR   PhylomeDB; A7IPJ9; -.
DR   UniPathway; UPA00945; UER00908.
DR   Proteomes; UP000002417; Chromosome.
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};
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:UP000002417}.
FT   DOMAIN          1..451
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          600..675
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   675 AA;  72656 MW;  71AC4C2CDE199308 CRC64;
     MFSKILIANR GEIACRVIKT ARKMGIKTVA VYSDADKDAL HVEMADEAVH IGPPQAAQSY
     LIAEKIVEAC KLTGAEAVHP GYGFLSERAS FPKLLAEHGI VFIGPNPHAI DAMGDKIESK
     KAAAAAHVST VPGYLGVLEN GTEAAKIADE IGYPVMIKAS AGGGGKGMRI AYSRDEVQDG
     FDRAKSEAKS SFGDDRVFVE KFIVDPRHIE IQVLGDKHGN VIYLGERECS IQRRNQKVVE
     EAPSPLLDEA TRKKMGEQAV ALAKAVGYDS AGTVEFVAGQ DKSFYFLEMN TRLQVEHPVT
     ELITGIDLVE QMIRVAAGEP LSITQDDVKL TGWAVESRIY AEDPYRNFLP STGRLVRYRP
     PAEGKDGPIT VRNDTGVYEG GEISIFYDPM IAKLVTHAPT RAIAIEAQAD ALDAFAIDGI
     GHNIPFLSAL MSHPRWRDGR LSTGFIAEEY PDGFHARAPE GELVHTLSAV AAVIDHIHNA
     RKRHISGQTS GVPVAFAKRR IVHLSAAEET LSTACEVEAV DGGYKVQIFD ADGTAGHTHL
     LRSTWKPGDV VWTGTIDADQ VAVQVRTIPN GYLLAHRGIA TKARVYTELS ASLAALMPKK
     ETAGGGKELL CPMPGLVVSI AVTPGQEVKN GEILAIVEAM KMENVLRAER DGVIKAVHAK
     AGDSLAVDAV ILEFA
//
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