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Database: UniProt
Entry: H1KHB8_METEX
LinkDB: H1KHB8_METEX
Original site: H1KHB8_METEX 
ID   H1KHB8_METEX            Unreviewed;       667 AA.
AC   H1KHB8;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=propionyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00013050};
DE            EC=6.4.1.3 {ECO:0000256|ARBA:ARBA00013050};
GN   ORFNames=MetexDRAFT_2030 {ECO:0000313|EMBL:EHP93070.1};
OS   Methylorubrum extorquens DSM 13060.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylorubrum.
OX   NCBI_TaxID=882800 {ECO:0000313|EMBL:EHP93070.1, ECO:0000313|Proteomes:UP000004382};
RN   [1] {ECO:0000313|EMBL:EHP93070.1, ECO:0000313|Proteomes:UP000004382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13060 {ECO:0000313|EMBL:EHP93070.1,
RC   ECO:0000313|Proteomes:UP000004382};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Land M.L., Hauser L., Koskimaki J., Halonen O., Pirttila A.,
RA   Frank C., Woyke T.J.;
RT   "The draft genome of Methylobacterium extorquens DSM 13060.";
RL   Submitted (SEP-2011) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHP93070.1}.
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DR   EMBL; AGJK01000041; EHP93070.1; -; Genomic_DNA.
DR   RefSeq; WP_003599287.1; NZ_AGJK01000041.1.
DR   AlphaFoldDB; H1KHB8; -.
DR   SMR; H1KHB8; -.
DR   PATRIC; fig|882800.3.peg.1991; -.
DR   UniPathway; UPA00945; UER00908.
DR   Proteomes; UP000004382; Unassembled WGS sequence.
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:EHP93070.1};
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}.
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          592..667
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   667 AA;  71903 MW;  AD197C37635F0D41 CRC64;
     MFDKILIANR GEIACRIIKT AQKMGIKTVA VYSDADRDAV HVAMADEAVH IGPAPAAQSY
     LLIEKIIDAC KQTGAQAVHP GYGFLSERES FPKALAEAGI VFIGPNPGAI AAMGDKIESK
     KAAAAAEVST VPGFLGVIES PEHAVTIADE IGYPVMIKAS AGGGGKGMRI AESADEVAEG
     FARAKSEASS SFGDDRVFVE KFITDPRHIE IQVIGDKHGN VIYLGERECS IQRRNQKVIE
     EAPSPLLDEE TRRKMGEQAV ALAKAVNYDS AGTVEFVAGQ DKSFYFLEMN TRLQVEHPVT
     EMITGLDLVE LMIRVAAGEK LPLSQDQVKL DGWAVESRVY AEDPTRNFLP SIGRLTTYQP
     PEEGPLGGAI VRNDTGVEEG GEIAIHYDPM IAKLVTWAPT RLEAIEAQAT ALDAFAIEGI
     RHNIPFLATL MAHPRWRDGR LSTGFIKEEF PEGFIAPEPE GPVAHRLAAV AAAIDHKLNI
     RKRGISGQMR DPSLLTFQRE RVVVLSGQRF NVTVDPDGDD LLVTFDDGTT APVRSAWRPG
     APVWSGTVGD QSVAIQVRPL LNGVFLQHAG AAAEARVFTR REAELADLMP VKENAGSGKQ
     LLCPMPGLVK QIMVSEGQEV KNGEPLAIVE AMKMENVLRA ERDGTISKIA AKEGDSLAVD
     AVILEFA
//
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