ID A0A1M6AQI3_9RHOB Unreviewed; 681 AA.
AC A0A1M6AQI3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=propionyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00013050};
DE EC=6.4.1.3 {ECO:0000256|ARBA:ARBA00013050};
GN ORFNames=SAMN05444417_0565 {ECO:0000313|EMBL:SHI38681.1};
OS Wenxinia saemankumensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Wenxinia.
OX NCBI_TaxID=1447782 {ECO:0000313|EMBL:SHI38681.1, ECO:0000313|Proteomes:UP000184292};
RN [1] {ECO:0000313|EMBL:SHI38681.1, ECO:0000313|Proteomes:UP000184292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100565 {ECO:0000313|EMBL:SHI38681.1,
RC ECO:0000313|Proteomes:UP000184292};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FQYO01000001; SHI38681.1; -; Genomic_DNA.
DR RefSeq; WP_073326280.1; NZ_FQYO01000001.1.
DR AlphaFoldDB; A0A1M6AQI3; -.
DR STRING; 1447782.SAMN05444417_0565; -.
DR OrthoDB; 9763189at2; -.
DR UniPathway; UPA00945; UER00908.
DR Proteomes; UP000184292; 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; cd00945; Aldolase_Class_I; 1.
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:UP000184292}.
FT DOMAIN 1..466
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 605..681
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 681 AA; 73137 MW; D0B0B74A665CDFA1 CRC64;
MIRKLLIANR GEIACRVIRT ARRMGIATVA VHSEADAGAL HVRLADEAVA IGPAPAAQSY
IAIDRVMEAI RASGADAVHP GYGFLSENPR FAEALQAEGI AFVGPPVKAI EAMGDKITSK
KIAAEAGVST VPGYMGLIGD ADEAARIAGE IGYPVMIKAS AGGGGKGMRI AWDEAEAREG
FESSRSEAAS SFGDDRIFIE KFVTQPRHIE IQVLADTHGT CLYLGERECS IQRRNQKVVE
EAPSPFLDAA TRKAMGEQAV ALAQAVGYAS AGTVEFIVDG DRNFYFLEMN TRLQVEHPVT
ELVTGIDLVE QMIRVAAGER LSFGQEDVRL TGWAIENRLY AEDPYRGFLP SIGRLTRYRP
PAERAAGPML DAGTWHGEAG TGETAIRNDT GVFEGGEISM FYDPMIAKLC SWGPDRASAI
ETMRGALDAF EVEGIGHNLP FLAAVMDHPR FVSGELTTAF IAEEWPDGFD GVALPEGELR
RVAAAAAAMN RVAEIRRTRV SGRLGNHERK VGDDWVVVID RAEWPVRVAA GPGGADVTFD
GGVTLRVEGD WTPGQSLARL VVDGAPLVLK VGKATGGFRL RSRGADLRVH VYTPRQAELA
RLMPEKIAPD TSRQLLCPMP GMLVKLNVGP GDEVQEGQAL CIVEAMKMEN MLRAERQGVV
AAVNAAPGDS LAVDEVILEF E
//
