ID A0A2V4NFW4_9RHOB Unreviewed; 681 AA.
AC A0A2V4NFW4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=propionyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00013050};
DE EC=6.4.1.3 {ECO:0000256|ARBA:ARBA00013050};
GN ORFNames=DI396_02005 {ECO:0000313|EMBL:PYC48880.1};
OS Litorivita pollutaquae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Litorivita.
OX NCBI_TaxID=2200892 {ECO:0000313|EMBL:PYC48880.1, ECO:0000313|Proteomes:UP000248012};
RN [1] {ECO:0000313|EMBL:PYC48880.1, ECO:0000313|Proteomes:UP000248012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSX-11 {ECO:0000313|EMBL:PYC48880.1,
RC ECO:0000313|Proteomes:UP000248012};
RA Hetharua B.H., Min D., Liao H., Tian Y.;
RT "Oceanovita maritima gen. nov., sp. nov., a marine bacterium in the family
RT Rhodobacteraceae isolated from surface seawater of Lundu port Xiamen,
RT China.";
RL Submitted (MAY-2018) 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:PYC48880.1}.
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DR EMBL; QFVT01000002; PYC48880.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V4NFW4; -.
DR OrthoDB; 9763189at2; -.
DR UniPathway; UPA00945; UER00908.
DR Proteomes; UP000248012; 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};
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:UP000248012}.
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; 74022 MW; 7F4E0B6CFDA761E6 CRC64;
MFKKILIANR GEIACRVIKT ARKMGIQTVA VYSDADKNAL HVSMADEAYH IGPPPANQSY
IVIDKIMEAI KATGAEAVHP GYGFLSENSK FAEALSAAGV AFIGPPVGAI EAMGDKITSK
KLAQEANVST VPGFMGLIDD AEHAVKISNE VGYPVMIKAS AGGGGKGMRI AWNDDEAREG
FQSSKNEAAN SFGDDRIFIE KFVTQPRHIE IQVLCDSHGN GIYLGERECS IQRRNQKVVE
EAPSPFLDEA TRKAMGEQAV ALAQAVDYAS AGTVEFIVDG ARNFYFLEMN TRLQVEHPVT
ELITGVDLVE QMIRVAYGEK LTMTQDDVKL TGWAIENRLY AEDPYRGFLP SIGRLSRYRP
PAEQASGPLL ENDKWQGDAP AGTVAVRNDT GVFEGGEISM YYDPMIAKLC TWAPTREAAI
EAMRNALDGF EVEGIGHNLP FLSAVMDHPI FIKGEMTTAF IEEEYPEGFE GVELPDEALR
KIAASCAAMH RVAEIRRTRV SGRMDNHERH VGENWVVSVQ GQSYPVTVAA DHDGSTVTFE
DGTALRVAST WTPGDQLATI TVDGEGLVLK VGKVSGGFRI RSRGADLKVH VRSPRQAELA
ALMPEKVAPD TSKLLLCPMP GLVVKVDVEV GDEVQEGQAL CTIEAMKMEN ILRAEKKSVV
TKINAVAGDS LAVDEVIMEF E
//
