ID A0A0P1F7T4_THAGE Unreviewed; 682 AA.
AC A0A0P1F7T4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=propionyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00013050};
DE EC=6.4.1.3 {ECO:0000256|ARBA:ARBA00013050};
GN Name=accA1_1 {ECO:0000313|EMBL:CUH64079.1};
GN ORFNames=TG4357_01056 {ECO:0000313|EMBL:CUH64079.1};
OS Thalassovita gelatinovora (Thalassobius gelatinovorus).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Thalassovita.
OX NCBI_TaxID=53501 {ECO:0000313|EMBL:CUH64079.1, ECO:0000313|Proteomes:UP000051587};
RN [1] {ECO:0000313|EMBL:CUH64079.1, ECO:0000313|Proteomes:UP000051587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 4357 {ECO:0000313|EMBL:CUH64079.1,
RC ECO:0000313|Proteomes:UP000051587};
RG Swine Surveillance;
RL Submitted (SEP-2015) 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; CYSA01000015; CUH64079.1; -; Genomic_DNA.
DR RefSeq; WP_058261829.1; NZ_FOFW01000009.1.
DR AlphaFoldDB; A0A0P1F7T4; -.
DR STRING; 53501.SAMN04488043_10997; -.
DR OrthoDB; 9763189at2; -.
DR UniPathway; UPA00945; UER00908.
DR Proteomes; UP000051587; 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:UP000051587}.
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 603..682
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 682 AA; 74354 MW; D982A264F622718B CRC64;
MFNKILIANR GEIACRVIKT ARKMGIQTVA IYSDADKQAL HVQMADEAVH IGPPPANQSY
IVIDKVMEAI RASGAQAVHP GYGFLSENSK FAQELEAAGV AFVGPPVGAI EAMGDKITSK
KIAQEAGVST VPGYMGLIED AEDAVKISNQ VGYPVMIKAS AGGGGKGMRI AWNDEEAREG
FQSSKNEAAN SFGDDRIFIE KFVTQPRHIE IQVLCDTHGN GVYLGERECS IQRRNQKVVE
EAPSPFLDEA TRKAMGEQAV ALAQAVGYAS AGTVEFIVDG NKNFYFLEMN TRLQVEHPVT
ELITGVDLVE QMIRVAAGEK LTMTQDDVKL TGWAIENRLY AEDPYRNFLP SIGRLTRYRP
PVEMAAGPLL TNDKWQGEAA AGAHAVRNDT GVYEGGEISM YYDPMIAKLC TWAPTRAEAI
EAMRNALDGF EVEGIGHNLP FLSAVMDHPI FMAGEMTTAF IAEQYPDGFD GVELPGDTLR
RIAAAAAAMH RVAEIRRTRV SGRMDNHERR VGTEWVVTLQ GQDFPVHIDA DHDGSTVKFE
DGGSLRVASD WTPGDQLAEI TFDGHEGLVL KVGKISGGFR IRSRGADLKV HVRSARQAEL
ARLMPEKLPP DTSKMLLCPM PGLIVKINVE EGEEVQEGQA LCTVEAMKME NILRAEKKAV
VKKINAAPGD SLAVDEVIIE FE
//
