ID A0A0D8CUG5_9GAMM Unreviewed; 669 AA.
AC A0A0D8CUG5;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=3-methylcrotonyl-CoA carboxylase {ECO:0000313|EMBL:KJE39885.1};
GN ORFNames=SG35_18200 {ECO:0000313|EMBL:KJE39885.1};
OS Thalassomonas actiniarum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Thalassomonas.
OX NCBI_TaxID=485447 {ECO:0000313|EMBL:KJE39885.1};
RN [1] {ECO:0000313|EMBL:KJE39885.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A5K-106 {ECO:0000313|EMBL:KJE39885.1};
RA Olonade I., van Zyl L.J., Tuffin M.I.;
RT "Genome sequence of Japanese sea anemone isolate Thalassomonas
RT actiniarum.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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:KJE39885.1}.
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DR EMBL; JYNI01000046; KJE39885.1; -; Genomic_DNA.
DR RefSeq; WP_044833892.1; NZ_CP059735.1.
DR AlphaFoldDB; A0A0D8CUG5; -.
DR STRING; 485447.SG35_18200; -.
DR PATRIC; fig|485447.4.peg.3708; -.
DR OrthoDB; 9763189at2; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.700.40; -; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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; 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 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 1..447
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 591..666
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 669 AA; 73642 MW; 01AFCD9A6F0FDDF9 CRC64;
MFTKILIANR GEIACRVIKT ARQMGILTVA VYSDADADSL HVNMADEAIY LGPSPSRESY
LLGEKVIEAA KRTGAQAIHP GYGFLSENAE FCRLCEKENI VFIGPPVAAI EAMGSKSAAK
NIMEQAKVPL VPGYHGDDQS TEVLKKAADD MGYPVLLKAT AGGGGKGMRQ VWSSEEFSEG
LAAAKREAKS SFGDDTMLVE KYLTQPRHVE IQVFCDNHGN AVYLFERDCS VQRRHQKVIE
EAPAPGMSED LRAAMGESAI KSAQAIGYQG AGTVEFLLDV DGSFYFMEMN TRLQVEHPVT
EFISGQDLVE WQLRVAAGEN LPKRQDELKI KGHAFEARIY AEDANNDFLP ATGTLDFLQP
PLESEHVRID TGVRQGDEVS VFYDPMIAKL IVWDENRDKA LQRLAKALAE YRINGVVTNI
DFLYNLATCP AFVEADLDTG FIDKHQADIF HESEQALADE LPMAALYLVL ANANNAKEQG
AKTNDPHSPW NTTNAWRLNE AHIHQLTLSH NDVEYPVTIE QKRQGSSSFY LIDVDGTKVD
CQGRIEGDML HSNINGYRSN ATIVHNQNQI SLFRQNGVFN FTQIFADCGD LDDQGDQGGL
CAPMNGTMVS VLVKAGDKVE KDQPLVIMEA MKMEHTIRAP GDGKVEAIYF NEGDMVDGGA
ELLAFAAEE
//
