ID A0A0A1YE54_9PSED Unreviewed; 660 AA.
AC A0A0A1YE54;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=3-methylcrotonyl-CoA carboxylase {ECO:0000313|EMBL:KFX67985.1};
GN ORFNames=TMS3_0122530 {ECO:0000313|EMBL:KFX67985.1};
OS Pseudomonas taeanensis MS-3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1395571 {ECO:0000313|EMBL:KFX67985.1, ECO:0000313|Proteomes:UP000030063};
RN [1] {ECO:0000313|EMBL:KFX67985.1, ECO:0000313|Proteomes:UP000030063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS-3 {ECO:0000313|EMBL:KFX67985.1,
RC ECO:0000313|Proteomes:UP000030063};
RX PubMed=24407626;
RA Lee S.Y., Kim S.H., Lee D.G., Shin S., Yun S.H., Choi C.W., Chung Y.H.,
RA Choi J.S., Kahng H.Y., Kim S.I.;
RT "Draft Genome Sequence of Petroleum Oil-Degrading Marine Bacterium
RT Pseudomonas taeanensis Strain MS-3, Isolated from a Crude Oil-Contaminated
RT Seashore.";
RL Genome Announc. 2:0-0(2014).
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:KFX67985.1}.
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DR EMBL; AWSQ01000009; KFX67985.1; -; Genomic_DNA.
DR RefSeq; WP_025167451.1; NZ_AWSQ01000009.1.
DR AlphaFoldDB; A0A0A1YE54; -.
DR STRING; 1395571.TMS3_0122530; -.
DR eggNOG; COG4770; Bacteria.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000030063; Unassembled WGS sequence.
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; 3.30.470.20; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000030063}.
FT DOMAIN 3..448
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 122..319
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 582..658
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 660 AA; 71591 MW; 491B2B8DAC4BB3BB CRC64;
MPAFTKILIA NRGEIACRVI HTAHNLGYRT VAVYSQADAE SRHVQLADEA LCIGPAPVNQ
SYLLIDAIIA AARKTGADAI HPGYGFLSEN AEFARACQAA GIQFIGPSAE AIRLMGSKRL
SKIAMLQSGV PCIPGYEGAE QDDDTLSHEA ERIGYPLMIK ASAGGGGRGM RLVHHASELL
AQIRTARSEA QNAFGSGELI LERAVTQPRH VEIQVFGDQH GHMVYLGERD CSVQRRHQKV
VEEAPCPLMT PELRQAMGEA AVKAAASVDY VGAGTVEFLL DQSGAFYFLE MNTRLQVEHP
VTELVTGQDL VAWQIRVAEG QPLPLSQDEI RLSGHAIEVR LYAEDSSHDF MPQTGHVLRW
EPALLDGIRI DHGLIEGQAI TPFYDPMLAK IIAYGATRDE ARRKLVRAVE DCVLLGVKAN
QRFLANLLQH PEFAAGNATT AFIAEHFAAD PSLIPQPPSP AELASAAALL YQISAQSSAH
QTGLAGWRNA GNAPWRFLLK HGEQQFAVEL SVLEAGLQPR LDVKIGEQQL QLRLLGADGR
WATLELDGVR RRLAYQQSAS SVWLYGDNGN LELIDVSHVP ASAAVGTGSG MIKAPMDGAI
VEVLVEDGSK VSKGQLLLVL EAMKMEHPVK ASIDGIIRRV QVSKGDQVRN RQQLLEVQAE
//