ID A0A099TC57_9RHOB Unreviewed; 658 AA.
AC A0A099TC57;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=3-methylcrotonyl-CoA carboxylase {ECO:0000313|EMBL:KGL02668.1};
GN ORFNames=PM04_01380 {ECO:0000313|EMBL:KGL02668.1};
OS Thalassobacter sp. 16PALIMAR09.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Thalassobacter.
OX NCBI_TaxID=1225651 {ECO:0000313|EMBL:KGL02668.1, ECO:0000313|Proteomes:UP000029829};
RN [1] {ECO:0000313|EMBL:KGL02668.1, ECO:0000313|Proteomes:UP000029829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16PALIMAR09 {ECO:0000313|EMBL:KGL02668.1,
RC ECO:0000313|Proteomes:UP000029829};
RA Mas-Llado M., Nogales B., Bosch R.;
RT "Draft genome sequence of Thalassobacter sp. 16PALIMAR09.";
RL Submitted (MAR-2014) 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:KGL02668.1}.
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DR EMBL; JHAK01000001; KGL02668.1; -; Genomic_DNA.
DR RefSeq; WP_038002903.1; NZ_JHAK01000001.1.
DR AlphaFoldDB; A0A099TC57; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000029829; 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; 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:UP000029829}.
FT DOMAIN 2..457
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 121..323
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 575..653
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 658 AA; 70479 MW; 4EDD5A7E44FDFB2D CRC64;
MGIKKLLIAN RGEIACRVIS TARRMGIRTV AVYSDADRDA QHVRMADETA YIGPSAAQES
YLNIDSLIAA IRLTGADAVH PGYGFLSENA AFVEAVEGAG AVFVGPPASA IRAMGLKDAA
KALMAEAGVP VVPGYHGADQ SPEVLAQQAA EIGYPVMIKA RAGGGGKGMR HVTRPEDFLQ
ALEGAQREGE ASFGDPSVLI EKFITHPRHI EVQVFADSHG NFVHLYERDC SLQRRHQKVI
EEAPAPGMTP ELRAHLGDIA LRAARAVNYV GAGTVEFIVD GSGLLRADGC WFMEMNTRLQ
VEHPVTEAIT GIDLVEWQLN VAAGLPLPLA QADIPLRGHA MEARIYAEDV PKGFLPATGR
CSQVAFPSGA SFAHGDIRID SGVAQGDEIS AWYDPMIAKL ITHGDTREAA LSRLTQALED
TRIVGPTTNV TFLHQLASLS TFETGAVHTG LIENHLDALT QESEPDAASW ALAALTMLDL
LHAQPLRGWR AWGQARYVCQ LAHGDQSVEI GVTDAGESRY IVDESRYIVE MRDDARILVS
QDGGPGRSYC VHRDKETVTV FSQSKAFVFK RRPQGGQAEA AAGDGRIMAP MPGVIKAVSC
AVGDHVEAGT PLIVMEAMKM EHTLVAPKDG VISSVTVVPG AQVSDNAVLI EFEETQDD
//
