ID F6YR02_CIOIN Unreviewed; 723 AA.
AC F6YR02;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 2.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial {ECO:0008006|Google:ProtNLM};
OS Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC Cionidae; Ciona.
OX NCBI_TaxID=7719 {ECO:0000313|Ensembl:ENSCINP00000007911.3, ECO:0000313|Proteomes:UP000008144};
RN [1] {ECO:0000313|Proteomes:UP000008144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12481130; DOI=10.1126/science.1080049;
RA Dehal P., Satou Y., Campbell R.K., Chapman J., Degnan B., De Tomaso A.,
RA Davidson B., Di Gregorio A., Gelpke M., Goodstein D.M., Harafuji N.,
RA Hastings K.E., Ho I., Hotta K., Huang W., Kawashima T., Lemaire P.,
RA Martinez D., Meinertzhagen I.A., Necula S., Nonaka M., Putnam N., Rash S.,
RA Saiga H., Satake M., Terry A., Yamada L., Wang H.G., Awazu S., Azumi K.,
RA Boore J., Branno M., Chin-Bow S., DeSantis R., Doyle S., Francino P.,
RA Keys D.N., Haga S., Hayashi H., Hino K., Imai K.S., Inaba K., Kano S.,
RA Kobayashi K., Kobayashi M., Lee B.I., Makabe K.W., Manohar C., Matassi G.,
RA Medina M., Mochizuki Y., Mount S., Morishita T., Miura S., Nakayama A.,
RA Nishizaka S., Nomoto H., Ohta F., Oishi K., Rigoutsos I., Sano M.,
RA Sasaki A., Sasakura Y., Shoguchi E., Shin-i T., Spagnuolo A., Stainier D.,
RA Suzuki M.M., Tassy O., Takatori N., Tokuoka M., Yagi K., Yoshizaki F.,
RA Wada S., Zhang C., Hyatt P.D., Larimer F., Detter C., Doggett N.,
RA Glavina T., Hawkins T., Richardson P., Lucas S., Kohara Y., Levine M.,
RA Satoh N., Rokhsar D.S.;
RT "The draft genome of Ciona intestinalis: insights into chordate and
RT vertebrate origins.";
RL Science 298:2157-2167(2002).
RN [2] {ECO:0000313|Ensembl:ENSCINP00000007911.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; EAAA01002537; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; EAAA01002538; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; F6YR02; -.
DR STRING; 7719.ENSCINP00000007911; -.
DR Ensembl; ENSCINT00000007911.3; ENSCINP00000007911.3; ENSCING00000019260.1.
DR GeneTree; ENSGT00940000156941; -.
DR HOGENOM; CLU_000395_3_1_1; -.
DR InParanoid; F6YR02; -.
DR OMA; TGFYDRH; -.
DR TreeFam; TF105650; -.
DR Proteomes; UP000008144; Chromosome 7.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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; 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:UP000008144}.
FT DOMAIN 49..494
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 165..362
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 642..717
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 723 AA; 79691 MW; C07063084F517E1F CRC64;
MLQITRTAIF SRFRWRRVRN SAECVNFVPN YRRYSSHPVE INENVKETQI SKLLIANRGE
IACRVMKTAK NMGISTVAVY SEVDRSQMHV QMADEAFCIG DEQGYLGMDG ILNVAKDSGA
EAIHPGYGFL SENAEFAELC SSNGVIFVGP PPSAIRDMGI KSTSKRIMSA ANVPIIEGYH
GEEQSDSRLL EEAHGIGFPV MIKAVRGGGG KGMRIATSRD VFLEQLSSAR SEAIKSFGDD
VMLVEKYVDR PRHVEVQVFG DHHGNAVHLF ERDCSVQRRH QKVIEESPAP GISLRTRTNL
GEAAVRAARA VGYVGAGTVE FVMDPQQNFY FMEMNTRLQV EHPVTEMVTG TDLVEWQLLV
AQGHPIPSTQ QEIFDRTRGH AFEARIYAED PDDDFMPRAG PLIHLSAPKV TPNTRVETGV
RQGDVVSHYY DPMIAKLVVW GKDRGSALRG LVRGLGEYSV VGLDTNIKFL QRLALHPSFK
AGDVHTGFIE QHNEALFPDK PTEISPHAAC RAALGYLLLE ETPNTQDPFV DCSNFQVNIP
SPRTIELTVG DCDVIVGITP LSDGKYSMNV NGDVTNENND MIVSGSLTKD IMTSSMNLKT
TIDDITTSEK MVFIPDSIHL YPTNGEESLK FSLPLPKYLS EFAASGVSGD PMAPMVGEIQ
KVLVTPGEEV AQGQPLVVMI AMKMEHTIRS PRDGVVESVH VAAKDNVARF DVLVKLVQAF
NEQ
//
